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Q92569

- P55G_HUMAN

UniProt

Q92569 - P55G_HUMAN

Protein

Phosphatidylinositol 3-kinase regulatory subunit gamma

Gene

PIK3R3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1.

    GO - Molecular functioni

    1. 1-phosphatidylinositol-3-kinase activity Source: ProtInc
    2. phosphatidylinositol 3-kinase regulator activity Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. insulin receptor signaling pathway Source: ProtInc
    2. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    3. phosphatidylinositol biosynthetic process Source: Reactome
    4. phospholipid metabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000117461-MONOMER.
    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_115529. Interleukin-7 signaling.
    REACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19344. Costimulation by the CD28 family.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiQ92569.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 3-kinase regulatory subunit gamma
    Short name:
    PI3-kinase regulatory subunit gamma
    Short name:
    PI3K regulatory subunit gamma
    Short name:
    PtdIns-3-kinase regulatory subunit gamma
    Alternative name(s):
    Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma
    Short name:
    PI3-kinase subunit p55-gamma
    Short name:
    PtdIns-3-kinase regulatory subunit p55-gamma
    p55PIK
    Gene namesi
    Name:PIK3R3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8981. PIK3R3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. phosphatidylinositol 3-kinase complex Source: InterPro

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33314.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Phosphatidylinositol 3-kinase regulatory subunit gammaPRO_0000080767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei341 – 3411PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ92569.
    PaxDbiQ92569.
    PRIDEiQ92569.

    PTM databases

    PhosphoSiteiQ92569.

    Expressioni

    Tissue specificityi

    Highest levels in brain and testis. Lower levels in adipose tissue, kidney, heart, lung and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ92569.
    BgeeiQ92569.
    CleanExiHS_PIK3R3.
    GenevestigatoriQ92569.

    Organism-specific databases

    HPAiHPA005751.

    Interactioni

    Subunit structurei

    Heterodimer of a regulatory subunit PIK3R3 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP02EBI-79893,EBI-375446
    ARP1027537EBI-79893,EBI-608057
    EGFRP005335EBI-79893,EBI-297353
    ERBB2P046269EBI-79893,EBI-641062
    ERBB3P2186022EBI-79893,EBI-720706
    GAB1Q1348036EBI-79893,EBI-517684
    HTTP428586EBI-79893,EBI-466029
    KITP1072131EBI-79893,EBI-1379503
    METP0858111EBI-79893,EBI-1039152

    Protein-protein interaction databases

    BioGridi114075. 34 interactions.
    DIPiDIP-30925N.
    IntActiQ92569. 43 interactions.
    MINTiMINT-1490763.
    STRINGi9606.ENSP00000262741.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92569.
    SMRiQ92569. Positions 55-455.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 16096SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini358 – 45295SH2 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi34 – 4411Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PI3K p85 subunit family.Curated
    Contains 2 SH2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain

    Phylogenomic databases

    eggNOGiNOG263689.
    HOVERGENiHBG082100.
    InParanoidiQ92569.
    KOiK02649.
    OrthoDBiEOG7BP831.
    PhylomeDBiQ92569.
    TreeFamiTF102033.

    Family and domain databases

    Gene3Di3.30.505.10. 2 hits.
    InterProiIPR001720. PI3kinase_P85.
    IPR000980. SH2.
    [Graphical view]
    PANTHERiPTHR10155. PTHR10155. 1 hit.
    PfamiPF00017. SH2. 2 hits.
    [Graphical view]
    PRINTSiPR00678. PI3KINASEP85.
    PR00401. SH2DOMAIN.
    SMARTiSM00252. SH2. 2 hits.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 2 hits.
    PROSITEiPS50001. SH2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92569-1) [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

    MYNTVWSMDR DDADWREVMM PYSTELIFYI EMDPPALPPK PPKPMTSAVP    50
    NGMKDSSVSL QDAEWYWGDI SREEVNDKLR DMPDGTFLVR DASTKMQGDY 100
    TLTLRKGGNN KLIKIYHRDG KYGFSDPLTF NSVVELINHY HHESLAQYNP 150
    KLDVKLMYPV SRYQQDQLVK EDNIDAVGKK LQEYHSQYQE KSKEYDRLYE 200
    EYTRTSQEIQ MKRTAIEAFN ETIKIFEEQC HTQEQHSKEY IERFRREGNE 250
    KEIERIMMNY DKLKSRLGEI HDSKMRLEQD LKNQALDNRE IDKKMNSIKP 300
    DLIQLRKIRD QHLVWLNHKG VRQKRLNVWL GIKNEDADEN YFINEEDENL 350
    PHYDEKTWFV EDINRVQAED LLYGKPDGAF LIRESSKKGC YACSVVADGE 400
    VKHCVIYSTA RGYGFAEPYN LYSSLKELVL HYQQTSLVQH NDSLNVRLAY 450
    PVHAQMPSLC R 461
    Length:461
    Mass (Da):54,448
    Last modified:January 11, 2011 - v2
    Checksum:i303BCC2F9EEE5364
    GO
    Isoform 2 (identifier: Q92569-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         256-314: Missing.

    Show »
    Length:402
    Mass (Da):47,348
    Checksum:i054C2111B68F17A6
    GO
    Isoform 3 (identifier: Q92569-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         36-71: Missing.
         256-314: Missing.

    Show »
    Length:366
    Mass (Da):43,465
    Checksum:iF8B6B90E29AA2DF6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211P → L in AAC39696. (PubMed:9524259)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti283 – 2831N → K.4 Publications
    Corresponds to variant rs785467 [ dbSNP | Ensembl ].
    VAR_047153

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei36 – 7136Missing in isoform 3. 1 PublicationVSP_004713Add
    BLAST
    Alternative sequencei256 – 31459Missing in isoform 2 and isoform 3. 1 PublicationVSP_004714Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF028785 mRNA. Translation: AAC39696.1.
    D88532 mRNA. Translation: BAA13636.1.
    AK313726 mRNA. Translation: BAG36468.1.
    AL358075 Genomic DNA. Translation: CAI21702.1.
    AL358075 Genomic DNA. Translation: CAI21703.1.
    CH471059 Genomic DNA. Translation: EAX06946.1.
    CH471059 Genomic DNA. Translation: EAX06947.1.
    CH471059 Genomic DNA. Translation: EAX06944.1.
    CH471059 Genomic DNA. Translation: EAX06945.1.
    CCDSiCCDS529.1. [Q92569-1]
    RefSeqiNP_001107644.1. NM_001114172.1. [Q92569-1]
    NP_003620.3. NM_003629.3. [Q92569-1]
    UniGeneiHs.655387.

    Genome annotation databases

    EnsembliENST00000262741; ENSP00000262741; ENSG00000117461. [Q92569-1]
    ENST00000372006; ENSP00000361075; ENSG00000117461. [Q92569-1]
    ENST00000420542; ENSP00000412546; ENSG00000117461. [Q92569-1]
    ENST00000423209; ENSP00000391431; ENSG00000117461. [Q92569-2]
    GeneIDi8503.
    KEGGihsa:8503.
    UCSCiuc001cpb.4. human. [Q92569-1]
    uc009vyb.3. human. [Q92569-2]

    Polymorphism databases

    DMDMi317373310.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF028785 mRNA. Translation: AAC39696.1 .
    D88532 mRNA. Translation: BAA13636.1 .
    AK313726 mRNA. Translation: BAG36468.1 .
    AL358075 Genomic DNA. Translation: CAI21702.1 .
    AL358075 Genomic DNA. Translation: CAI21703.1 .
    CH471059 Genomic DNA. Translation: EAX06946.1 .
    CH471059 Genomic DNA. Translation: EAX06947.1 .
    CH471059 Genomic DNA. Translation: EAX06944.1 .
    CH471059 Genomic DNA. Translation: EAX06945.1 .
    CCDSi CCDS529.1. [Q92569-1 ]
    RefSeqi NP_001107644.1. NM_001114172.1. [Q92569-1 ]
    NP_003620.3. NM_003629.3. [Q92569-1 ]
    UniGenei Hs.655387.

    3D structure databases

    ProteinModelPortali Q92569.
    SMRi Q92569. Positions 55-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114075. 34 interactions.
    DIPi DIP-30925N.
    IntActi Q92569. 43 interactions.
    MINTi MINT-1490763.
    STRINGi 9606.ENSP00000262741.

    PTM databases

    PhosphoSitei Q92569.

    Polymorphism databases

    DMDMi 317373310.

    Proteomic databases

    MaxQBi Q92569.
    PaxDbi Q92569.
    PRIDEi Q92569.

    Protocols and materials databases

    DNASUi 8503.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262741 ; ENSP00000262741 ; ENSG00000117461 . [Q92569-1 ]
    ENST00000372006 ; ENSP00000361075 ; ENSG00000117461 . [Q92569-1 ]
    ENST00000420542 ; ENSP00000412546 ; ENSG00000117461 . [Q92569-1 ]
    ENST00000423209 ; ENSP00000391431 ; ENSG00000117461 . [Q92569-2 ]
    GeneIDi 8503.
    KEGGi hsa:8503.
    UCSCi uc001cpb.4. human. [Q92569-1 ]
    uc009vyb.3. human. [Q92569-2 ]

    Organism-specific databases

    CTDi 8503.
    GeneCardsi GC01M046505.
    H-InvDB HIX0000542.
    HGNCi HGNC:8981. PIK3R3.
    HPAi HPA005751.
    MIMi 606076. gene.
    neXtProti NX_Q92569.
    PharmGKBi PA33314.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263689.
    HOVERGENi HBG082100.
    InParanoidi Q92569.
    KOi K02649.
    OrthoDBi EOG7BP831.
    PhylomeDBi Q92569.
    TreeFami TF102033.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000117461-MONOMER.
    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_115529. Interleukin-7 signaling.
    REACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19344. Costimulation by the CD28 family.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki Q92569.

    Miscellaneous databases

    GeneWikii PIK3R3.
    GenomeRNAii 8503.
    NextBioi 31821.
    PROi Q92569.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92569.
    Bgeei Q92569.
    CleanExi HS_PIK3R3.
    Genevestigatori Q92569.

    Family and domain databases

    Gene3Di 3.30.505.10. 2 hits.
    InterProi IPR001720. PI3kinase_P85.
    IPR000980. SH2.
    [Graphical view ]
    PANTHERi PTHR10155. PTHR10155. 1 hit.
    Pfami PF00017. SH2. 2 hits.
    [Graphical view ]
    PRINTSi PR00678. PI3KINASEP85.
    PR00401. SH2DOMAIN.
    SMARTi SM00252. SH2. 2 hits.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 2 hits.
    PROSITEi PS50001. SH2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of human p55 gamma, a regulatory subunit of phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen with the insulin-like growth factor-I receptor."
      Dey B.R., Furlanetto R.W., Nissley S.P.
      Gene 209:175-183(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT LYS-283.
      Tissue: Fetal brain.
    2. "Molecular cloning of human p55pik."
      Suzuki T.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-283.
    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] (ISOFORM 1), VARIANT LYS-283.
      Tissue: Brain.
    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], VARIANT LYS-283.
    6. "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin."
      Hafizi S., Alindri F., Karlsson R., Dahlbaeck B.
      Biochem. Biophys. Res. Commun. 299:793-800(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXL.

    Entry informationi

    Entry nameiP55G_HUMAN
    AccessioniPrimary (citable) accession number: Q92569
    Secondary accession number(s): B2R9C1
    , D3DQ12, O60482, Q5T4P1, Q5T4P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 129 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 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3