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Protein Page:
AMFR (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
AMFR E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97- AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97- AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis. Interacts with RNF5. Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 AND RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation. Interacts with DRL1. Interacts (through a region distinct from the RING finger) with UBE2G2/UBC7. Component of the VCP/p97-AMFR/gp78 complex that enhances VCP/p97 binding to polyubiquitinated proteins for their degradation by the endoplasmic reticulum-associated degradation (ERAD) pathway. Interacts (via the VIM) with VCP/p97. Interacts (via its membrane domain) with INSIG1; the interaction initiates the sterol-mediated ubiquitination and degradation of HMGCR by the ERAD pathway. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system; Ligase; EC 6.3.2.-; EC 6.3.2.19; Endoplasmic reticulum; Motility/polarity/chemotaxis; Ubiquitin ligase; Receptor, misc.; Membrane protein, integral; Membrane protein, multi-pass
Cellular Component: endoplasmic reticulum membrane; protein complex; growth cone; cell soma; membrane; perinuclear region of cytoplasm; dendrite; integral to membrane; integral to endoplasmic reticulum membrane; nucleus
Molecular Function: protein binding; zinc ion binding; ubiquitin-protein ligase activity; receptor activity; ligase activity
Biological Process: ubiquitin-dependent protein catabolic process; ER-associated protein catabolic process; learning and/or memory; protein polyubiquitination; unfolded protein response; cell motility; signal transduction; protein oligomerization; aging
Reference #:  Q9UKV5 (UniProtKB)
Alt. Names/Synonyms: AMF receptor, isoform 1; AMF receptor, isoform 2; AMFR; AMFR2; autocrine motility factor receptor; autocrine motility factor receptor, isoform 1; Autocrine motility factor receptor, isoform 2; gp78; RING finger protein 45; RNF45
Gene Symbols: AMFR
Molecular weight: 72,996 Da
Basal Isoelectric point: 5.95  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

AMFR

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K353 DSMQAARKLPCGHLF
0 1 R391 IADNNRVREEHQGEN
0 1 S507 VPFPTQRSDSIRPAL
0 1 S509 FPTQRSDSIRPALNs
0 3 S516-p SIRPALNsPVERPss
0 1 S522-p NsPVERPssDQEEGE
0 2 S523-p sPVERPssDQEEGEt
0 1 T530-p sDQEEGEtsAQTERV
0 1 S531-p DQEEGEtsAQTERVP
0 18 S542-p ERVPLDLsPRLEEtL
0 3 T548-p LsPRLEEtLDFGEVE
0 2 K573 ARGSRFSKSADERQR
0 1 K586 QRMLVQRKDELLQQA
0 4 K600-ub ARKRFLNkSsEDDAA
0 2 S602-p KRFLNkSsEDDAASE
0 9 T623-p GASSDPVtLRRRMLA
  mouse

 
K353-ub DSMQAARkLPCGHLF
R391 IADGSRAREDHQGEN
S507-p VPFPTQRsDsLRPAL
S509-p FPTQRsDsLRPALNs
S516-p sLRPALNsPVERPSP
S522 NsPVERPSPDLEEGE
P523 sPVERPSPDLEEGEA
A530 PDLEEGEASVQTERV
S531 DLEEGEASVQTERVP
S542-p ERVPLDLsPRLEETL
T548 LsPRLEETLDFSEVE
K573-ub ARGSRFSkSADERQR
K586-ub QRMLVQRkDDLLQQA
K600-ub ARKRFLNkSsEDDGA
S602-p KRFLNkSsEDDGASE
T623 GTSSDPVTLRRRMLA
  rat

 
K468 DSMQAARKLPCGHLF
R506-m1 IADGSRArEDHQGEN
S622 VPFPVQRSDSLRPAL
S624 FPVQRSDSLRPALNS
S631 SLRPALNSPVERPGT
G637 NSPVERPGTDLEEGE
T638 SPVERPGTDLEEGEA
A645 TDLEEGEASVQTERV
S646 DLEEGEASVQTERVP
S657-p ERVPLDLsPRLEETL
T663 LsPRLEETLDFSEVE
K688 ARGSRFSKSADERQR
K701 QRMLVQRKDDLLQQA
K715 ARKRFLNKSSEDDGA
S717 KRFLNKSSEDDGASE
T738 GTSSDPVTLRRRMLA
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