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P27348

- 1433T_HUMAN

UniProt

P27348 - 1433T_HUMAN

Protein

14-3-3 protein theta

Gene

YWHAQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei56 – 561Interaction with phosphoserine on interacting protein
    Sitei127 – 1271Interaction with phosphoserine on interacting protein

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. intrinsic apoptotic signaling pathway Source: Reactome
    3. membrane organization Source: Reactome
    4. negative regulation of transcription, DNA-templated Source: BHF-UCL
    5. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    6. protein targeting Source: Ensembl
    7. small GTPase mediated signal transduction Source: Ensembl
    8. substantia nigra development Source: UniProt

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinkiP27348.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    14-3-3 protein theta
    Alternative name(s):
    14-3-3 protein T-cell
    14-3-3 protein tau
    Protein HS1
    Gene namesi
    Name:YWHAQ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12854. YWHAQ.

    Subcellular locationi

    Cytoplasm
    Note: In neurons, axonally transported to the nerve terminals.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytoplasmic vesicle membrane Source: Reactome
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProtKB
    5. membrane Source: UniProtKB
    6. protein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37443.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24524514-3-3 protein thetaPRO_0000058636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei49 – 491N6-acetyllysine1 Publication
    Modified residuei68 – 681N6-acetyllysine1 Publication
    Modified residuei115 – 1151N6-acetyllysine1 Publication
    Modified residuei232 – 2321Phosphoserine2 Publications

    Post-translational modificationi

    Ser-232 is probably phosphorylated by CK1.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP27348.
    PaxDbiP27348.
    PeptideAtlasiP27348.
    PRIDEiP27348.

    2D gel databases

    OGPiP27348.
    REPRODUCTION-2DPAGEIPI00018146.

    PTM databases

    PhosphoSiteiP27348.

    Miscellaneous databases

    PMAP-CutDBP27348.

    Expressioni

    Tissue specificityi

    Abundantly expressed in brain, heart and pancreas, and at lower levels in kidney and placenta. Up-regulated in the lumbar spinal cord from patients with sporadic amyotrophic lateral sclerosis (ALS) compared with controls, with highest levels of expression in individuals with predominant lower motor neuron involvement.1 Publication

    Gene expression databases

    ArrayExpressiP27348.
    BgeeiP27348.
    CleanExiHS_YWHAQ.
    GenevestigatoriP27348.

    Organism-specific databases

    HPAiCAB010286.
    HPA007925.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CDK16 By similarity. Interacts with SSH1. Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CDKN1B to the cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241' phosphorylated form of PDPK1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAM22Q9P0K1-32EBI-359854,EBI-1567267
    ARRB1P494073EBI-359854,EBI-743313
    ARRB2P321213EBI-359854,EBI-714559
    CBLP226816EBI-359854,EBI-518228
    CDK14O949213EBI-359854,EBI-1043945
    CDKN1BP465274EBI-359854,EBI-519280
    CSNK1A1P678282EBI-359854,EBI-7540603From a different organism.
    EGFRP005335EBI-359854,EBI-297353
    FSHRP239454EBI-359854,EBI-848239
    KANK1Q146782EBI-359854,EBI-2556221
    KANK1Q14678-23EBI-359854,EBI-6173812
    LRRK2Q5S0078EBI-359854,EBI-5323863
    Rnd3P615882EBI-359854,EBI-6930266From a different organism.
    SSH1Q8WYL52EBI-359854,EBI-1222387

    Protein-protein interaction databases

    BioGridi116168. 374 interactions.
    DIPiDIP-27584N.
    IntActiP27348. 82 interactions.
    MINTiMINT-121282.
    STRINGi9606.ENSP00000238081.

    Structurei

    Secondary structure

    1
    245
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513
    Helixi19 – 3113
    Helixi38 – 6831
    Helixi75 – 10329
    Turni104 – 1085
    Helixi112 – 13221
    Helixi135 – 15925
    Helixi165 – 18016
    Helixi185 – 20117
    Turni202 – 2054
    Helixi208 – 22720

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BTPX-ray2.80A/B1-234[»]
    ProteinModelPortaliP27348.
    SMRiP27348. Positions 1-230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27348.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    eggNOGiCOG5040.
    HOGENOMiHOG000240379.
    HOVERGENiHBG050423.
    InParanoidiP27348.
    KOiK16197.
    OMAiCELRSIC.
    OrthoDBiEOG7HHWT3.
    PhylomeDBiP27348.
    TreeFamiTF102002.

    Family and domain databases

    Gene3Di1.20.190.20. 1 hit.
    InterProiIPR000308. 14-3-3.
    IPR023409. 14-3-3_CS.
    IPR023410. 14-3-3_domain.
    [Graphical view]
    PANTHERiPTHR18860. PTHR18860. 1 hit.
    PfamiPF00244. 14-3-3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000868. 14-3-3. 1 hit.
    PRINTSiPR00305. 1433ZETA.
    SMARTiSM00101. 14_3_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48445. SSF48445. 1 hit.
    PROSITEiPS00796. 1433_1. 1 hit.
    PS00797. 1433_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27348-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN    50
    VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL 100
    LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ 150
    EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI 200
    AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN 245
    Length:245
    Mass (Da):27,764
    Last modified:August 1, 1992 - v1
    Checksum:i175534325E9E37C4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361D → N in AAV38817. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56468 mRNA. Translation: CAA39840.1.
    X57347 mRNA. Translation: CAA40622.1.
    BT020014 mRNA. Translation: AAV38817.1.
    CH471053 Genomic DNA. Translation: EAX00977.1.
    CH471053 Genomic DNA. Translation: EAX00979.1.
    BC050601 mRNA. Translation: AAH50601.1.
    BC056867 mRNA. Translation: AAH56867.1.
    BC093019 mRNA. Translation: AAH93019.1.
    AF070556 mRNA. Translation: AAC28640.1.
    CCDSiCCDS1666.1.
    PIRiS15076.
    RefSeqiNP_006817.1. NM_006826.3.
    UniGeneiHs.74405.

    Genome annotation databases

    EnsembliENST00000238081; ENSP00000238081; ENSG00000134308.
    ENST00000381844; ENSP00000371267; ENSG00000134308.
    GeneIDi10971.
    KEGGihsa:10971.
    UCSCiuc002qzx.3. human.

    Polymorphism databases

    DMDMi112690.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56468 mRNA. Translation: CAA39840.1 .
    X57347 mRNA. Translation: CAA40622.1 .
    BT020014 mRNA. Translation: AAV38817.1 .
    CH471053 Genomic DNA. Translation: EAX00977.1 .
    CH471053 Genomic DNA. Translation: EAX00979.1 .
    BC050601 mRNA. Translation: AAH50601.1 .
    BC056867 mRNA. Translation: AAH56867.1 .
    BC093019 mRNA. Translation: AAH93019.1 .
    AF070556 mRNA. Translation: AAC28640.1 .
    CCDSi CCDS1666.1.
    PIRi S15076.
    RefSeqi NP_006817.1. NM_006826.3.
    UniGenei Hs.74405.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BTP X-ray 2.80 A/B 1-234 [» ]
    ProteinModelPortali P27348.
    SMRi P27348. Positions 1-230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116168. 374 interactions.
    DIPi DIP-27584N.
    IntActi P27348. 82 interactions.
    MINTi MINT-121282.
    STRINGi 9606.ENSP00000238081.

    PTM databases

    PhosphoSitei P27348.

    Polymorphism databases

    DMDMi 112690.

    2D gel databases

    OGPi P27348.
    REPRODUCTION-2DPAGE IPI00018146.

    Proteomic databases

    MaxQBi P27348.
    PaxDbi P27348.
    PeptideAtlasi P27348.
    PRIDEi P27348.

    Protocols and materials databases

    DNASUi 10971.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238081 ; ENSP00000238081 ; ENSG00000134308 .
    ENST00000381844 ; ENSP00000371267 ; ENSG00000134308 .
    GeneIDi 10971.
    KEGGi hsa:10971.
    UCSCi uc002qzx.3. human.

    Organism-specific databases

    CTDi 10971.
    GeneCardsi GC02M009724.
    H-InvDB HIX0077146.
    HGNCi HGNC:12854. YWHAQ.
    HPAi CAB010286.
    HPA007925.
    MIMi 609009. gene.
    neXtProti NX_P27348.
    PharmGKBi PA37443.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5040.
    HOGENOMi HOG000240379.
    HOVERGENi HBG050423.
    InParanoidi P27348.
    KOi K16197.
    OMAi CELRSIC.
    OrthoDBi EOG7HHWT3.
    PhylomeDBi P27348.
    TreeFami TF102002.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    SignaLinki P27348.

    Miscellaneous databases

    ChiTaRSi YWHAQ. human.
    EvolutionaryTracei P27348.
    GeneWikii YWHAQ.
    GenomeRNAii 10971.
    NextBioi 41686.
    PMAP-CutDB P27348.
    PROi P27348.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27348.
    Bgeei P27348.
    CleanExi HS_YWHAQ.
    Genevestigatori P27348.

    Family and domain databases

    Gene3Di 1.20.190.20. 1 hit.
    InterProi IPR000308. 14-3-3.
    IPR023409. 14-3-3_CS.
    IPR023410. 14-3-3_domain.
    [Graphical view ]
    PANTHERi PTHR18860. PTHR18860. 1 hit.
    Pfami PF00244. 14-3-3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000868. 14-3-3. 1 hit.
    PRINTSi PR00305. 1433ZETA.
    SMARTi SM00101. 14_3_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48445. SSF48445. 1 hit.
    PROSITEi PS00796. 1433_1. 1 hit.
    PS00797. 1433_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of a human protein kinase regulator protein."
      Nielsen P.J.
      Biochim. Biophys. Acta 1088:425-428(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: T-cell.
    2. "Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway."
      Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., Vandekerckhove J., Celis J.E.
      J. Mol. Biol. 231:982-998(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Keratinocyte.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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, Skin and Uterus.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-18.
      Tissue: Platelet.
    7. Bienvenut W.V., Dhillon A.S., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma and Hepatoma.
    8. Yu W., Gibbs R.A.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245.
      Tissue: Brain.
    9. "14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction."
      Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N., Moelling K., Aitken A.
      J. Biol. Chem. 272:28882-28888(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal cord."
      Malaspina A., Kaushik N., de Belleroche J.
      J. Neurochem. 75:2511-2520(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."
      Fujita N., Sato S., Katayama K., Tsuruo T.
      J. Biol. Chem. 277:28706-28713(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDKN1B.
    12. "Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3."
      Sato S., Fujita N., Tsuruo T.
      J. Biol. Chem. 277:39360-39367(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PDPK1.
    13. "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia."
      Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.
      J. Cell Biol. 165:465-471(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSH1.
    14. "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.
    15. "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
      Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
      EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAB2.
    16. "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.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3; LYS-49; LYS-68 AND LYS-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways."
      Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., Gamblin S.J.
      Nature 376:188-191(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    24. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

    Entry informationi

    Entry namei1433T_HUMAN
    AccessioniPrimary (citable) accession number: P27348
    Secondary accession number(s): D6W4Z5
    , Q567U5, Q5TZU8, Q9UP48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 160 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3