2ZNV,2ZNR


Conserved Protein Domain Family
MPN_AMSH_like

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cd08066: MPN_AMSH_like 
Click on image for an interactive view with Cn3D
Mov34/MPN/PAD-1 family
AMSH (associated molecule with the Src homology 3 domain (SH3) of STAM (signal-transducing adapter molecule, also known as STAMBP)) and AMSH-like proteins (AMSH-LP) are members of JAMM/MPN+ deubiquitinases (DUBs), with Zn2+-dependent ubiquitin isopeptidase activity. AMSH specifically cleaves Lys 63 and not Lys48-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. AMSH and AMSH-LP are anchored on the early endosomal membrane via interaction with the clathrin coat. AMSH shares a common SH3-binding site with another endosomal DUB, UBPY (ubiquitin-specific protease Y; also known as USP8), the latter being a cysteine protease that does not discriminate between Lys48 and Lys63-linked ubiquitin. AMSH is involved in the degradation of EGF receptor (EGFR) and possibly other ubiquitinated endocytosed proteins. AMSH also interacts with CHMP1, CHMP2, and CHMP3 proteins, all of which are components of ESCRT-III, suggested to be required for EGFR down-regulation. The function of AMSH-LP has not been elucidated; however, it exhibits two fundamentally distinct features from AMSH: first, there is a substitution in the critical amino acid residue in the SH3-binding motif (SBM) in the human AMSH-LP, but not in its mouse ortholog, and lacks STAM-binding ability; second, AMSH-LP lacks the ability to interact with CHMP proteins. It is therefore likely that AMSH and AMSH-LP play different roles on early endosomes.
Statistics
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PSSM-Id: 163697
View PSSM: cd08066
Aligned: 31 rows
Threshold Bit Score: 232.486
Threshold Setting Gi: 239876048
Created: 23-Jul-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:MPN+ (JAMM) motif
Evidence:
  • Structure:2ZNR: Human AMSH-like protein (AMSH-LP); contacts calculated at 4.0A.
    View structure with Cn3D
  • Comment:AMSH (associated molecule with the SH3 domain of STAM) family protein, termed AMSH-like protein (AMSH-LP), is a deubiqutinating enzyme (DUB) and a zinc metalloprotease. It's catalytic and metal binding residues have also been determined experimentally.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                     #                                                  
2ZNV_A         8 LRCVVLPeDLCHKFLQLAESNTVr---GIATCGILCGKLTh--NEFTITHVIVPKQSAGpDYCDMENVEELFNVQDQHDL 82  human
2ZNR_A         8 LRCVVLPeDLCHKFLQLAESNTVr---GIETCGILCGKLTh--NEFTITHVIVPKQSAGpDYCDMENVEELFNVQDQHDL 82  human
XP_002154488 268 KRFIILPaDLTDKFLLLAASNTKr---NIETCGILCGRMVq--SQFRVTHLIIPKQHGTsDSCTTEKEEEMFDVQDKYDL 342 green hydra
XP_001763948 333 PKRLHIStKMLNEFMRLSKANTTr---NLETCGVLAGSLKk--GVFYVCTLIVPKQEATsDSCQTINEEEIFDAQDKRSL 407 Physcomitrella ...
XP_001899109 173 HKEVVVAaDLVENFVQLAQVNTNr---NVETCAILCGSLIt-gGVCRITHAVIPKQTGAaDSCDTHNEEEVFAYQDANNL 248 agent of lympha...
O15731       264 LRKIIVHgEVFQEFMRLAENNTKr---SIETCGILSGTLSn--DVFRITTIIIPKQEGTtDTCNTIEEHEIFEYQLENDL 338 Dictyostelium d...
XP_002129764 164 LRTILSPaDLPTKFMQLAHSNTSr---NIETCGVLFGKLAn--EVFVITHVLIPHQKGApDSCDTTREEDMWDFQDQYDG 238 Ciona intestinalis
XP_001689539   8 LRDVHVSvALMEEFLHYARSNTAr---GIESCGILAGKLLagdSTFAINTLIIPKQQGTtDTVQALNEEEIFEAQFEREL 84  Chlamydomonas r...
NP_172530     46 LRDVHISeRLLEDFTELARENTEk---DLETCGTLAAFLEr--GIFYVTTLIIPKQESTsNSCQAMNEVEVFSIQNEREL 120 thale cress
EEY69372     234 IRTLEIPsGIIAQFTLLASPNTNqppyGIETCGILAGILHd--RKLIITTLIIPKQEGSsDMCTMTNEEELYDFCFSNEL 311 Phytophthora in...
Feature 1              # #       #  #                                                            
2ZNV_A        83 LTLGWIHTHPTQTaFLSSVDLHTHCSYQLMlPEAIAIVCSPK--HKDTGIFRLT-NAGMLEVSACKKkGFHPHTKe---p 156 human
2ZNR_A        83 LTLGWIHTHPTQTaFLSSVDLHTHCSYQLMlPEAIAIVCSPK--HKDTGIFRLT-NAGMLEVSACKKkGFHPHTKe---p 156 human
XP_002154488 343 ITVGWIHTHPSQTcFLSSVDLHTQCSYQQLlPEAIAVVCSPK--YNNFGVYRLT-MHGLKLITNCTQnGFHPHNKd---p 416 green hydra
XP_001763948 408 FQLGWIHTHPTQScFMSSIDLHTHYSYQIMlPEAIAIVMAPTdnSRPYGIFRLSdPGGVKVIQQCQKrGFHPHENppggg 487 Physcomitrella ...
XP_001899109 249 ITLGWIHTHPSQTaFLSSVDLHTHCSYQLMlSEAVAIVVAPK--FNEVGIFRLS-ERGMKEINECRKvGFHPHENs---s 322 agent of lympha...
O15731       339 LTLGWIHTHPTQDcFLSAVDVHTHCSYQYLlQEAIAVVISPMa-NPNFGIFRLTdPPGLETVQKCKLkSFHPHPPvn-gi 416 Dictyostelium d...
XP_002129764 239 ICLGWIHTHPSQTaFLSSVDMHTHYPYQCLmPESVAIVCSGK--FNEVGYFMLDpGRGMNEIGKCRKpGFHPHPTt---p 313 Ciona intestinalis
XP_001689539  85 YPMGWIHTHPTQTcFLSSVDVHTQCGYQTMlDEAVAIVMAPSdrSKRCGLFRLStPGGLTLVQKCPLrGFHTHPPtdtgq 164 Chlamydomonas r...
NP_172530    121 YPVGWIHTHPSQGcFMSSVDLHTHYSYQVMvPEAFAIVVAPTdsSKSYGIFKLTdPGGMEVLRGCSEtGFHPHKEpedgn 200 thale cress
EEY69372     312 LTLGWIHTHPKQDcFLSSVDVHTQCGFQSIlPEAVAIVVAPSdpRRNVGVFRLTePSGLQLIQNCNMtGFHTHPSh---i 388 Phytophthora in...
Feature 1                                 
2ZNV_A       157 RLFSICkHVLVKD---IKIIVLDLR 178 human
2ZNR_A       157 RLFSICkHVLVKD---IKIIVLDLR 178 human
XP_002154488 417 PLFEESsGINIQDs--YGITIVDLR 439 green hydra
XP_001763948 488 PIYEWCnHVYMNPn--LQFDVMDLR 510 Physcomitrella patens subsp. patens
XP_001899109 323 ALFFYC-HDIRFEn-sLTATVVDLR 345 agent of lymphatic filariasis
O15731       417 PIYTKVdHVDLIWgkkSDSKVVDLR 441 Dictyostelium discoideum
XP_002129764 314 PLFESCdHVKPSPt--DAVHIVDWR 336 Ciona intestinalis
XP_001689539 165 ELYELCgHVFLNPr--TKHEVLDLR 187 Chlamydomonas reinhardtii
NP_172530    201 PVYEHCsNVYKNSn--LRFEIFDLR 223 thale cress
EEY69372     389 EIYSDAfEGKWQEq--VTAQIVDMR 411 Phytophthora infestans T30-4

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