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P63151

- 2ABA_HUMAN

UniProt

P63151 - 2ABA_HUMAN

Protein

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform

Gene

PPP2R2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (27 Sep 2004)
      Previous versions | rss
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    Functioni

    The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein phosphatase type 2A regulator activity Source: UniProtKB
    3. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. G2/M transition of mitotic cell cycle Source: Reactome
    2. gene expression Source: Reactome
    3. mitotic cell cycle Source: Reactome
    4. mitotic nuclear envelope reassembly Source: Reactome
    5. mRNA metabolic process Source: Reactome
    6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    7. protein dephosphorylation Source: UniProtKB
    8. regulation of catalytic activity Source: GOC
    9. response to morphine Source: Ensembl
    10. RNA metabolic process Source: Reactome
    11. signal transduction Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_821. Cyclin D associated events in G1.
    SignaLinkiP63151.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
    Alternative name(s):
    PP2A subunit B isoform B55-alpha
    PP2A subunit B isoform PR55-alpha
    PP2A subunit B isoform R2-alpha
    PP2A subunit B isoform alpha
    Gene namesi
    Name:PPP2R2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9304. PPP2R2A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. protein phosphatase type 2A complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33668.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 447446Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoformPRO_0000071415Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP63151.
    PaxDbiP63151.
    PeptideAtlasiP63151.
    PRIDEiP63151.

    PTM databases

    PhosphoSiteiP63151.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined.1 Publication

    Gene expression databases

    ArrayExpressiP63151.
    BgeeiP63151.
    CleanExiHS_PPP2R2A.
    GenevestigatoriP63151.

    Organism-specific databases

    HPAiHPA042122.
    HPA042770.

    Interactioni

    Subunit structurei

    Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD By similarity. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with TP53.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP2R1AP301538EBI-1048931,EBI-302388
    PPP2R1BP301542EBI-1048931,EBI-357094

    Protein-protein interaction databases

    BioGridi111512. 53 interactions.
    DIPiDIP-29398N.
    IntActiP63151. 18 interactions.
    MINTiMINT-2835351.
    STRINGi9606.ENSP00000370113.

    Structurei

    Secondary structure

    1
    447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 164
    Beta strandi21 – 233
    Helixi27 – 293
    Beta strandi30 – 367
    Beta strandi38 – 4710
    Beta strandi50 – 578
    Beta strandi71 – 788
    Beta strandi83 – 853
    Helixi86 – 883
    Beta strandi90 – 923
    Beta strandi98 – 1014
    Beta strandi106 – 1149
    Beta strandi119 – 13214
    Beta strandi156 – 17217
    Beta strandi182 – 1854
    Beta strandi189 – 1957
    Beta strandi197 – 2048
    Beta strandi207 – 21610
    Helixi222 – 2243
    Beta strandi229 – 2346
    Beta strandi241 – 2466
    Beta strandi251 – 2555
    Turni256 – 2583
    Beta strandi260 – 2623
    Beta strandi267 – 2693
    Helixi280 – 2845
    Beta strandi288 – 2936
    Beta strandi297 – 31216
    Beta strandi323 – 3253
    Helixi327 – 3293
    Turni330 – 3323
    Helixi333 – 3386
    Helixi341 – 3433
    Beta strandi348 – 3503
    Beta strandi354 – 3607
    Beta strandi365 – 3706
    Turni371 – 3733
    Beta strandi376 – 3805
    Helixi410 – 4123
    Beta strandi421 – 4244
    Beta strandi426 – 4349
    Beta strandi439 – 4435

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DW8X-ray2.85B/E1-447[»]
    ProteinModelPortaliP63151.
    SMRiP63151. Positions 8-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63151.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati26 – 6540WD 1Add
    BLAST
    Repeati91 – 13242WD 2Add
    BLAST
    Repeati175 – 21339WD 3Add
    BLAST
    Repeati224 – 26441WD 4Add
    BLAST
    Repeati283 – 32139WD 5Add
    BLAST
    Repeati338 – 37942WD 6Add
    BLAST
    Repeati414 – 44633WD 7Add
    BLAST

    Sequence similaritiesi

    Contains 7 WD repeats.Curated

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG5170.
    HOGENOMiHOG000089745.
    HOVERGENiHBG000012.
    InParanoidiP63151.
    KOiK04354.
    OMAiQRNMAGA.
    OrthoDBiEOG7Q5HCZ.
    PhylomeDBiP63151.
    TreeFamiTF105553.

    Family and domain databases

    Gene3Di2.130.10.10. 3 hits.
    InterProiIPR000009. PP2A_PR55.
    IPR018067. PP2A_PR55_CS.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR11871. PTHR11871. 1 hit.
    PIRSFiPIRSF037309. PP2A_PR55. 1 hit.
    PRINTSiPR00600. PP2APR55.
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 3 hits.
    PROSITEiPS01024. PR55_1. 1 hit.
    PS01025. PR55_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P63151-1) [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

    MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG    50
    RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR 100
    WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT 150
    TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI 200
    NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT 250
    IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM 300
    MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW 350
    NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS 400
    GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN 447
    Length:447
    Mass (Da):51,692
    Last modified:September 27, 2004 - v1
    Checksum:iF4D407FF7ADA4ED6
    GO
    Isoform 2 (identifier: P63151-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: MA → MFPKFSLRSMFH

    Note: No experimental confirmation available.

    Show »
    Length:457
    Mass (Da):53,000
    Checksum:i242C50314171EDDE
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 22MA → MFPKFSLRSMFH in isoform 2. 1 PublicationVSP_043100

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64929 mRNA. Translation: AAA36490.1.
    AK303981 mRNA. Translation: BAG64899.1.
    AK314823 mRNA. Translation: BAG37345.1.
    AC022911 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63578.1.
    BC041071 mRNA. Translation: AAH41071.1.
    CCDSiCCDS34867.1. [P63151-1]
    CCDS55213.1. [P63151-2]
    PIRiA38351.
    RefSeqiNP_001171062.1. NM_001177591.1. [P63151-2]
    NP_002708.1. NM_002717.3. [P63151-1]
    UniGeneiHs.146339.

    Genome annotation databases

    EnsembliENST00000315985; ENSP00000325074; ENSG00000221914. [P63151-2]
    ENST00000380737; ENSP00000370113; ENSG00000221914. [P63151-1]
    GeneIDi5520.
    KEGGihsa:5520.
    UCSCiuc003xeu.3. human. [P63151-1]
    uc011laf.2. human. [P63151-2]

    Polymorphism databases

    DMDMi52783535.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64929 mRNA. Translation: AAA36490.1 .
    AK303981 mRNA. Translation: BAG64899.1 .
    AK314823 mRNA. Translation: BAG37345.1 .
    AC022911 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63578.1 .
    BC041071 mRNA. Translation: AAH41071.1 .
    CCDSi CCDS34867.1. [P63151-1 ]
    CCDS55213.1. [P63151-2 ]
    PIRi A38351.
    RefSeqi NP_001171062.1. NM_001177591.1. [P63151-2 ]
    NP_002708.1. NM_002717.3. [P63151-1 ]
    UniGenei Hs.146339.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DW8 X-ray 2.85 B/E 1-447 [» ]
    ProteinModelPortali P63151.
    SMRi P63151. Positions 8-446.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111512. 53 interactions.
    DIPi DIP-29398N.
    IntActi P63151. 18 interactions.
    MINTi MINT-2835351.
    STRINGi 9606.ENSP00000370113.

    Chemistry

    BindingDBi P63151.
    ChEMBLi CHEMBL4284.

    PTM databases

    PhosphoSitei P63151.

    Polymorphism databases

    DMDMi 52783535.

    Proteomic databases

    MaxQBi P63151.
    PaxDbi P63151.
    PeptideAtlasi P63151.
    PRIDEi P63151.

    Protocols and materials databases

    DNASUi 5520.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315985 ; ENSP00000325074 ; ENSG00000221914 . [P63151-2 ]
    ENST00000380737 ; ENSP00000370113 ; ENSG00000221914 . [P63151-1 ]
    GeneIDi 5520.
    KEGGi hsa:5520.
    UCSCi uc003xeu.3. human. [P63151-1 ]
    uc011laf.2. human. [P63151-2 ]

    Organism-specific databases

    CTDi 5520.
    GeneCardsi GC08P026204.
    HGNCi HGNC:9304. PPP2R2A.
    HPAi HPA042122.
    HPA042770.
    MIMi 604941. gene.
    neXtProti NX_P63151.
    PharmGKBi PA33668.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5170.
    HOGENOMi HOG000089745.
    HOVERGENi HBG000012.
    InParanoidi P63151.
    KOi K04354.
    OMAi QRNMAGA.
    OrthoDBi EOG7Q5HCZ.
    PhylomeDBi P63151.
    TreeFami TF105553.

    Enzyme and pathway databases

    Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_821. Cyclin D associated events in G1.
    SignaLinki P63151.

    Miscellaneous databases

    ChiTaRSi PPP2R2A. human.
    EvolutionaryTracei P63151.
    GeneWikii PPP2R2A.
    GenomeRNAii 5520.
    NextBioi 21352.
    PROi P63151.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63151.
    Bgeei P63151.
    CleanExi HS_PPP2R2A.
    Genevestigatori P63151.

    Family and domain databases

    Gene3Di 2.130.10.10. 3 hits.
    InterProi IPR000009. PP2A_PR55.
    IPR018067. PP2A_PR55_CS.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR11871. PTHR11871. 1 hit.
    PIRSFi PIRSF037309. PP2A_PR55. 1 hit.
    PRINTSi PR00600. PP2APR55.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 3 hits.
    PROSITEi PS01024. PR55_1. 1 hit.
    PS01025. PR55_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform."
      Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., Merlevede W., Hofsteenge J., Hemmings B.A.
      Biochemistry 30:3589-3597(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Lung fibroblast.
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Trachea.
    3. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Blood.
    6. "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55."
      Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.
      EMBO J. 26:402-411(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry namei2ABA_HUMAN
    AccessioniPrimary (citable) accession number: P63151
    Secondary accession number(s): B2RBU8
    , B4E1T7, P50409, Q00007
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 112 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 8
      Human chromosome 8: 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