Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UJM3

- ERRFI_HUMAN

UniProt

Q9UJM3 - ERRFI_HUMAN

Protein

ERBB receptor feedback inhibitor 1

Gene

ERRFI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 binding Source: IntAct
    2. protein kinase binding Source: UniProtKB
    3. 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

    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

    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

    ArrayExpressiQ9UJM3.
    BgeeiQ9UJM3.
    CleanExiHS_ERRFI1.
    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. 11 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 – 3443
    Turni356 – 3583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000234207.
    HOVERGENiHBG031710.
    InParanoidiQ9UJM3.
    OMAiKPAIRIS.
    PhylomeDBiQ9UJM3.
    TreeFamiTF335720.

    Family and domain databases

    InterProiIPR015116. Cdc42_binding_dom_like.
    IPR021619. Inhibitor_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

    MSIAGVAAQE IRVPLKTGFL HNGRAMGNMR KTYWSSRSEF KNNFLNIDPI    50
    TMAYSLNSSA QERLIPLGHA SKSAPMNGHC FAENGPSQKS SLPPLLIPPS 100
    ENLGPHEEDQ VVCGFKKLTV NGVCASTPPL TPIKNSPSLF PCAPLCERGS 150
    RPLPPLPISE ALSLDDTDCE VEFLTSSDTD FLLEDSTLSD FKYDVPGRRS 200
    FRGCGQINYA YFDTPAVSAA DLSYVSDQNG GVPDPNPPPP QTHRRLRRSH 250
    SGPAGSFNKP AIRISNCCIH RASPNSDEDK PEVPPRVPIP PRPVKPDYRR 300
    WSAEVTSSTY SDEDRPPKVP PREPLSPSNS RTPSPKSLPS YLNGVMPPTQ 350
    SFAPDPKYVS SKALQRQNSE GSASKVPCIL PIIENGKKVS STHYYLLPER 400
    PPYLDKYEKF FREAEETNGG AQIQPLPADC GISSATEKPD SKTKMDLGGH 450
    VKRKHLSYVV SP 462
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS94.1.
    PIRi T46346.
    RefSeqi NP_061821.1. NM_018948.3.
    XP_006710760.1. XM_006710697.1.
    UniGenei Hs.605445.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RF9 X-ray 3.50 C/D 315-374 [» ]
    2RFD X-ray 3.60 C/D 340-364 [» ]
    2RFE X-ray 2.90 E/F 325-364 [» ]
    4I21 X-ray 3.37 C/D 315-374 [» ]
    ProteinModelPortali Q9UJM3.
    SMRi Q9UJM3. Positions 335-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119923. 11 interactions.
    DIPi DIP-42379N.
    IntActi Q9UJM3. 18 interactions.
    MINTi MINT-1591605.
    STRINGi 9606.ENSP00000366702.

    PTM databases

    PhosphoSitei Q9UJM3.

    Polymorphism databases

    DMDMi 27923810.

    Proteomic databases

    MaxQBi Q9UJM3.
    PaxDbi Q9UJM3.
    PRIDEi Q9UJM3.

    Protocols and materials databases

    DNASUi 54206.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377482 ; ENSP00000366702 ; ENSG00000116285 .
    GeneIDi 54206.
    KEGGi hsa:54206.
    UCSCi uc001aoz.3. human.

    Organism-specific databases

    CTDi 54206.
    GeneCardsi GC01M008064.
    HGNCi HGNC:18185. ERRFI1.
    HPAi HPA027206.
    MIMi 608069. gene.
    neXtProti NX_Q9UJM3.
    PharmGKBi PA142671904.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147618.
    HOGENOMi HOG000234207.
    HOVERGENi HBG031710.
    InParanoidi Q9UJM3.
    OMAi KPAIRIS.
    PhylomeDBi Q9UJM3.
    TreeFami TF335720.

    Enzyme and pathway databases

    SignaLinki Q9UJM3.

    Miscellaneous databases

    ChiTaRSi ERRFI1. human.
    EvolutionaryTracei Q9UJM3.
    GeneWikii ERRFI1.
    GenomeRNAii 54206.
    NextBioi 56530.
    PROi Q9UJM3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJM3.
    Bgeei Q9UJM3.
    CleanExi HS_ERRFI1.
    Genevestigatori Q9UJM3.

    Family and domain databases

    InterProi IPR015116. Cdc42_binding_dom_like.
    IPR021619. Inhibitor_Mig-6.
    [Graphical view ]
    Pfami PF09027. GTPase_binding. 1 hit.
    PF11555. Inhibitor_Mig-6. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 108 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