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Q9H8E8

- CSR2B_HUMAN

UniProt

Q9H8E8 - CSR2B_HUMAN

Protein

Cysteine-rich protein 2-binding protein

Gene

CSRP2BP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle.1 Publication

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: MGI
    2. LIM domain binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. embryo development Source: Ensembl
    3. G2/M transition of mitotic cell cycle Source: Ensembl
    4. histone H3 acetylation Source: BHF-UCL

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine-rich protein 2-binding protein
    Short name:
    CSRP2-binding protein
    Alternative name(s):
    ADA2A-containing complex subunit 2
    Short name:
    ATAC2
    CRP2-binding partner
    Short name:
    CRP2BP
    Gene namesi
    Name:CSRP2BP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15904. CSRP2BP.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Mainly nuclear.

    GO - Cellular componenti

    1. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26969.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 782782Cysteine-rich protein 2-binding proteinPRO_0000074603Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei231 – 2311N6-acetyllysineBy similarity
    Modified residuei292 – 2921N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9H8E8.
    PaxDbiQ9H8E8.
    PRIDEiQ9H8E8.

    PTM databases

    PhosphoSiteiQ9H8E8.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, heart, lung, placenta, brain, liver, pancreas and kidney. High expression in skeletal muscle and heart. Lower expression in lung.

    Gene expression databases

    ArrayExpressiQ9H8E8.
    BgeeiQ9H8E8.
    CleanExiHS_CSRP2BP.
    GenevestigatoriQ9H8E8.

    Organism-specific databases

    HPAiCAB034224.

    Interactioni

    Subunit structurei

    Interacts with the LIM 1 domain of CSRP2. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, MBIP and WDR5.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MBIPQ9NS733EBI-750907,EBI-741953

    Protein-protein interaction databases

    BioGridi121485. 6 interactions.
    IntActiQ9H8E8. 5 interactions.
    MINTiMINT-1479938.
    STRINGi9606.ENSP00000278816.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H8E8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini638 – 782145N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG295186.
    HOGENOMiHOG000230880.
    HOVERGENiHBG051142.
    InParanoidiQ9H8E8.
    OMAiKEDICAF.
    OrthoDBiEOG7M6D6R.
    PhylomeDBiQ9H8E8.
    TreeFamiTF324809.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H8E8-1) [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

    MDSSIHLSSL ISRHDDEATR TSTSEGLEEG EVEGETLLIV ESEDQASVDL    50
    SHDQSGDSLN SDEGDVSWME EQLSYFCDKC QKWIPASQLR EQLSYLKGDN 100
    FFRFTCSDCS ADGKEQYERL KLTWQQVVML AMYNLSLEGS GRQGYFRWKE 150
    DICAFIEKHW TFLLGNRKKT STWWSTVAGC LSVGSPMYFR SGAQEFGEPG 200
    WWKLVHNKPP TMKPEGEKLS ASTLKIKAAS KPTLDPIITV EGLRKRASRN 250
    PVESAMELKE KRSRTQEAKD IRRAQKEAAG FLDRSTSSTP VKFISRGRRP 300
    DVILEKGEVI DFSSLSSSDR TPLTSPSPSP SLDFSAPGTP ASHSATPSLL 350
    SEADLIPDVM PPQALFHDDD EMEGDGVIDP GMEYVPPPAG SVASGPVVGV 400
    RKKVRGPEQI KQEVESEEEK PDRMDIDSED TDSNTSLQTR AREKRKPQLE 450
    KDTKPKEPRY TPVSIYEEKL LLKRLEACPG AVAMTPEARR LKRKLIVRQA 500
    KRDRGLPLFD LDQVVNAALL LVDGIYGAKE GGISRLPAGQ ATYRTTCQDF 550
    RILDRYQTSL PSRKGFRHQT TKFLYRLVGS EDMAVDQSIV SPYTSRILKP 600
    YIRRDYETKP PKLQLLSQIR SHLHRSDPHW TPEPDAPLDY CYVRPNHIPT 650
    INSMCQEFFW PGIDLSECLQ YPDFSVVVLY KKVIIAFGFM VPDVKYNEAY 700
    ISFLFVHPEW RRAGIATFMI YHLIQTCMGK DVTLHVSASN PAMLLYQKFG 750
    FKTEEYVLDF YDKYYPLEST ECKHAFFLRL RR 782
    Length:782
    Mass (Da):88,844
    Last modified:October 5, 2010 - v3
    Checksum:iE84FAEF06412EA77
    GO
    Isoform 2 (identifier: Q9H8E8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-128: Missing.

    Note: May be due to an intron retention.

    Show »
    Length:654
    Mass (Da):74,324
    Checksum:i2EA7F2981E7D4195
    GO

    Sequence cautioni

    The sequence CAB56651.2 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti535 – 5351R → G in BAB14669. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141P → L.
    Corresponds to variant rs6081011 [ dbSNP | Ensembl ].
    VAR_028034
    Natural varianti400 – 4001V → G.2 Publications
    Corresponds to variant rs1205193 [ dbSNP | Ensembl ].
    VAR_028035
    Natural varianti442 – 4421R → T.
    Corresponds to variant rs2295182 [ dbSNP | Ensembl ].
    VAR_020466
    Natural varianti600 – 6001P → R.
    Corresponds to variant rs11557577 [ dbSNP | Ensembl ].
    VAR_033839
    Natural varianti738 – 7381A → S.
    Corresponds to variant rs6081027 [ dbSNP | Ensembl ].
    VAR_048166

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 128128Missing in isoform 2. 2 PublicationsVSP_000070Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK023759 mRNA. Translation: BAB14669.1.
    AL050321 Genomic DNA. Translation: CAB56651.2. Sequence problems.
    AL050321 Genomic DNA. Translation: CAM28294.1.
    CH471133 Genomic DNA. Translation: EAX10255.1.
    BC007537 mRNA. Translation: AAH07537.1.
    BC009174 mRNA. No translation available.
    AF252257 mRNA. Translation: AAG10249.1.
    CCDSiCCDS13133.1. [Q9H8E8-1]
    RefSeqiNP_065397.3. NM_020536.4.
    UniGeneiHs.488051.
    Hs.728790.

    Genome annotation databases

    EnsembliENST00000435364; ENSP00000392318; ENSG00000149474. [Q9H8E8-1]
    ENST00000489634; ENSP00000425909; ENSG00000149474. [Q9H8E8-2]
    GeneIDi57325.
    KEGGihsa:57325.
    UCSCiuc002wqk.3. human. [Q9H8E8-1]

    Polymorphism databases

    DMDMi308153608.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK023759 mRNA. Translation: BAB14669.1 .
    AL050321 Genomic DNA. Translation: CAB56651.2 . Sequence problems.
    AL050321 Genomic DNA. Translation: CAM28294.1 .
    CH471133 Genomic DNA. Translation: EAX10255.1 .
    BC007537 mRNA. Translation: AAH07537.1 .
    BC009174 mRNA. No translation available.
    AF252257 mRNA. Translation: AAG10249.1 .
    CCDSi CCDS13133.1. [Q9H8E8-1 ]
    RefSeqi NP_065397.3. NM_020536.4.
    UniGenei Hs.488051.
    Hs.728790.

    3D structure databases

    ProteinModelPortali Q9H8E8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121485. 6 interactions.
    IntActi Q9H8E8. 5 interactions.
    MINTi MINT-1479938.
    STRINGi 9606.ENSP00000278816.

    PTM databases

    PhosphoSitei Q9H8E8.

    Polymorphism databases

    DMDMi 308153608.

    Proteomic databases

    MaxQBi Q9H8E8.
    PaxDbi Q9H8E8.
    PRIDEi Q9H8E8.

    Protocols and materials databases

    DNASUi 57325.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000435364 ; ENSP00000392318 ; ENSG00000149474 . [Q9H8E8-1 ]
    ENST00000489634 ; ENSP00000425909 ; ENSG00000149474 . [Q9H8E8-2 ]
    GeneIDi 57325.
    KEGGi hsa:57325.
    UCSCi uc002wqk.3. human. [Q9H8E8-1 ]

    Organism-specific databases

    CTDi 57325.
    GeneCardsi GC20P018066.
    HGNCi HGNC:15904. CSRP2BP.
    HPAi CAB034224.
    neXtProti NX_Q9H8E8.
    PharmGKBi PA26969.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295186.
    HOGENOMi HOG000230880.
    HOVERGENi HBG051142.
    InParanoidi Q9H8E8.
    OMAi KEDICAF.
    OrthoDBi EOG7M6D6R.
    PhylomeDBi Q9H8E8.
    TreeFami TF324809.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    GeneWikii CSRP2BP.
    NextBioi 63428.
    PROi Q9H8E8.

    Gene expression databases

    ArrayExpressi Q9H8E8.
    Bgeei Q9H8E8.
    CleanExi HS_CSRP2BP.
    Genevestigatori Q9H8E8.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view ]
    Pfami PF00583. Acetyltransf_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51186. GNAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 2), VARIANT GLY-400.
      Tissue: Placenta.
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2), VARIANT GLY-400.
      Tissue: Eye and Placenta.
    5. "The cysteine- and glycine-rich LIM domain protein CRP2 specifically interacts with a novel human protein."
      Weiskirchen R., Gressner A.M.
      Biochem. Biophys. Res. Commun. 274:655-663(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 546-782, INTERACTION WITH CSRP2.
      Tissue: Kidney.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
      Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
      Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
    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-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCSR2B_HUMAN
    AccessioniPrimary (citable) accession number: Q9H8E8
    Secondary accession number(s): A2A2I5
    , Q96GW6, Q96IH3, Q9HBF0, Q9UIY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 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 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3