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O15042

- SR140_HUMAN

UniProt

O15042 - SR140_HUMAN

Protein

U2 snRNP-associated SURP motif-containing protein

Gene

U2SURP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. RNA processing Source: InterPro

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U2 snRNP-associated SURP motif-containing protein
    Alternative name(s):
    140 kDa Ser/Arg-rich domain protein
    U2-associated protein SR140
    Gene namesi
    Name:U2SURP
    Synonyms:KIAA0332, SR140
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:30855. U2SURP.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10291028U2 snRNP-associated SURP motif-containing proteinPRO_0000280070Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei202 – 2021Phosphoserine1 Publication
    Modified residuei485 – 4851Phosphoserine2 Publications
    Modified residuei760 – 7601N6-acetyllysine1 Publication
    Modified residuei788 – 7881Phosphoserine3 Publications
    Modified residuei800 – 8001Phosphoserine2 Publications
    Modified residuei811 – 8111Phosphoserine3 Publications
    Modified residuei931 – 9311Phosphothreonine1 Publication
    Modified residuei946 – 9461Phosphoserine1 Publication
    Modified residuei948 – 9481Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO15042.
    PaxDbiO15042.
    PRIDEiO15042.

    PTM databases

    PhosphoSiteiO15042.

    Miscellaneous databases

    PMAP-CutDBO15042.

    Expressioni

    Gene expression databases

    ArrayExpressiO15042.
    BgeeiO15042.
    GenevestigatoriO15042.

    Organism-specific databases

    HPAiHPA037545.

    Interactioni

    Subunit structurei

    Interacts with ERBB4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RBM10P981752EBI-310697,EBI-721525
    RBM5P527562EBI-310697,EBI-714003

    Protein-protein interaction databases

    BioGridi116932. 32 interactions.
    IntActiO15042. 18 interactions.
    MINTiMINT-2795506.

    Structurei

    3D structure databases

    ProteinModelPortaliO15042.
    SMRiO15042. Positions 276-353, 538-675.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini274 – 35582RRMPROSITE-ProRule annotationAdd
    BLAST
    Repeati430 – 47344SURP motifAdd
    BLAST
    Domaini534 – 679146CIDPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili92 – 12130Sequence AnalysisAdd
    BLAST
    Coiled coili192 – 23241Sequence AnalysisAdd
    BLAST
    Coiled coili837 – 91579Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi357 – 40246Pro-richAdd
    BLAST
    Compositional biasi689 – 74658Asp-richAdd
    BLAST
    Compositional biasi762 – 917156Glu-richAdd
    BLAST
    Compositional biasi922 – 100180Arg/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the splicing factor SR family.Curated
    Contains 1 CID domain.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation
    Contains 1 SURP motif repeat.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG307351.
    HOGENOMiHOG000286037.
    HOVERGENiHBG093996.
    InParanoidiO15042.
    KOiK12842.
    OMAiANSPTKW.
    OrthoDBiEOG74FF05.
    PhylomeDBiO15042.
    TreeFamiTF318729.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR006569. CID_dom.
    IPR008942. ENTH_VHS.
    IPR013170. mRNA_splic_Cwf21.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR000061. Surp.
    [Graphical view]
    PfamiPF08312. cwf21. 1 hit.
    PF00076. RRM_1. 1 hit.
    PF01805. Surp. 1 hit.
    [Graphical view]
    SMARTiSM00582. RPR. 1 hit.
    SM00360. RRM. 1 hit.
    SM00648. SWAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF109905. SSF109905. 1 hit.
    SSF48464. SSF48464. 1 hit.
    PROSITEiPS51391. CID. 1 hit.
    PS50102. RRM. 1 hit.
    PS50128. SURP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15042-1) [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

    MADKTPGGSQ KASSKTRSSD VHSSGSSDAH MDASGPSDSD MPSRTRPKSP     50
    RKHNYRNESA RESLCDSPHQ NLSRPLLENK LKAFSIGKMS TAKRTLSKKE 100
    QEELKKKEDE KAAAEIYEEF LAAFEGSDGN KVKTFVRGGV VNAAKEEHET 150
    DEKRGKIYKP SSRFADQKNP PNQSSNERPP SLLVIETKKP PLKKGEKEKK 200
    KSNLELFKEE LKQIQEERDE RHKTKGRLSR FEPPQSDSDG QRRSMDAPSR 250
    RNRSSGVLDD YAPGSHDVGD PSTTNLYLGN INPQMNEEML CQEFGRFGPL 300
    ASVKIMWPRT DEERARERNC GFVAFMNRRD AERALKNLNG KMIMSFEMKL 350
    GWGKAVPIPP HPIYIPPSMM EHTLPPPPSG LPFNAQPRER LKNPNAPMLP 400
    PPKNKEDFEK TLSQAIVKVV IPTERNLLAL IHRMIEFVVR EGPMFEAMIM 450
    NREINNPMFR FLFENQTPAH VYYRWKLYSI LQGDSPTKWR TEDFRMFKNG 500
    SFWRPPPLNP YLHGMSEEQE TEAFVEEPSK KGALKEEQRD KLEEILRGLT 550
    PRKNDIGDAM VFCLNNAEAA EEIVDCITES LSILKTPLPK KIARLYLVSD 600
    VLYNSSAKVA NASYYRKFFE TKLCQIFSDL NATYRTIQGH LQSENFKQRV 650
    MTCFRAWEDW AIYPEPFLIK LQNIFLGLVN IIEEKETEDV PDDLDGAPIE 700
    EELDGAPLED VDGIPIDATP IDDLDGVPIK SLDDDLDGVP LDATEDSKKN 750
    EPIFKVAPSK WEAVDESELE AQAVTTSKWE LFDQHEESEE EENQNQEEES 800
    EDEEDTQSSK SEEHHLYSNP IKEEMTESKF SKYSEMSEEK RAKLREIELK 850
    VMKFQDELES GKRPKKPGQS FQEQVEHYRD KLLQREKEKE LERERERDKK 900
    DKEKLESRSK DKKEKDECTP TRKERKRRHS TSPSPSRSSS GRRVKSPSPK 950
    SERSERSERS HKESSRSRSS HKDSPRDVSK KAKRSPSGSR TPKRSRRSRS 1000
    RSPKKSGKKS RSQSRSPHRS HKKSKKNKH 1029
    Length:1,029
    Mass (Da):118,292
    Last modified:March 6, 2007 - v2
    Checksum:i7AB9235C63299714
    GO
    Isoform 2 (identifier: O15042-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,028
    Mass (Da):118,235
    Checksum:i626B4D73CC24A992
    GO
    Isoform 3 (identifier: O15042-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-409: Missing.
         410-424: KTLSQAIVKVVIPTE → MLLCYRHLKTKRILR

    Show »
    Length:620
    Mass (Da):72,523
    Checksum:iBA78B39559885CBC
    GO

    Sequence cautioni

    The sequence AAH16323.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAI05605.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 409409Missing in isoform 3. 1 PublicationVSP_023522Add
    BLAST
    Alternative sequencei256 – 2561Missing in isoform 2. 1 PublicationVSP_023523
    Alternative sequencei410 – 42415KTLSQ…VIPTE → MLLCYRHLKTKRILR in isoform 3. 1 PublicationVSP_023524Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC018450 Genomic DNA. No translation available.
    AC026304 Genomic DNA. No translation available.
    BC006474 mRNA. Translation: AAH06474.1.
    BC016323 mRNA. Translation: AAH16323.1. Sequence problems.
    BC105604 mRNA. Translation: AAI05605.1. Sequence problems.
    BC111692 mRNA. Translation: AAI11693.1.
    AB002330 mRNA. Translation: BAA20790.1.
    BK000564 mRNA. Translation: DAA00075.1.
    CCDSiCCDS46928.1. [O15042-1]
    RefSeqiNP_001073884.1. NM_001080415.1. [O15042-1]
    XP_005247303.1. XM_005247246.2. [O15042-2]
    XP_005247306.1. XM_005247249.2. [O15042-3]
    UniGeneiHs.596572.

    Genome annotation databases

    EnsembliENST00000473835; ENSP00000418563; ENSG00000163714. [O15042-1]
    GeneIDi23350.
    KEGGihsa:23350.
    UCSCiuc003evh.1. human. [O15042-1]
    uc003evi.1. human. [O15042-3]
    uc003evk.1. human. [O15042-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC018450 Genomic DNA. No translation available.
    AC026304 Genomic DNA. No translation available.
    BC006474 mRNA. Translation: AAH06474.1 .
    BC016323 mRNA. Translation: AAH16323.1 . Sequence problems.
    BC105604 mRNA. Translation: AAI05605.1 . Sequence problems.
    BC111692 mRNA. Translation: AAI11693.1 .
    AB002330 mRNA. Translation: BAA20790.1 .
    BK000564 mRNA. Translation: DAA00075.1 .
    CCDSi CCDS46928.1. [O15042-1 ]
    RefSeqi NP_001073884.1. NM_001080415.1. [O15042-1 ]
    XP_005247303.1. XM_005247246.2. [O15042-2 ]
    XP_005247306.1. XM_005247249.2. [O15042-3 ]
    UniGenei Hs.596572.

    3D structure databases

    ProteinModelPortali O15042.
    SMRi O15042. Positions 276-353, 538-675.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116932. 32 interactions.
    IntActi O15042. 18 interactions.
    MINTi MINT-2795506.

    PTM databases

    PhosphoSitei O15042.

    Proteomic databases

    MaxQBi O15042.
    PaxDbi O15042.
    PRIDEi O15042.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000473835 ; ENSP00000418563 ; ENSG00000163714 . [O15042-1 ]
    GeneIDi 23350.
    KEGGi hsa:23350.
    UCSCi uc003evh.1. human. [O15042-1 ]
    uc003evi.1. human. [O15042-3 ]
    uc003evk.1. human. [O15042-2 ]

    Organism-specific databases

    CTDi 23350.
    GeneCardsi GC03P142720.
    H-InvDB HIX0003746.
    HGNCi HGNC:30855. U2SURP.
    HPAi HPA037545.
    neXtProti NX_O15042.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307351.
    HOGENOMi HOG000286037.
    HOVERGENi HBG093996.
    InParanoidi O15042.
    KOi K12842.
    OMAi ANSPTKW.
    OrthoDBi EOG74FF05.
    PhylomeDBi O15042.
    TreeFami TF318729.

    Miscellaneous databases

    ChiTaRSi u2surp. human.
    GenomeRNAii 23350.
    NextBioi 45335.
    PMAP-CutDB O15042.
    PROi O15042.

    Gene expression databases

    ArrayExpressi O15042.
    Bgeei O15042.
    Genevestigatori O15042.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR006569. CID_dom.
    IPR008942. ENTH_VHS.
    IPR013170. mRNA_splic_Cwf21.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR000061. Surp.
    [Graphical view ]
    Pfami PF08312. cwf21. 1 hit.
    PF00076. RRM_1. 1 hit.
    PF01805. Surp. 1 hit.
    [Graphical view ]
    SMARTi SM00582. RPR. 1 hit.
    SM00360. RRM. 1 hit.
    SM00648. SWAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109905. SSF109905. 1 hit.
    SSF48464. SSF48464. 1 hit.
    PROSITEi PS51391. CID. 1 hit.
    PS50102. RRM. 1 hit.
    PS50128. SURP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1029 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-189 (ISOFORMS 1/2).
      Tissue: Lung and Urinary bladder.
    3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1029 (ISOFORM 1).
      Tissue: Brain.
    4. "Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein."
      Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.
      EMBO J. 21:4978-4988(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
    5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND SER-800, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-788 AND SER-800, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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 LYS-760, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
      Gilmore-Hebert M., Ramabhadran R., Stern D.F.
      Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
    10. "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-485; SER-811; THR-931; SER-946 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-202; SER-485; SER-788 AND SER-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSR140_HUMAN
    AccessioniPrimary (citable) accession number: O15042
    Secondary accession number(s): A0PJ60
    , Q0D2M1, Q2NKQ7, Q9BR70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 106 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3