Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase AMFR

Gene

AMFR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 as a receptor for the GPI/autocrine motility factor.4 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri341 – 37939RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. receptor activity Source: UniProtKB
  3. ubiquitin protein ligase activity Source: MGI
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. aging Source: Ensembl
  2. endoplasmic reticulum unfolded protein response Source: UniProtKB
  3. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. learning or memory Source: Ensembl
  5. movement of cell or subcellular component Source: ProtInc
  6. protein oligomerization Source: UniProtKB
  7. protein polyubiquitination Source: UniProtKB
  8. signal transduction Source: ProtInc
  9. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Receptor

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase AMFR (EC:6.3.2.-)
Alternative name(s):
Autocrine motility factor receptor
Short name:
AMF receptor
RING finger protein 45
gp78
Gene namesi
Name:AMFR
Synonyms:RNF45
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:463. AMFR.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST
Transmembranei145 – 16521HelicalSequence AnalysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence AnalysisAdd
BLAST
Transmembranei215 – 23521HelicalSequence AnalysisAdd
BLAST
Transmembranei276 – 29621HelicalSequence AnalysisAdd
BLAST
Transmembranei429 – 44921HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. growth cone Source: Ensembl
  4. Hrd1p ubiquitin ligase complex Source: UniProtKB
  5. integral component of endoplasmic reticulum membrane Source: UniProtKB
  6. integral component of membrane Source: UniProtKB
  7. membrane Source: UniProtKB
  8. neuronal cell body Source: Ensembl
  9. nucleus Source: Ensembl
  10. perinuclear region of cytoplasm Source: ParkinsonsUK-UCL
  11. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi356 – 3561C → G: No degradation of HMGCR. 1 Publication

Organism-specific databases

PharmGKBiPA24768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643E3 ubiquitin-protein ligase AMFRPRO_0000064579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei516 – 5161Phosphoserine1 Publication
Modified residuei523 – 5231Phosphoserine1 Publication
Modified residuei542 – 5421PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UKV5.
PeptideAtlasiQ9UKV5.
PRIDEiQ9UKV5.

PTM databases

PhosphoSiteiQ9UKV5.

Expressioni

Gene expression databases

BgeeiQ9UKV5.
CleanExiHS_AMFR.
ExpressionAtlasiQ9UKV5. baseline and differential.
GenevestigatoriQ9UKV5.

Organism-specific databases

HPAiCAB026381.
HPA029018.

Interactioni

Subunit structurei

Interacts with RNF5. Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 AND RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation (By similarity). 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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VCPP550726EBI-1046367,EBI-355164

Protein-protein interaction databases

BioGridi106764. 88 interactions.
DIPiDIP-29060N.
IntActiQ9UKV5. 16 interactions.
MINTiMINT-2821880.
STRINGi9606.ENSP00000290649.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi332 – 3376Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi359 – 3613Combined sources
Helixi362 – 3698Combined sources
Beta strandi376 – 3783Combined sources
Helixi456 – 46712Combined sources
Helixi473 – 48311Combined sources
Helixi486 – 4949Combined sources
Helixi575 – 59925Combined sources
Helixi625 – 63713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJSNMR-A452-502[»]
2LVNNMR-C453-504[»]
2LVONMR-C453-504[»]
2LVPNMR-C453-504[»]
2LVQNMR-D453-504[»]
2LXHNMR-C313-393[»]
2LXPNMR-B574-600[»]
C327-384[»]
3FSHX-ray2.76C574-601[»]
3H8KX-ray1.80B573-600[»]
3TIWX-ray1.80C/D622-640[»]
4G3OX-ray1.60A456-498[»]
4LADX-ray2.30B313-393[»]
B574-600[»]
ProteinModelPortaliQ9UKV5.
SMRiQ9UKV5. Positions 327-384, 453-504, 574-599.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UKV5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini456 – 49843CUEPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni622 – 64019VCP/p97-interacting motif (VIM)1 PublicationAdd
BLAST

Domaini

The VCP/p97-interacting motif (VIM) is sufficient for binding VCP/p97 to form a complex capable of transferring VCP/p97 from the cytosol to microsomes.

Sequence similaritiesi

Contains 1 CUE domain.CuratedPROSITE-ProRule annotation
Contains 1 RING-type zinc finger.CuratedPROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri341 – 37939RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5243.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000037436.
HOVERGENiHBG044694.
InParanoidiQ9UKV5.
KOiK10636.
OMAiNTACCFL.
OrthoDBiEOG7QRQT8.
PhylomeDBiQ9UKV5.
TreeFamiTF320052.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003892. CUE.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51140. CUE. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UKV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLLFLERFP WPSLRTYTGL SGLALLGTII SAYRALSQPE AGPGEPDQLT
60 70 80 90 100
ASLQPEPPAP ARPSAGGPRA RDVAQYLLSD SLFVWVLVNT ACCVLMLVAK
110 120 130 140 150
LIQCIVFGPL RVSERQHLKD KFWNFIFYKF IFIFGVLNVQ TVEEVVMWCL
160 170 180 190 200
WFAGLVFLHL MVQLCKDRFE YLSFSPTTPM SSHGRVLSLL VAMLLSCCGL
210 220 230 240 250
AAVCSITGYT HGMHTLAFMA AESLLVTVRT AHVILRYVIH LWDLNHEGTW
260 270 280 290 300
EGKGTYVYYT DFVMELTLLS LDLMHHIHML LFGNIWLSMA SLVIFMQLRY
310 320 330 340 350
LFHEVQRRIR RHKNYLRVVG NMEARFAVAT PEELAVNNDD CAICWDSMQA
360 370 380 390 400
ARKLPCGHLF HNSCLRSWLE QDTSCPTCRM SLNIADNNRV REEHQGENLD
410 420 430 440 450
ENLVPVAAAE GRPRLNQHNH FFHFDGSRIA SWLPSFSVEV MHTTNILGIT
460 470 480 490 500
QASNSQLNAM AHQIQEMFPQ VPYHLVLQDL QLTRSVEITT DNILEGRIQV
510 520 530 540 550
PFPTQRSDSI RPALNSPVER PSSDQEEGET SAQTERVPLD LSPRLEETLD
560 570 580 590 600
FGEVEVEPSE VEDFEARGSR FSKSADERQR MLVQRKDELL QQARKRFLNK
610 620 630 640
SSEDDAASES FLPSEGASSD PVTLRRRMLA AAAERRLQKQ QTS
Length:643
Mass (Da):72,996
Last modified:June 1, 2003 - v2
Checksum:i8782324609C0E62A
GO

Sequence cautioni

The sequence AAA36671.1 differs from that shown.Several sequencing errors.Curated
The sequence AAA79362.1 differs from that shown. Reason: Frameshift at positions 355, 388, 411, 487, 537, 583 and 632. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti406 – 4061V → D in AAA79362 (PubMed:7626106).Curated
Sequence conflicti491 – 4911D → V in AAA79362 (PubMed:7626106).Curated
Sequence conflicti500 – 5001V → L in AAA79362 (PubMed:7626106).Curated
Sequence conflicti614 – 6141S → L in AAD56722 (PubMed:10456327).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti605 – 6051D → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035790

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124145 mRNA. Translation: AAD56722.1.
BC069197 mRNA. Translation: AAH69197.1.
L35233 mRNA. Translation: AAA79362.1. Frameshift.
M63175 mRNA. Translation: AAA36671.1. Sequence problems.
CCDSiCCDS10758.1.
PIRiA39877.
RefSeqiNP_001135.3. NM_001144.5.
UniGeneiHs.295137.

Genome annotation databases

GeneIDi267.
KEGGihsa:267.
UCSCiuc002eiy.4. human.

Polymorphism databases

DMDMi34922250.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124145 mRNA. Translation: AAD56722.1.
BC069197 mRNA. Translation: AAH69197.1.
L35233 mRNA. Translation: AAA79362.1. Frameshift.
M63175 mRNA. Translation: AAA36671.1. Sequence problems.
CCDSiCCDS10758.1.
PIRiA39877.
RefSeqiNP_001135.3. NM_001144.5.
UniGeneiHs.295137.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJSNMR-A452-502[»]
2LVNNMR-C453-504[»]
2LVONMR-C453-504[»]
2LVPNMR-C453-504[»]
2LVQNMR-D453-504[»]
2LXHNMR-C313-393[»]
2LXPNMR-B574-600[»]
C327-384[»]
3FSHX-ray2.76C574-601[»]
3H8KX-ray1.80B573-600[»]
3TIWX-ray1.80C/D622-640[»]
4G3OX-ray1.60A456-498[»]
4LADX-ray2.30B313-393[»]
B574-600[»]
ProteinModelPortaliQ9UKV5.
SMRiQ9UKV5. Positions 327-384, 453-504, 574-599.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106764. 88 interactions.
DIPiDIP-29060N.
IntActiQ9UKV5. 16 interactions.
MINTiMINT-2821880.
STRINGi9606.ENSP00000290649.

PTM databases

PhosphoSiteiQ9UKV5.

Polymorphism databases

DMDMi34922250.

Proteomic databases

MaxQBiQ9UKV5.
PeptideAtlasiQ9UKV5.
PRIDEiQ9UKV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi267.
KEGGihsa:267.
UCSCiuc002eiy.4. human.

Organism-specific databases

CTDi267.
GeneCardsiGC16M056395.
HGNCiHGNC:463. AMFR.
HPAiCAB026381.
HPA029018.
MIMi603243. gene.
neXtProtiNX_Q9UKV5.
PharmGKBiPA24768.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5243.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000037436.
HOVERGENiHBG044694.
InParanoidiQ9UKV5.
KOiK10636.
OMAiNTACCFL.
OrthoDBiEOG7QRQT8.
PhylomeDBiQ9UKV5.
TreeFamiTF320052.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiAMFR. human.
EvolutionaryTraceiQ9UKV5.
GeneWikiiAMFR.
GenomeRNAii267.
NextBioi1049.
PROiQ9UKV5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKV5.
CleanExiHS_AMFR.
ExpressionAtlasiQ9UKV5. baseline and differential.
GenevestigatoriQ9UKV5.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003892. CUE.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51140. CUE. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein."
    Shimizu K., Tani M., Watanabe H., Nagamachi Y., Niinaka Y., Shiroishi T., Ohwada S., Raz A., Yokota J.
    FEBS Lett. 456:295-300(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. "Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor."
    Huang B., Xie Y., Raz A.
    Biochem. Biophys. Res. Commun. 212:727-742(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 358-643.
    Tissue: Placenta.
  4. "Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor."
    Watanabe H., Carmi P., Hogan V., Raz T., Silletti S., Nabi I.R., Raz A.
    J. Biol. Chem. 266:13442-13448(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 520-643.
  5. "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum."
    Fang S., Ferrone M., Yang C., Jensen J.P., Tiwari S., Weissman A.M.
    Proc. Natl. Acad. Sci. U.S.A. 98:14422-14427(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A UBIQUITIN LIGASE, SUBCELLULAR LOCATION, INTERACTION WITH UBE2G2.
  6. "Overexpression of the tumor autocrine motility factor receptor, gp78, a ubiquitin protein ligase (E3), results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in Hep G2 cells."
    Liang J.S., Kim T., Fang S., Yamaguchi J., Weissman A.M., Fisher E.A., Ginsberg H.N.
    J. Biol. Chem. 278:23984-23988(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION OF APOB.
  7. "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase."
    Song B.L., Sever N., DeBose-Boyd R.A.
    Mol. Cell 19:829-840(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INSIG1 AND VCP, FUNCTION, MUTAGENESIS OF CYS-356.
  8. "Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane."
    Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.
    Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DERL1 AND VCP.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases."
    Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.
    Arch. Biochem. Biophys. 483:66-74(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Solution structure of RSGI RUH-076, a human CUE domain."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 452-502.
  13. "The structural and functional basis of the p97/valosin-containing protein (VCP)-interacting motif (VIM): mutually exclusive binding of cofactors to the N-terminal domain of p97."
    Hanzelmann P., Schindelin H.
    J. Biol. Chem. 286:38679-38690(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 622-640 IN COMPLEX WITH VCP, VIM MOTIF.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-605.

Entry informationi

Entry nameiAMFR_HUMAN
AccessioniPrimary (citable) accession number: Q9UKV5
Secondary accession number(s): P26442, Q8IZ70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 1, 2003
Last modified: March 4, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.