U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

GORASP1 golgi reassembly stacking protein 1 [ Homo sapiens (human) ]

Gene ID: 64689, updated on 2-Nov-2024

Summary

Go to the top of the page Help
Official Symbol
GORASP1provided by HGNC
Official Full Name
golgi reassembly stacking protein 1provided by HGNC
Primary source
HGNC:HGNC:16769
See related
Ensembl:ENSG00000114745 MIM:606867; AllianceGenome:HGNC:16769
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
P65; GOLPH5; GRASP65
Summary
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is a membrane protein involved in establishing the stacked structure of the Golgi apparatus. It is a caspase-3 substrate, and cleavage of this encoded protein contributes to Golgi fragmentation in apoptosis. This encoded protein can form a complex with the Golgi matrix protein GOLGA2, and this complex binds to the vesicle docking protein p115. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jul 2013]
Expression
Ubiquitous expression in testis (RPKM 12.9), brain (RPKM 12.1) and 25 other tissues See more
Orthologs
mouse all
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See GORASP1 in Genome Data Viewer
Location:
3p22.2
Exon count:
11
Annotation release Status Assembly Chr Location
RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 3 NC_000003.12 (39096599..39107627, complement)
RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 3 NC_060927.1 (39108763..39119791, complement)
RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 3 NC_000003.11 (39138090..39149118, complement)

Chromosome 3 - NC_000003.12Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC107986042 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 14215 Neighboring gene NANOG-H3K4me1 hESC enhancer GRCh37_chr3:38877996-38878572 Neighboring gene CDK7 strongly-dependent group 2 enhancer GRCh37_chr3:38912374-38913573 Neighboring gene sodium voltage-gated channel alpha subunit 11 Neighboring gene NANOG hESC enhancer GRCh37_chr3:39020389-39020890 Neighboring gene RNA, U6 small nuclear 1227, pseudogene Neighboring gene H3K27ac hESC enhancer GRCh37_chr3:39092668-39093540 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 14216 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 19690 Neighboring gene WD repeat domain 48 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr3:39144473-39144972 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 14217 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 14218 Neighboring gene ReSE screen-validated silencer GRCh37_chr3:39166834-39167009 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr3:39177733-39178638 Neighboring gene tetratricopeptide repeat domain 21A Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr3:39187593-39188286 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr3:39188287-39188980 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 14219 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 19693 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr3:39193407-39194267 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr3:39194268-39195127 Neighboring gene uncharacterized LOC101928263 Neighboring gene H3K27ac hESC enhancer GRCh37_chr3:39195907-39196406 Neighboring gene microRNA 6822 Neighboring gene cysteine and serine rich nuclear protein 1

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help
  • Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network. Sengupta D, et al. J Cell Biol, 2009 Jul 13. PMID 19581411, Free PMC Article
  2. Caspase cleavage of the Golgi stacking factor GRASP65 is required for Fas/CD95-mediated apoptosis. Cheng JP, et al. Cell Death Dis, 2010 Oct 7. PMID 21368855, Free PMC Article
  3. Mena-GRASP65 interaction couples actin polymerization to Golgi ribbon linking. Tang D, et al. Mol Biol Cell, 2016 Jan 1. PMID 26538023, Free PMC Article
  4. Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2. Lin CY, et al. Proc Natl Acad Sci U S A, 2000 Nov 7. PMID 11050165, Free PMC Article
  5. The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division. Sütterlin C, et al. Mol Biol Cell, 2005 Jul. PMID 15888544, Free PMC Article

See all (75) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. GRASP depletion-mediated Golgi fragmentation impairs glycosaminoglycan synthesis, sulfation, and secretion.
    Title: GRASP depletion-mediated Golgi fragmentation impairs glycosaminoglycan synthesis, sulfation, and secretion.
  2. Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure.
    Title: Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure.
  3. Biophysical characterization of intrinsically disordered human Golgi matrix protein GRASP65.
    Title: Biophysical characterization of intrinsically disordered human Golgi matrix protein GRASP65.
  4. Markers of malignant prostate cancer cells: Golgi localization of alpha-mannosidase 1A at GM130-GRASP65 site and appearance of high mannose N-glycans on cell surface.
    Title: Markers of malignant prostate cancer cells: Golgi localization of α-mannosidase 1A at GM130-GRASP65 site and appearance of high mannose N-glycans on cell surface.
  5. GRASP65 modulates Golgi structure and microtubule organization during cell division.
    Title: GRASP65 controls Golgi position and structure during G2/M transition by regulating the stability of microtubules.
  6. DjA1 interacts with GRASP65 to enhance Golgi structure formation through the promotion of GRASP65 trans-oligomerization.
    Title: DjA1 maintains Golgi integrity via interaction with GRASP65.
  7. In situ proximity ligation assays of Golgi localization of alpha-mannosidase IA at giantin versus GM130-GRASP65 site, and absence or presence of N-glycans terminated with alpha3-mannose on trans-Golgi glycosyltransferases may be useful for distinguishing indolent from aggressive prostate cancer cells.
    Title: Shifted Golgi targeting of glycosyltransferases and α-mannosidase IA from giantin to GM130-GRASP65 results in formation of high mannose N-glycans in aggressive prostate cancer cells.
  8. Results demonstrate a critical role for GRASP55 and GRASP65 in maintaining the stacked structure of the Golgi, which is required for accurate posttranslational modifications in the Golgi. Additionally, the GRASP knockout cell lines developed in this study will be useful tools for studying the role of GRASP proteins in other important cellular processes.
    Title: Knockout of the Golgi stacking proteins GRASP55 and GRASP65 impairs Golgi structure and function.
  9. The authors determined that Golgi membrane ribbon fragmentation increased during the early cytoplasmic phase of cytomegalovirus virion assembly and that Golgi membrane fragmentation in infected cells was dependent on the phosphorylation of an integral cis-Golgi protein, Grasp65.
    Title: Phosphorylation of Golgi Peripheral Membrane Protein Grasp65 Is an Integral Step in the Formation of the Human Cytomegalovirus Cytoplasmic Assembly Compartment.
  10. In cells, Mena and actin were required for Golgi ribbon formation after nocodazole washout; in vitro, Mena and microfilaments enhanced GRASP65 oligomerization and Golgi membrane fusion. Thus Mena interacts with GRASP65 to promote local actin polymerization, which facilitates Golgi ribbon linking.
    Title: Mena-GRASP65 interaction couples actin polymerization to Golgi ribbon linking.
Submit: New GeneRIF Correction See all GeneRIFs (27)

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
Variability in the common genetic architecture of social-communication spectrum phenotypes during childhood and adolescence.
EBI GWAS Catalog

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Genotypes

HIV-1 interactions

Go to the top of the page Help

Protein interactions

Protein Gene Interaction Pubs
Nef nef HIV-1 Nef causes the FMS N-glycosylation defect and induces relocalization of the GM130 by activating the p56Hck/MEK/ERK/GRASP65 phosphorylation cascade in the Golgi PubMed

Go to the HIV-1, Human Interaction Database

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Markers

Homology

Clone Names

  • FLJ23443, MGC118894, MGC118897

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in Golgi organization IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in Golgi organization ISS
Inferred from Sequence or Structural Similarity
more info
  
involved_in Golgi organization NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in Golgi ribbon formation IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in establishment of protein localization to plasma membrane IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in negative regulation of dendrite morphogenesis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein N-linked glycosylation IEA
Inferred from Electronic Annotation
more info
  
involved_in protein transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in Golgi apparatus IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in Golgi apparatus IDA
Inferred from Direct Assay
more info
 PubMed 
located_in Golgi membrane TAS
Traceable Author Statement
more info
  
located_in cis-Golgi network NAS
Non-traceable Author Statement
more info
 PubMed 
located_in endoplasmic reticulum-Golgi intermediate compartment membrane TAS
Traceable Author Statement
more info
  

General protein information

Go to the top of the page Help
Preferred Names
Golgi reassembly-stacking protein 1
Names
Golgi peripheral membrane protein p65
Golgi phosphoprotein 5
Golgi reassembly and stacking protein 1
golgi reassembly stacking protein 1, 65kDa
golgi reassembly-stacking protein of 65 kDa

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001278789.2 → NP_001265718.1  Golgi reassembly-stacking protein 1 isoform 2

    See identical proteins and their annotated locations for NP_001265718.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) lacks two alternate in-frame exons in the 5' coding region, compared to variant 1. It encodes isoform 2, which lacks an internal segment and is shorter than isoform 1.
    Source sequence(s)
    AI824080, AK001574, AK057043, AK124755, AK303847
    Consensus CDS
    CCDS63597.1
    UniProtKB/TrEMBL
    B4E1H8
    Related
    ENSP00000419123.1, ENST00000479927.6
    Conserved Domains (2) summary
    cl00117
    Location:3 → 110
    PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...
    cl27544
    Location:99 → 203
    Herpes_glycop_D; Herpesvirus glycoprotein D/GG/GX domain

  2. NM_001278790.2 → NP_001265719.1  Golgi reassembly-stacking protein 1 isoform 3

    See identical proteins and their annotated locations for NP_001265719.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) lacks three alternate exons and uses an alternate splice site in the 5' coding region, compared to variant 1. It encodes isoform 3, which lacks two internal segments and is shorter than isoform 1.
    Source sequence(s)
    AI824080, AK057043, BC008928
    Consensus CDS
    CCDS63596.1
    UniProtKB/TrEMBL
    B3KPY8
    Related
    ENSP00000395709.2, ENST00000422110.7
    Conserved Domains (1) summary
    cl00117
    Location:3 → 50
    PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...

  3. NM_001410726.1 → NP_001397655.1  Golgi reassembly-stacking protein 1 isoform 4

    Status: REVIEWED

    Source sequence(s)
    AC138124
    Consensus CDS
    CCDS93246.1
    UniProtKB/TrEMBL
    A0A8Q3SHU6
    Related
    ENSP00000511895.1, ENST00000695414.1

  4. NM_001410731.1 → NP_001397660.1  Golgi reassembly-stacking protein 1 isoform 5

    Status: REVIEWED

    Source sequence(s)
    AC138124
    Consensus CDS
    CCDS93245.1
    UniProtKB/TrEMBL
    A0A8Q3WL08
    Related
    ENSP00000511911.1, ENST00000695430.1

  5. NM_031899.4 → NP_114105.1  Golgi reassembly-stacking protein 1 isoform 1

    See identical proteins and their annotated locations for NP_114105.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) encodes the longest isoform (1).
    Source sequence(s)
    AI824080, AK001574, AK057043, AK124755
    Consensus CDS
    CCDS2681.1
    UniProtKB/Swiss-Prot
    B3KWC8, Q3SYG7, Q8N272, Q96H42, Q9BQQ3
    UniProtKB/TrEMBL
    A0A8Q3WKF9, C9J9V9
    Related
    ENSP00000313869.3, ENST00000319283.8
    Conserved Domains (3) summary
    pfam04495
    Location:69 → 205
    GRASP55_65; GRASP55/65 PDZ-like domain
    cl00117
    Location:3 → 100
    PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...
    cl27544
    Location:194 → 298
    Herpes_glycop_D; Herpesvirus glycoprotein D/GG/GX domain

RNA

  1. NR_103866.2 RNA Sequence

    Status: REVIEWED

    Description
    Transcript Variant: This variant (4) uses an alternate splice site in an internal exon, compared to variant 1. This variant is represented as non-coding because the use of the 5'-most expected translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
    Source sequence(s)
    AI824080, AK124755, BC008928, BM470731, DB031221
    Related
    ENST00000452389.7

  2. NR_103867.2 RNA Sequence

    Status: REVIEWED

    Description
    Transcript Variant: This variant (5) uses an alternate splice site in an internal exon, compared to variant 1. This variant is represented as non-coding because the use of the 5'-most expected translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
    Source sequence(s)
    AI824080, AK057043, BC064624
    Related
    ENST00000453680.6

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000003.12 Reference GRCh38.p14 Primary Assembly

    Range
    39096599..39107627 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_047448726.1 → XP_047304682.1  Golgi reassembly-stacking protein 1 isoform X5

  2. XM_006713301.5 → XP_006713364.1  Golgi reassembly-stacking protein 1 isoform X1

    UniProtKB/TrEMBL
    A0A8Q3WKF9
    Related
    ENSP00000392993.2, ENST00000437458.4
    Conserved Domains (2) summary
    pfam04495
    Location:74 → 210
    GRASP55_65; GRASP55/65 PDZ-like domain
    cl00117
    Location:26 → 105
    PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...

  3. XM_011534021.4 → XP_011532323.1  Golgi reassembly-stacking protein 1 isoform X3

    UniProtKB/TrEMBL
    A0A8Q3WKF9
    Conserved Domains (1) summary
    cl00117
    Location:74 → 150
    PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...

  4. XM_011534020.4 → XP_011532322.1  Golgi reassembly-stacking protein 1 isoform X2

    UniProtKB/TrEMBL
    A0A8Q3WKF9
    Conserved Domains (2) summary
    pfam04495
    Location:74 → 180
    GRASP55_65; GRASP55/65 PDZ-like domain
    cl00117
    Location:26 → 105
    PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...

  5. XM_047448729.1 → XP_047304685.1  Golgi reassembly-stacking protein 1 isoform X8

    Related
    ENST00000695594.1

  6. XM_047448730.1 → XP_047304686.1  Golgi reassembly-stacking protein 1 isoform X9

    Related
    ENST00000695416.1

  7. XM_047448728.1 → XP_047304684.1  Golgi reassembly-stacking protein 1 isoform X7

  8. XM_047448725.1 → XP_047304681.1  Golgi reassembly-stacking protein 1 isoform X4

  9. XM_047448727.1 → XP_047304683.1  Golgi reassembly-stacking protein 1 isoform X6

RNA

  1. XR_940494.4 RNA Sequence

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060927.1 Alternate T2T-CHM13v2.0

    Range
    39108763..39119791 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_054347558.1 → XP_054203533.1  Golgi reassembly-stacking protein 1 isoform X5

  2. XM_054347554.1 → XP_054203529.1  Golgi reassembly-stacking protein 1 isoform X1

  3. XM_054347556.1 → XP_054203531.1  Golgi reassembly-stacking protein 1 isoform X3

  4. XM_054347555.1 → XP_054203530.1  Golgi reassembly-stacking protein 1 isoform X2

  5. XM_054347561.1 → XP_054203536.1  Golgi reassembly-stacking protein 1 isoform X8

  6. XM_054347562.1 → XP_054203537.1  Golgi reassembly-stacking protein 1 isoform X9

  7. XM_054347560.1 → XP_054203535.1  Golgi reassembly-stacking protein 1 isoform X7

  8. XM_054347557.1 → XP_054203532.1  Golgi reassembly-stacking protein 1 isoform X4

  9. XM_054347559.1 → XP_054203534.1  Golgi reassembly-stacking protein 1 isoform X6

RNA

  1. XR_008486775.1 RNA Sequence

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q9BQQ3.3 GenPept UniProtKB/Swiss-Prot:Q9BQQ3

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Chemical Information
Molecular Biology Databases
Research Materials
Tools
Miscellaneous