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Q9NPQ8

- RIC8A_HUMAN

UniProt

Q9NPQ8 - RIC8A_HUMAN

Protein

Synembryn-A

Gene

RIC8A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex By similarity. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation.By similarity1 Publication

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: Ensembl
    2. basement membrane organization Source: Ensembl
    3. cell-cell adhesion involved in gastrulation Source: Ensembl
    4. cell migration involved in gastrulation Source: Ensembl
    5. in utero embryonic development Source: Ensembl
    6. vasculature development Source: Ensembl
    7. visual learning Source: Ensembl

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synembryn-A
    Alternative name(s):
    Protein Ric-8A
    Gene namesi
    Name:RIC8A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:29550. RIC8A.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: Colocalizes with RIC8A in CA2 hippocampal neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671067.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Synembryn-APRO_0000235890Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei436 – 4361Phosphoserine3 Publications
    Modified residuei441 – 4411Phosphothreonine3 Publications
    Modified residuei502 – 5021Phosphoserine2 Publications
    Modified residuei523 – 5231Phosphoserine1 Publication
    Modified residuei524 – 5241Phosphoserine1 Publication
    Modified residuei528 – 5281Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NPQ8.
    PaxDbiQ9NPQ8.
    PRIDEiQ9NPQ8.

    PTM databases

    PhosphoSiteiQ9NPQ8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NPQ8.
    BgeeiQ9NPQ8.
    GenevestigatoriQ9NPQ8.

    Organism-specific databases

    HPAiCAB046012.
    HPA041491.

    Interactioni

    Subunit structurei

    Interacts with GDP-bound G alpha proteins GNAI1, GNAO1 and GNAQ, and with GNA13 with lower affinity. Does not interact with G-alpha proteins when they are in complex with subunits beta and gamma. Interacts (via C-terminus) with RGS14; the interaction stimulates the dissociation of the complex between RGS14 and the active GTP-bound form of GNAI1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBQLN1Q9UMX03EBI-717509,EBI-741480

    Protein-protein interaction databases

    BioGridi121946. 27 interactions.
    IntActiQ9NPQ8. 11 interactions.
    MINTiMINT-1422193.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NPQ8.
    SMRiQ9NPQ8. Positions 373-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the synembryn family.Curated

    Phylogenomic databases

    eggNOGiNOG322219.
    HOVERGENiHBG054867.
    InParanoidiQ9NPQ8.
    OMAiLHQTHRL.
    OrthoDBiEOG72JWG4.
    PhylomeDBiQ9NPQ8.
    TreeFamiTF314907.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR019318. Gua_nucleotide_exch_fac_Ric8.
    IPR008376. Synembryn.
    [Graphical view]
    PfamiPF10165. Ric8. 1 hit.
    [Graphical view]
    PRINTSiPR01802. SYNEMBRYN.
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NPQ8-1) [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

    MEPRAVAEAV ETGEEDVIME ALRSYNQEHS QSFTFDDAQQ EDRKRLAELL    50
    VSVLEQGLPP SHRVIWLQSV RILSRDRNCL DPFTSRQSLQ ALACYADISV 100
    SEGSVPESAD MDVVLESLKC LCNLVLSSPV AQMLAAEARL VVKLTERVGL 150
    YRERSFPHDV QFFDLRLLFL LTALRTDVRQ QLFQELKGVR LLTDTLELTL 200
    GVTPEGNPPP TLLPSQETER AMEILKVLFN ITLDSIKGEV DEEDAALYRH 250
    LGTLLRHCVM IATAGDRTEE FHGHAVNLLG NLPLKCLDVL LTLEPHGDST 300
    EFMGVNMDVI RALLIFLEKR LHKTHRLKES VAPVLSVLTE CARMHRPARK 350
    FLKAQVLPPL RDVRTRPEVG EMLRNKLVRL MTHLDTDVKR VAAEFLFVLC 400
    SESVPRFIKY TGYGNAAGLL AARGLMAGGR PEGQYSEDED TDTDEYKEAK 450
    ASINPVTGRV EEKPPNPMEG MTEEQKEHEA MKLVTMFDKL SRNRVIQPMG 500
    MSPRGHLTSL QDAMCETMEQ QLSSDPDSDP D 531
    Length:531
    Mass (Da):59,710
    Last modified:October 5, 2010 - v3
    Checksum:i2BAF3E2791F6E021
    GO
    Isoform 2 (identifier: Q9NPQ8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: MEPRAVAEAV...FDDAQQEDRK → MMPNRRTGRW...WWSRSSPCPQ

    Show »
    Length:525
    Mass (Da):58,943
    Checksum:i823D0B28817F594D
    GO
    Isoform 3 (identifier: Q9NPQ8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         354-354: A → AQGWPPP

    Show »
    Length:537
    Mass (Da):60,372
    Checksum:iC46E2F66B44DE40D
    GO
    Isoform 4 (identifier: Q9NPQ8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         209-209: Missing.

    Show »
    Length:530
    Mass (Da):59,612
    Checksum:i46ED334ED07C9EA8
    GO

    Sequence cautioni

    The sequence BAB14282.1 differs from that shown. Reason: Frameshift at position 397.
    The sequence BAB55126.1 differs from that shown. Reason: Frameshift at position 48.
    The sequence BAB14282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB15653.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481E → V in BAB55126. (PubMed:14702039)Curated
    Sequence conflicti405 – 4051P → L in CAD98025. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444MEPRA…QEDRK → MMPNRRTGRWVLAQGVKGQG RVAPGRRAWWSRSSPCPQ in isoform 2. 1 PublicationVSP_018507Add
    BLAST
    Alternative sequencei209 – 2091Missing in isoform 4. 1 PublicationVSP_039849
    Alternative sequencei354 – 3541A → AQGWPPP in isoform 3. 1 PublicationVSP_018508

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136935 mRNA. Translation: CAB66869.1.
    AK022870 mRNA. Translation: BAB14282.1. Sequence problems.
    AK027090 mRNA. Translation: BAB15653.1. Different initiation.
    AK027461 mRNA. Translation: BAB55126.1. Frameshift.
    AL390088 mRNA. Translation: CAB98211.1.
    BX538115 mRNA. Translation: CAD98025.1.
    AC069287 Genomic DNA. No translation available.
    BC011821 mRNA. Translation: AAH11821.2.
    BC111499 mRNA. Translation: AAI11500.1.
    BC121807 mRNA. Translation: AAI21808.1.
    BC121808 mRNA. Translation: AAI21809.1.
    CCDSiCCDS65982.1. [Q9NPQ8-1]
    CCDS7690.1. [Q9NPQ8-3]
    RefSeqiNP_001273063.1. NM_001286134.1. [Q9NPQ8-1]
    NP_068751.4. NM_021932.5. [Q9NPQ8-3]
    XP_006718333.1. XM_006718270.1.
    UniGeneiHs.592292.

    Genome annotation databases

    EnsembliENST00000325207; ENSP00000325941; ENSG00000177963. [Q9NPQ8-3]
    ENST00000526104; ENSP00000432008; ENSG00000177963. [Q9NPQ8-1]
    ENST00000527696; ENSP00000434833; ENSG00000177963. [Q9NPQ8-2]
    GeneIDi60626.
    KEGGihsa:60626.
    UCSCiuc001lof.3. human. [Q9NPQ8-3]
    uc001log.3. human. [Q9NPQ8-1]
    uc001loh.3. human. [Q9NPQ8-2]

    Polymorphism databases

    DMDMi308153562.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136935 mRNA. Translation: CAB66869.1 .
    AK022870 mRNA. Translation: BAB14282.1 . Sequence problems.
    AK027090 mRNA. Translation: BAB15653.1 . Different initiation.
    AK027461 mRNA. Translation: BAB55126.1 . Frameshift.
    AL390088 mRNA. Translation: CAB98211.1 .
    BX538115 mRNA. Translation: CAD98025.1 .
    AC069287 Genomic DNA. No translation available.
    BC011821 mRNA. Translation: AAH11821.2 .
    BC111499 mRNA. Translation: AAI11500.1 .
    BC121807 mRNA. Translation: AAI21808.1 .
    BC121808 mRNA. Translation: AAI21809.1 .
    CCDSi CCDS65982.1. [Q9NPQ8-1 ]
    CCDS7690.1. [Q9NPQ8-3 ]
    RefSeqi NP_001273063.1. NM_001286134.1. [Q9NPQ8-1 ]
    NP_068751.4. NM_021932.5. [Q9NPQ8-3 ]
    XP_006718333.1. XM_006718270.1.
    UniGenei Hs.592292.

    3D structure databases

    ProteinModelPortali Q9NPQ8.
    SMRi Q9NPQ8. Positions 373-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121946. 27 interactions.
    IntActi Q9NPQ8. 11 interactions.
    MINTi MINT-1422193.

    PTM databases

    PhosphoSitei Q9NPQ8.

    Polymorphism databases

    DMDMi 308153562.

    Proteomic databases

    MaxQBi Q9NPQ8.
    PaxDbi Q9NPQ8.
    PRIDEi Q9NPQ8.

    Protocols and materials databases

    DNASUi 60626.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325207 ; ENSP00000325941 ; ENSG00000177963 . [Q9NPQ8-3 ]
    ENST00000526104 ; ENSP00000432008 ; ENSG00000177963 . [Q9NPQ8-1 ]
    ENST00000527696 ; ENSP00000434833 ; ENSG00000177963 . [Q9NPQ8-2 ]
    GeneIDi 60626.
    KEGGi hsa:60626.
    UCSCi uc001lof.3. human. [Q9NPQ8-3 ]
    uc001log.3. human. [Q9NPQ8-1 ]
    uc001loh.3. human. [Q9NPQ8-2 ]

    Organism-specific databases

    CTDi 60626.
    GeneCardsi GC11P000200.
    HGNCi HGNC:29550. RIC8A.
    HPAi CAB046012.
    HPA041491.
    MIMi 609146. gene.
    neXtProti NX_Q9NPQ8.
    PharmGKBi PA142671067.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322219.
    HOVERGENi HBG054867.
    InParanoidi Q9NPQ8.
    OMAi LHQTHRL.
    OrthoDBi EOG72JWG4.
    PhylomeDBi Q9NPQ8.
    TreeFami TF314907.

    Miscellaneous databases

    ChiTaRSi RIC8A. human.
    GeneWikii RIC8A.
    GenomeRNAii 60626.
    NextBioi 65465.
    PROi Q9NPQ8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPQ8.
    Bgeei Q9NPQ8.
    Genevestigatori Q9NPQ8.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR019318. Gua_nucleotide_exch_fac_Ric8.
    IPR008376. Synembryn.
    [Graphical view ]
    Pfami PF10165. Ric8. 1 hit.
    [Graphical view ]
    PRINTSi PR01802. SYNEMBRYN.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Uterus.
    2. "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] (ISOFORM 1).
      Tissue: Teratocarcinoma.
    3. The European IMAGE consortium
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Uterine endothelium.
    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] (ISOFORM 4).
      Tissue: Lymph and Uterus.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells."
      Nishimura A., Okamoto M., Sugawara Y., Mizuno N., Yamauchi J., Itoh H.
      Genes Cells 11:487-498(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441; SER-523; SER-524 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND THR-441, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRIC8A_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPQ8
    Secondary accession number(s): Q0P508
    , Q2T9J1, Q7Z352, Q96EZ1, Q96SZ2, Q9H064, Q9H5H3, Q9H9E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 93 of the entry and version 3 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 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3