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Protein

ERBB receptor feedback inhibitor 1

Gene

ERRFI1

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

Functioni

Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity).By similarity

GO - Molecular functioni

  1. protein kinase binding Source: UniProtKB
  2. Rho GTPase activator activity Source: ProtInc

GO - Biological processi

  1. lung alveolus development Source: UniProtKB
  2. lung epithelium development Source: UniProtKB
  3. lung vasculature development Source: UniProtKB
  4. negative regulation of epidermal growth factor-activated receptor activity Source: UniProtKB
  5. negative regulation of protein autophosphorylation Source: UniProtKB
  6. positive regulation of Rho GTPase activity Source: GOC
  7. regulation of keratinocyte differentiation Source: UniProtKB
  8. response to stress Source: ProtInc
  9. skin morphogenesis Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ9UJM3.

Names & Taxonomyi

Protein namesi
Recommended name:
ERBB receptor feedback inhibitor 1
Alternative name(s):
Mitogen-inducible gene 6 protein
Short name:
MIG-6
Gene namesi
Name:ERRFI1
Synonyms:MIG6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:18185. ERRFI1.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Nucleus By similarity
Note: Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi346 – 3461M → A: Abolishes inhibition of EGFR activity. 1 Publication
Mutagenesisi352 – 3521F → A: Abolishes inhibition of EGFR activity. 1 Publication
Mutagenesisi358 – 3581Y → A: Abolishes inhibition of EGFR activity. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA142671904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 462461ERBB receptor feedback inhibitor 1PRO_0000096487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei131 – 1311PhosphothreonineBy similarity
Modified residuei251 – 2511Phosphoserine2 Publications
Modified residuei273 – 2731PhosphoserineBy similarity
Modified residuei302 – 3021PhosphoserineBy similarity
Modified residuei461 – 4611Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UJM3.
PaxDbiQ9UJM3.
PRIDEiQ9UJM3.

PTM databases

PhosphoSiteiQ9UJM3.

Expressioni

Inductioni

Levels are very low in quiescent cells. Up-regulated by mitogens.

Gene expression databases

BgeeiQ9UJM3.
CleanExiHS_ERRFI1.
ExpressionAtlasiQ9UJM3. baseline and differential.
GenevestigatoriQ9UJM3.

Organism-specific databases

HPAiHPA027206.

Interactioni

Subunit structurei

Interacts with ERBB2 (By similarity). Interacts with EGFR.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK1O147572EBI-2941912,EBI-974488
EGFRP005338EBI-2941912,EBI-297353
GRB2P629938EBI-2941912,EBI-401755
SFNP319473EBI-2941912,EBI-476295

Protein-protein interaction databases

BioGridi119923. 10 interactions.
DIPiDIP-42379N.
IntActiQ9UJM3. 18 interactions.
MINTiMINT-1591605.
STRINGi9606.ENSP00000366702.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi342 – 3443Combined sources
Turni356 – 3583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RF9X-ray3.50C/D315-374[»]
2RFDX-ray3.60C/D340-364[»]
2RFEX-ray2.90E/F325-364[»]
4I21X-ray3.37C/D315-374[»]
ProteinModelPortaliQ9UJM3.
SMRiQ9UJM3. Positions 335-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJM3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 36330Interaction with EGFR and ERBB2 and regulation of EGFR activationAdd
BLAST

Domaini

The EGFR-binding region prevents binding of a cyclin-like activator to the EGFR kinase domain, and thereby keeps EGFR in an inactive conformation. Also maintains EGFR in an inactive conformation by preventing formation of an asymmetric homodimer.1 Publication

Sequence similaritiesi

Belongs to the MIG6 family.Curated

Phylogenomic databases

eggNOGiNOG147618.
GeneTreeiENSGT00440000033870.
HOGENOMiHOG000234207.
HOVERGENiHBG031710.
InParanoidiQ9UJM3.
OMAiKPAIRIS.
PhylomeDBiQ9UJM3.
TreeFamiTF335720.

Family and domain databases

InterProiIPR015116. Cdc42_binding_dom_like.
IPR021619. Mig-6.
[Graphical view]
PfamiPF09027. GTPase_binding. 1 hit.
PF11555. Inhibitor_Mig-6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UJM3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIAGVAAQE IRVPLKTGFL HNGRAMGNMR KTYWSSRSEF KNNFLNIDPI
60 70 80 90 100
TMAYSLNSSA QERLIPLGHA SKSAPMNGHC FAENGPSQKS SLPPLLIPPS
110 120 130 140 150
ENLGPHEEDQ VVCGFKKLTV NGVCASTPPL TPIKNSPSLF PCAPLCERGS
160 170 180 190 200
RPLPPLPISE ALSLDDTDCE VEFLTSSDTD FLLEDSTLSD FKYDVPGRRS
210 220 230 240 250
FRGCGQINYA YFDTPAVSAA DLSYVSDQNG GVPDPNPPPP QTHRRLRRSH
260 270 280 290 300
SGPAGSFNKP AIRISNCCIH RASPNSDEDK PEVPPRVPIP PRPVKPDYRR
310 320 330 340 350
WSAEVTSSTY SDEDRPPKVP PREPLSPSNS RTPSPKSLPS YLNGVMPPTQ
360 370 380 390 400
SFAPDPKYVS SKALQRQNSE GSASKVPCIL PIIENGKKVS STHYYLLPER
410 420 430 440 450
PPYLDKYEKF FREAEETNGG AQIQPLPADC GISSATEKPD SKTKMDLGGH
460
VKRKHLSYVV SP
Length:462
Mass (Da):50,560
Last modified:May 1, 2000 - v1
Checksum:i7AFA9F6CEB602912
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71A → T(PubMed:7641805)Curated
Sequence conflicti36 – 361S → C(PubMed:7641805)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091D → N.
Corresponds to variant rs34781518 [ dbSNP | Ensembl ].
VAR_063039
Natural varianti158 – 1581I → L.
Corresponds to variant rs34974993 [ dbSNP | Ensembl ].
VAR_050975

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276373 mRNA. Translation: CAC20426.1.
AL034417 Genomic DNA. Translation: CAB52551.1.
AK315718 mRNA. Translation: BAG38076.1.
CH471130 Genomic DNA. Translation: EAW71593.1.
BC025337 mRNA. Translation: AAH25337.1.
AL137274 mRNA. Translation: CAB70672.1.
CCDSiCCDS94.1.
PIRiT46346.
RefSeqiNP_061821.1. NM_018948.3.
XP_006710760.1. XM_006710697.1.
UniGeneiHs.605445.

Genome annotation databases

EnsembliENST00000377482; ENSP00000366702; ENSG00000116285.
GeneIDi54206.
KEGGihsa:54206.
UCSCiuc001aoz.3. human.

Polymorphism databases

DMDMi27923810.

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
AJ276373 mRNA. Translation: CAC20426.1.
AL034417 Genomic DNA. Translation: CAB52551.1.
AK315718 mRNA. Translation: BAG38076.1.
CH471130 Genomic DNA. Translation: EAW71593.1.
BC025337 mRNA. Translation: AAH25337.1.
AL137274 mRNA. Translation: CAB70672.1.
CCDSiCCDS94.1.
PIRiT46346.
RefSeqiNP_061821.1. NM_018948.3.
XP_006710760.1. XM_006710697.1.
UniGeneiHs.605445.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RF9X-ray3.50C/D315-374[»]
2RFDX-ray3.60C/D340-364[»]
2RFEX-ray2.90E/F325-364[»]
4I21X-ray3.37C/D315-374[»]
ProteinModelPortaliQ9UJM3.
SMRiQ9UJM3. Positions 335-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119923. 10 interactions.
DIPiDIP-42379N.
IntActiQ9UJM3. 18 interactions.
MINTiMINT-1591605.
STRINGi9606.ENSP00000366702.

PTM databases

PhosphoSiteiQ9UJM3.

Polymorphism databases

DMDMi27923810.

Proteomic databases

MaxQBiQ9UJM3.
PaxDbiQ9UJM3.
PRIDEiQ9UJM3.

Protocols and materials databases

DNASUi54206.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377482; ENSP00000366702; ENSG00000116285.
GeneIDi54206.
KEGGihsa:54206.
UCSCiuc001aoz.3. human.

Organism-specific databases

CTDi54206.
GeneCardsiGC01M008064.
HGNCiHGNC:18185. ERRFI1.
HPAiHPA027206.
MIMi608069. gene.
neXtProtiNX_Q9UJM3.
PharmGKBiPA142671904.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG147618.
GeneTreeiENSGT00440000033870.
HOGENOMiHOG000234207.
HOVERGENiHBG031710.
InParanoidiQ9UJM3.
OMAiKPAIRIS.
PhylomeDBiQ9UJM3.
TreeFamiTF335720.

Enzyme and pathway databases

SignaLinkiQ9UJM3.

Miscellaneous databases

ChiTaRSiERRFI1. human.
EvolutionaryTraceiQ9UJM3.
GeneWikiiERRFI1.
GenomeRNAii54206.
NextBioi56530.
PROiQ9UJM3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJM3.
CleanExiHS_ERRFI1.
ExpressionAtlasiQ9UJM3. baseline and differential.
GenevestigatoriQ9UJM3.

Family and domain databases

InterProiIPR015116. Cdc42_binding_dom_like.
IPR021619. Mig-6.
[Graphical view]
PfamiPF09027. GTPase_binding. 1 hit.
PF11555. Inhibitor_Mig-6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel mitogen-inducible gene (mig-6): regulation during G1 progression and differentiation."
    Wick M., Buerger C., Funk M., Mueller R.
    Exp. Cell Res. 219:527-535(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "The gene for Mig-6 is regulated by methylmethanesulphonate and shows high expression in the liver."
    Van Laar T., Schouten T., van der Eb A.J., Terleth C.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-462.
    Tissue: Testis.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface."
    Zhang X., Pickin K.A., Bose R., Jura N., Cole P.A., Kuriyan J.
    Nature 450:741-744(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 325-364 IN COMPLEX WITH EGFR, SUBUNIT, MUTAGENESIS OF MET-346; PHE-352 AND TYR-358, DOMAIN.

Entry informationi

Entry nameiERRFI_HUMAN
AccessioniPrimary (citable) accession number: Q9UJM3
Secondary accession number(s): B2RDX9, Q9NTG9, Q9UD05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 111 of the entry and version 1 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 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.