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)

Q8N3Y1

- FBXW8_HUMAN

UniProt

Q8N3Y1 - FBXW8_HUMAN

Protein

F-box/WD repeat-containing protein 8

Gene

FBXW8

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 121 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradatation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (PubMed:24793695).4 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. Golgi organization Source: UniProtKB
    3. labyrinthine layer blood vessel development Source: Ensembl
    4. positive regulation of dendrite morphogenesis Source: UniProtKB
    5. protein ubiquitination Source: UniProtKB
    6. spongiotrophoblast layer development Source: Ensembl

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ8N3Y1.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box/WD repeat-containing protein 8
    Alternative name(s):
    F-box and WD-40 domain-containing protein 8
    F-box only protein 29
    Gene namesi
    Name:FBXW8
    Synonyms:FBW6, FBW8, FBX29, FBXO29, FBXW6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:13597. FBXW8.

    Subcellular locationi

    Cytoplasmperinuclear region 1 Publication. Golgi apparatus 1 Publication
    Note: Colocalizes with CUL7 at the Golgi apparatus in neurons.By similarity

    GO - Cellular componenti

    1. Cul7-RING ubiquitin ligase complex Source: UniProtKB
    2. Golgi apparatus Source: UniProtKB
    3. perinuclear region of cytoplasm Source: UniProtKB
    4. SCF ubiquitin ligase complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28039.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 598598F-box/WD repeat-containing protein 8PRO_0000050997Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8N3Y1.
    PaxDbiQ8N3Y1.
    PRIDEiQ8N3Y1.

    PTM databases

    PhosphoSiteiQ8N3Y1.

    Expressioni

    Gene expression databases

    BgeeiQ8N3Y1.
    CleanExiHS_FBXW8.
    GenevestigatoriQ8N3Y1.

    Organism-specific databases

    HPAiHPA038851.

    Interactioni

    Subunit structurei

    Part of a Cul7-RING ubiquitin-protein ligase complex, consisting of CUL7, RBX1, SKP1 and FBXW8. Interacts with GLMN isoform 1. Interacts with CUL7. Interacts with OBSL1, CUL1, CUL2, SKP1, CCT6B, PFDN5, CCT2, CCT3, CCT6A, CCT7, VBP1, CCDC8, ARF1, TRIP13, PDCD5 and GORASP1. Interacts with IRS1 (when phosphorylated). Interacts with MAP4K1/HPK1 (when autophosphorylated). Associated component of the 3M complex.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYCP011063EBI-914770,EBI-447544

    Protein-protein interaction databases

    BioGridi117645. 38 interactions.
    DIPiDIP-37970N.
    IntActiQ8N3Y1. 3 interactions.
    MINTiMINT-8415331.
    STRINGi9606.ENSP00000310686.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N3Y1.
    SMRiQ8N3Y1. Positions 119-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini113 – 15947F-boxPROSITE-ProRule annotationAdd
    BLAST
    Repeati197 – 24549WD 1Add
    BLAST
    Repeati254 – 29441WD 2Add
    BLAST
    Repeati297 – 33640WD 3Add
    BLAST
    Repeati430 – 47041WD 4Add
    BLAST
    Repeati473 – 51038WD 5Add
    BLAST

    Sequence similaritiesi

    Contains 1 F-box domain.PROSITE-ProRule annotation
    Contains 5 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiNOG115403.
    HOGENOMiHOG000112555.
    HOVERGENiHBG051597.
    InParanoidiQ8N3Y1.
    KOiK10264.
    OMAiNIFQYLD.
    OrthoDBiEOG7N8ZV2.
    PhylomeDBiQ8N3Y1.
    TreeFamiTF332593.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR001810. F-box_dom.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00646. F-box. 1 hit.
    PF00400. WD40. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    SM00320. WD40. 5 hits.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 2 hits.
    SSF81383. SSF81383. 1 hit.
    PROSITEiPS50181. FBOX. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N3Y1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDDYSLDEFR RRWQEELAQA QAPKKRRRPE AAERRARRPE VGSGRGEQAS    50
    GDPALAQRLL EGAGRPPAAR ATRAEGQDVA SRSRSPLARE GAGGGEQLVD 100
    QLIRDLNEMN DVPFFDIQLP YELAINIFQY LDRKELGRCA QVSKTWKVIA 150
    EDEVLWYRLC QQEGHLPDSS ISDYSCWKLI FQECRAKEHM LRTNWKNRKG 200
    AVSELEHVPD TVLCDVHSHD GVVIAGYTSG DVRVWDTRTW DYVAPFLESE 250
    DEEDEPGMQP NVSFVRINSS LAVAAYEDGF LNIWDLRTGK YPVHRFEHDA 300
    RIQALALSQD DATVATASAF DVVMLSPNEE GYWQIAAEFE VPKLVQYLEI 350
    VPETRRYPVA VAAAGDLMYL LKAEDSARTL LYAHGPPVTC LDVSANQVAF 400
    GVQGLGWVYE GSKILVYSLE AGRRLLKLGN VLRDFTCVNL SDSPPNLMVS 450
    GNMDGRVRIH DLRSGNIALS LSAHQLRVSA VQMDDWKIVS GGEEGLVSVW 500
    DYRMNQKLWE VYSGHPVQHI SFSSHSLITA NVPYQTVMRN ADLDSFTTHR 550
    RHRGLIRAYE FAVDQLAFQS PLPVCRSSCD AMATHYYDLA LAFPYNHV 598
    Length:598
    Mass (Da):67,394
    Last modified:May 18, 2010 - v2
    Checksum:i03B3C283BA46DB6B
    GO
    Isoform 2 (identifier: Q8N3Y1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-106: Missing.

    Show »
    Length:532
    Mass (Da):60,705
    Checksum:i921550273E26D2F2
    GO

    Sequence cautioni

    The sequence AAF03129.1 differs from that shown. Reason: Frameshift at positions 282 and 295.
    The sequence AAF03129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461G → S in AAH37296. (PubMed:15489334)Curated
    Sequence conflicti58 – 581R → G in AAH37296. (PubMed:15489334)Curated
    Sequence conflicti380 – 3801L → I in AAH37296. (PubMed:15489334)Curated
    Sequence conflicti510 – 5101E → K in AAF03129. (PubMed:10531037)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti192 – 1921R → Q.2 Publications
    Corresponds to variant rs4076700 [ dbSNP | Ensembl ].
    VAR_060326
    Natural varianti211 – 2111T → A.
    Corresponds to variant rs36021180 [ dbSNP | Ensembl ].
    VAR_057597
    Natural varianti536 – 5361T → M.
    Corresponds to variant rs3741466 [ dbSNP | Ensembl ].
    VAR_057598
    Natural varianti563 – 5631V → M.
    Corresponds to variant rs56350562 [ dbSNP | Ensembl ].
    VAR_062096

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei41 – 10666Missing in isoform 2. 1 PublicationVSP_008501Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176707 mRNA. Translation: AAF03129.1. Sequence problems.
    AC026368 Genomic DNA. No translation available.
    AC083806 Genomic DNA. No translation available.
    AC127164 Genomic DNA. No translation available.
    BC037296 mRNA. Translation: AAH37296.1.
    CCDSiCCDS44988.1. [Q8N3Y1-2]
    CCDS9182.1. [Q8N3Y1-1]
    RefSeqiNP_036306.1. NM_012174.1. [Q8N3Y1-2]
    NP_699179.2. NM_153348.2. [Q8N3Y1-1]
    UniGeneiHs.624537.
    Hs.696428.

    Genome annotation databases

    GeneIDi26259.
    KEGGihsa:26259.
    UCSCiuc001twf.1. human. [Q8N3Y1-2]
    uc001twg.1. human. [Q8N3Y1-1]

    Polymorphism databases

    DMDMi296434513.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176707 mRNA. Translation: AAF03129.1 . Sequence problems.
    AC026368 Genomic DNA. No translation available.
    AC083806 Genomic DNA. No translation available.
    AC127164 Genomic DNA. No translation available.
    BC037296 mRNA. Translation: AAH37296.1 .
    CCDSi CCDS44988.1. [Q8N3Y1-2 ]
    CCDS9182.1. [Q8N3Y1-1 ]
    RefSeqi NP_036306.1. NM_012174.1. [Q8N3Y1-2 ]
    NP_699179.2. NM_153348.2. [Q8N3Y1-1 ]
    UniGenei Hs.624537.
    Hs.696428.

    3D structure databases

    ProteinModelPortali Q8N3Y1.
    SMRi Q8N3Y1. Positions 119-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117645. 38 interactions.
    DIPi DIP-37970N.
    IntActi Q8N3Y1. 3 interactions.
    MINTi MINT-8415331.
    STRINGi 9606.ENSP00000310686.

    PTM databases

    PhosphoSitei Q8N3Y1.

    Polymorphism databases

    DMDMi 296434513.

    Proteomic databases

    MaxQBi Q8N3Y1.
    PaxDbi Q8N3Y1.
    PRIDEi Q8N3Y1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 26259.
    KEGGi hsa:26259.
    UCSCi uc001twf.1. human. [Q8N3Y1-2 ]
    uc001twg.1. human. [Q8N3Y1-1 ]

    Organism-specific databases

    CTDi 26259.
    GeneCardsi GC12P117348.
    H-InvDB HIX0026457.
    HIX0037115.
    HGNCi HGNC:13597. FBXW8.
    HPAi HPA038851.
    MIMi 609073. gene.
    neXtProti NX_Q8N3Y1.
    PharmGKBi PA28039.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG115403.
    HOGENOMi HOG000112555.
    HOVERGENi HBG051597.
    InParanoidi Q8N3Y1.
    KOi K10264.
    OMAi NIFQYLD.
    OrthoDBi EOG7N8ZV2.
    PhylomeDBi Q8N3Y1.
    TreeFami TF332593.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q8N3Y1.

    Miscellaneous databases

    ChiTaRSi FBXW8. human.
    GeneWikii FBXW8.
    GenomeRNAii 26259.
    NextBioi 48503.
    PROi Q8N3Y1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8N3Y1.
    CleanExi HS_FBXW8.
    Genevestigatori Q8N3Y1.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR001810. F-box_dom.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00646. F-box. 1 hit.
    PF00400. WD40. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    SM00320. WD40. 5 hits.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 2 hits.
    SSF81383. SSF81383. 1 hit.
    PROSITEi PS50181. FBOX. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLN-192.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORM 1), VARIANT GLN-192.
      Tissue: Brain.
    4. "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex."
      Dias D.C., Dolios G., Wang R., Pan Z.Q.
      Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN SCF-LIKE COMPLEX.
    5. "Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis."
      Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CUL7; SKP1; RBX1 AND GLMN.
    6. Cited for: INTERACTION WITH CUL7.
    7. "The CUL7 E3 ubiquitin ligase targets insulin receptor substrate 1 for ubiquitin-dependent degradation."
      Xu X., Sarikas A., Dias-Santagata D.C., Dolios G., Lafontant P.J., Tsai S.C., Zhu W., Nakajima H., Nakajima H.O., Field L.J., Wang R., Pan Z.Q.
      Mol. Cell 30:403-414(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IRS1.
    8. "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterning."
      Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E., Gygi S.P., Harper J.W., Bonni A.
      PLoS Biol. 9:E1001060-E1001060(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH OBSL1; CUL1; CUL2; CUL7; SKP1; CCT6B; PFDN5; CCT2; CCT3; CCT6A; CCT7; VBP1; CCDC8; ARF1; TRIP13; PDCD5 AND GORASP1, SUBCELLULAR LOCATION.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The CUL7/F-box and WD repeat domain containing 8 (CUL7/Fbxw8) ubiquitin ligase promotes degradation of hematopoietic progenitor kinase 1."
      Wang H., Chen Y., Lin P., Li L., Zhou G., Liu G., Logsdon C., Jin J., Abbruzzese J.L., Tan T.H., Wang H.
      J. Biol. Chem. 289:4009-4017(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUL7 AND MAP4K1.
    11. Cited for: FUNCTION.

    Entry informationi

    Entry nameiFBXW8_HUMAN
    AccessioniPrimary (citable) accession number: Q8N3Y1
    Secondary accession number(s): Q9UK95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 121 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3