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Q16514

- TAF12_HUMAN

UniProt

Q16514 - TAF12_HUMAN

Protein

Transcription initiation factor TFIID subunit 12

Gene

TAF12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. transcription coactivator activity Source: UniProtKB
    4. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. DNA-templated transcription, initiation Source: UniProtKB
    3. gene expression Source: Reactome
    4. histone H3 acetylation Source: UniProtKB
    5. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    6. regulation of RNA biosynthetic process Source: GOC
    7. transcription elongation from RNA polymerase II promoter Source: Reactome
    8. transcription from RNA polymerase II promoter Source: Reactome
    9. transcription initiation from RNA polymerase II promoter Source: UniProtKB
    10. viral process Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_172610. HATs acetylate histones.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_6233. Transcription of the HIV genome.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6332. HIV Transcription Initiation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription initiation factor TFIID subunit 12
    Alternative name(s):
    Transcription initiation factor TFIID 20/15 kDa subunits
    Short name:
    TAFII-20/TAFII-15
    Short name:
    TAFII20/TAFII15
    Gene namesi
    Name:TAF12
    Synonyms:TAF15, TAF2J, TAFII20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11545. TAF12.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. PCAF complex Source: UniProtKB
    3. STAGA complex Source: UniProtKB
    4. transcription factor TFIID complex Source: MGI
    5. transcription factor TFTC complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36320.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 161161Transcription initiation factor TFIID subunit 12PRO_0000033580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431Phosphothreonine1 Publication
    Modified residuei51 – 511Phosphoserine3 Publications
    Modified residuei59 – 591Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ16514.
    PaxDbiQ16514.
    PRIDEiQ16514.

    PTM databases

    PhosphoSiteiQ16514.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    BgeeiQ16514.
    CleanExiHS_TAF12.
    HS_TAF15.
    GenevestigatoriQ16514.

    Organism-specific databases

    HPAiHPA008519.

    Interactioni

    Subunit structurei

    TFIID and PCAF are composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TBP is not part of TFTC. Interacts directly with TBP; additional interactions between TAFII20 and TAFII28 or TAFII30 were detected. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L/PAF65-beta, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, STAF65-gamma/KIAA0764, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Interacts (isoform TAFII15 and isoform TAFII20) with ATF7 (via the transactivation domain); the interaction is prevented by sumoylation of ATF7 and promotes (isoform TAFII20 only) the transactivation of ATF7.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TAF1CQ155722EBI-1034238,EBI-2510659
    TBPP202262EBI-1034238,EBI-355371

    Protein-protein interaction databases

    BioGridi112746. 25 interactions.
    DIPiDIP-496N.
    IntActiQ16514. 6 interactions.
    MINTiMINT-3032603.
    STRINGi9606.ENSP00000263974.

    Structurei

    Secondary structure

    1
    161
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi60 – 7011
    Helixi78 – 10528
    Helixi113 – 12311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H3OX-ray2.30B/D57-128[»]
    ProteinModelPortaliQ16514.
    SMRiQ16514. Positions 55-128.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16514.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TAF12 family.Curated
    Contains 1 histone-fold domain.Curated

    Phylogenomic databases

    eggNOGiCOG5624.
    HOGENOMiHOG000035092.
    HOVERGENiHBG055174.
    InParanoidiQ16514.
    KOiK03126.
    OMAiMHSLHEN.
    OrthoDBiEOG769ZMW.
    PhylomeDBiQ16514.
    TreeFamiTF323652.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR003228. TFIID_sub.
    [Graphical view]
    PfamiPF03847. TFIID_20kDa. 1 hit.
    [Graphical view]
    ProDomiPD012998. PD012998. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF47113. SSF47113. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform TAFII20 (identifier: Q16514-1) [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

    MNQFGPSALI NLSNFSSIKP EPASTPPQGS MANSTAVVKI PGTPGAGGRL    50
    SPENNQVLTK KKLQDLVREV DPNEQLDEDV EEMLLQIADD FIESVVTAAC 100
    QLARHRKSST LEVKDVQLHL ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ 150
    RMALIRKTTK K 161
    Length:161
    Mass (Da):17,924
    Last modified:November 1, 1996 - v1
    Checksum:i054B017CD7BF99CE
    GO
    Isoform TAFII15 (identifier: Q16514-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: Missing.

    Show »
    Length:131
    Mass (Da):14,825
    Checksum:i655B769918311CE1
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3030Missing in isoform TAFII15. 1 PublicationVSP_018888Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57693 mRNA. Translation: AAC50600.1.
    U57693 mRNA. Translation: AAC50601.1.
    D50544 mRNA. Translation: BAA09112.1.
    X84002 mRNA. Translation: CAA58826.1.
    BT007031 mRNA. Translation: AAP35678.1.
    AY206865 Genomic DNA. Translation: AAO13491.1.
    AL513497 Genomic DNA. Translation: CAI22291.1.
    CH471059 Genomic DNA. Translation: EAX07682.1.
    CH471059 Genomic DNA. Translation: EAX07683.1.
    BC011986 mRNA. Translation: AAH11986.1.
    CCDSiCCDS326.1. [Q16514-1]
    PIRiJC4676.
    RefSeqiNP_001128690.1. NM_001135218.1. [Q16514-1]
    NP_005635.1. NM_005644.3. [Q16514-1]
    XP_006710924.1. XM_006710861.1. [Q16514-1]
    UniGeneiHs.530251.

    Genome annotation databases

    EnsembliENST00000263974; ENSP00000263974; ENSG00000120656. [Q16514-1]
    ENST00000373824; ENSP00000362930; ENSG00000120656. [Q16514-1]
    GeneIDi6883.
    KEGGihsa:6883.
    UCSCiuc001bqx.3. human. [Q16514-1]

    Polymorphism databases

    DMDMi3024708.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57693 mRNA. Translation: AAC50600.1 .
    U57693 mRNA. Translation: AAC50601.1 .
    D50544 mRNA. Translation: BAA09112.1 .
    X84002 mRNA. Translation: CAA58826.1 .
    BT007031 mRNA. Translation: AAP35678.1 .
    AY206865 Genomic DNA. Translation: AAO13491.1 .
    AL513497 Genomic DNA. Translation: CAI22291.1 .
    CH471059 Genomic DNA. Translation: EAX07682.1 .
    CH471059 Genomic DNA. Translation: EAX07683.1 .
    BC011986 mRNA. Translation: AAH11986.1 .
    CCDSi CCDS326.1. [Q16514-1 ]
    PIRi JC4676.
    RefSeqi NP_001128690.1. NM_001135218.1. [Q16514-1 ]
    NP_005635.1. NM_005644.3. [Q16514-1 ]
    XP_006710924.1. XM_006710861.1. [Q16514-1 ]
    UniGenei Hs.530251.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H3O X-ray 2.30 B/D 57-128 [» ]
    ProteinModelPortali Q16514.
    SMRi Q16514. Positions 55-128.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112746. 25 interactions.
    DIPi DIP-496N.
    IntActi Q16514. 6 interactions.
    MINTi MINT-3032603.
    STRINGi 9606.ENSP00000263974.

    PTM databases

    PhosphoSitei Q16514.

    Polymorphism databases

    DMDMi 3024708.

    Proteomic databases

    MaxQBi Q16514.
    PaxDbi Q16514.
    PRIDEi Q16514.

    Protocols and materials databases

    DNASUi 6883.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263974 ; ENSP00000263974 ; ENSG00000120656 . [Q16514-1 ]
    ENST00000373824 ; ENSP00000362930 ; ENSG00000120656 . [Q16514-1 ]
    GeneIDi 6883.
    KEGGi hsa:6883.
    UCSCi uc001bqx.3. human. [Q16514-1 ]

    Organism-specific databases

    CTDi 6883.
    GeneCardsi GC01M028915.
    HGNCi HGNC:11545. TAF12.
    HPAi HPA008519.
    MIMi 600773. gene.
    neXtProti NX_Q16514.
    PharmGKBi PA36320.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5624.
    HOGENOMi HOG000035092.
    HOVERGENi HBG055174.
    InParanoidi Q16514.
    KOi K03126.
    OMAi MHSLHEN.
    OrthoDBi EOG769ZMW.
    PhylomeDBi Q16514.
    TreeFami TF323652.

    Enzyme and pathway databases

    Reactomei REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_172610. HATs acetylate histones.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_6233. Transcription of the HIV genome.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6332. HIV Transcription Initiation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

    Miscellaneous databases

    EvolutionaryTracei Q16514.
    GeneWikii TAF12.
    GenomeRNAii 6883.
    NextBioi 26891.
    PROi Q16514.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16514.
    CleanExi HS_TAF12.
    HS_TAF15.
    Genevestigatori Q16514.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR003228. TFIID_sub.
    [Graphical view ]
    Pfami PF03847. TFIID_20kDa. 1 hit.
    [Graphical view ]
    ProDomi PD012998. PD012998. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20).
    2. "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation."
      Hoffmann A., Roeder R.G.
      J. Biol. Chem. 271:18194-18202(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAFII15 AND TAFII20).
    3. "Isolation and characterization of a cDNA encoding a novel human transcription factor TFIID subunit containing similarities with histones H2B and H3."
      Choi B., Bando M., Hasegawa S., Horikoshi M.
      Gene 169:263-267(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20).
    4. "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID."
      Mengus G., May M., Jacq X., Staub A., Tora L., Chambon P., Davidson I.
      EMBO J. 14:1520-1531(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20), PARTIAL PROTEIN SEQUENCE.
    5. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAFII20).
    6. NIEHS SNPs program
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 TAFII20).
      Tissue: Lung.
    10. Cited for: PROTEIN SEQUENCE OF 50-60 AND 115-122, SUBUNIT, SUBCELLULAR LOCATION.
    11. "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
      Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
      Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SF3B3; GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10 AND TAF9, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily."
      Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J., Nakatani Y.
      Mol. Cell 2:869-875(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; SUPT3H; TAF6L; TAF10; TRRAP AND TAF9.
    13. "A functional interaction between ATF7 and TAF12 that is modulated by TAF4."
      Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C., Chatton B.
      Oncogene 24:3472-3483(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7.
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND THR-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs."
      Gangloff Y.-G., Werten S., Romier C., Carre L., Poch O., Moras D., Davidson I.
      Mol. Cell. Biol. 20:340-351(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 57-128 IN COMPLEX WITH TAF4.

    Entry informationi

    Entry nameiTAF12_HUMAN
    AccessioniPrimary (citable) accession number: Q16514
    Secondary accession number(s): D3DPM5, Q15775, Q5T077
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 155 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 1
      Human chromosome 1: 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