Q9H8E8 (CSR2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CSRP2BP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	782 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7
Subunit structure	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. Ref.5 Ref.7
Subcellular location	Nucleus. Cytoplasm. Note: Mainly nuclear.
Tissue specificity	Expressed in skeletal muscle, heart, lung, placenta, brain, liver, pancreas and kidney. High expression in skeletal muscle and heart. Lower expression in lung.
Sequence similarities	Contains 1 N-acetyltransferase domain.
Sequence caution	The sequence CAB56651.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle process Inferred from electronic annotation. Source: Compara embryo development Inferred from electronic annotation. Source: Compara histone H3 acetylation Inferred from direct assay PubMed 18838386. Source: BHF-UCL
Cellular_component	Ada2/Gcn5/Ada3 transcription activator complex Inferred from direct assay PubMed 18838386. Source: BHF-UCL cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	LIM domain binding Non-traceable author statement Ref.5. Source: UniProtKB histone acetyltransferase activity Inferred from direct assay Ref.7. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MBIP	Q9NS73	3	EBI-750907,EBI-741953

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H8E8-1)

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.

Isoform 2 (identifier: Q9H8E8-2)

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

Note: May be due to an intron retention.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 782	782	Cysteine-rich protein 2-binding protein		PRO_0000074603
Regions
	Domain	638 – 782	145	N-acetyltransferase
Amino acid modifications
	Modified residue	292	1	N6-acetyllysine Ref.8
Natural variations
	Alternative sequence	1 – 128	128	Missing in isoform 2.		VSP_000070
	Natural variant	214	1	P → L. Corresponds to variant rs6081011 [ dbSNP | Ensembl ].		VAR_028034
	Natural variant	400	1	V → G. Ref.1 Ref.4 Corresponds to variant rs1205193 [ dbSNP | Ensembl ].		VAR_028035
	Natural variant	442	1	R → T. Corresponds to variant rs2295182 [ dbSNP | Ensembl ].		VAR_020466
	Natural variant	600	1	P → R. Corresponds to variant rs11557577 [ dbSNP | Ensembl ].		VAR_033839
	Natural variant	738	1	A → S. Corresponds to variant rs6081027 [ dbSNP | Ensembl ].		VAR_048166
Experimental info
	Sequence conflict	535	1	R → G in BAB14669. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: E84FAEF06412EA77	FASTA	782	88,844
	10 20 30 40 50 60 MDSSIHLSSL ISRHDDEATR TSTSEGLEEG EVEGETLLIV ESEDQASVDL SHDQSGDSLN 70 80 90 100 110 120 SDEGDVSWME EQLSYFCDKC QKWIPASQLR EQLSYLKGDN FFRFTCSDCS ADGKEQYERL 130 140 150 160 170 180 KLTWQQVVML AMYNLSLEGS GRQGYFRWKE DICAFIEKHW TFLLGNRKKT STWWSTVAGC 190 200 210 220 230 240 LSVGSPMYFR SGAQEFGEPG WWKLVHNKPP TMKPEGEKLS ASTLKIKAAS KPTLDPIITV 250 260 270 280 290 300 EGLRKRASRN PVESAMELKE KRSRTQEAKD IRRAQKEAAG FLDRSTSSTP VKFISRGRRP 310 320 330 340 350 360 DVILEKGEVI DFSSLSSSDR TPLTSPSPSP SLDFSAPGTP ASHSATPSLL SEADLIPDVM 370 380 390 400 410 420 PPQALFHDDD EMEGDGVIDP GMEYVPPPAG SVASGPVVGV RKKVRGPEQI KQEVESEEEK 430 440 450 460 470 480 PDRMDIDSED TDSNTSLQTR AREKRKPQLE KDTKPKEPRY TPVSIYEEKL LLKRLEACPG 490 500 510 520 530 540 AVAMTPEARR LKRKLIVRQA KRDRGLPLFD LDQVVNAALL LVDGIYGAKE GGISRLPAGQ 550 560 570 580 590 600 ATYRTTCQDF RILDRYQTSL PSRKGFRHQT TKFLYRLVGS EDMAVDQSIV SPYTSRILKP 610 620 630 640 650 660 YIRRDYETKP PKLQLLSQIR SHLHRSDPHW TPEPDAPLDY CYVRPNHIPT INSMCQEFFW 670 680 690 700 710 720 PGIDLSECLQ YPDFSVVVLY KKVIIAFGFM VPDVKYNEAY ISFLFVHPEW RRAGIATFMI 730 740 750 760 770 780 YHLIQTCMGK DVTLHVSASN PAMLLYQKFG FKTEEYVLDF YDKYYPLEST ECKHAFFLRL RR
	Isoform 2 [UniParc]. Checksum: 2EA7F2981E7D4195	FASTA	654	74,324
	10 20 30 40 50 60 MLAMYNLSLE GSGRQGYFRW KEDICAFIEK HWTFLLGNRK KTSTWWSTVA GCLSVGSPMY 70 80 90 100 110 120 FRSGAQEFGE PGWWKLVHNK PPTMKPEGEK LSASTLKIKA ASKPTLDPII TVEGLRKRAS 130 140 150 160 170 180 RNPVESAMEL KEKRSRTQEA KDIRRAQKEA AGFLDRSTSS TPVKFISRGR RPDVILEKGE 190 200 210 220 230 240 VIDFSSLSSS DRTPLTSPSP SPSLDFSAPG TPASHSATPS LLSEADLIPD VMPPQALFHD 250 260 270 280 290 300 DDEMEGDGVI DPGMEYVPPP AGSVASGPVV GVRKKVRGPE QIKQEVESEE EKPDRMDIDS 310 320 330 340 350 360 EDTDSNTSLQ TRAREKRKPQ LEKDTKPKEP RYTPVSIYEE KLLLKRLEAC PGAVAMTPEA 370 380 390 400 410 420 RRLKRKLIVR QAKRDRGLPL FDLDQVVNAA LLLVDGIYGA KEGGISRLPA GQATYRTTCQ 430 440 450 460 470 480 DFRILDRYQT SLPSRKGFRH QTTKFLYRLV GSEDMAVDQS IVSPYTSRIL KPYIRRDYET 490 500 510 520 530 540 KPPKLQLLSQ IRSHLHRSDP HWTPEPDAPL DYCYVRPNHI PTINSMCQEF FWPGIDLSEC 550 560 570 580 590 600 LQYPDFSVVV LYKKVIIAFG FMVPDVKYNE AYISFLFVHP EWRRAGIATF MIYHLIQTCM 610 620 630 640 650 GKDVTLHVSA SNPAMLLYQK FGFKTEEYVL DFYDKYYPLE STECKHAFFL RLRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00063635. IPI00218147.
RefSeq	NP_065397.3. NM_020536.4.
UniGene	Hs.488051. Hs.728790.
3D structure databases
ProteinModelPortal	Q9H8E8.
SMR	Q9H8E8. Positions 672-758.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H8E8. 2 interactions.
MINT	MINT-1479938.
STRING	9606.ENSP00000278816.
PTM databases
PhosphoSite	Q9H8E8.
Polymorphism databases
DMDM	308153608.
Proteomic databases
PaxDb	Q9H8E8.
PRIDE	Q9H8E8.
Protocols and materials databases
DNASU	57325.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000278816; ENSP00000278816; ENSG00000149474. ENST00000377681; ENSP00000366909; ENSG00000149474. ENST00000435364; ENSP00000392318; ENSG00000149474. ENST00000489634; ENSP00000425909; ENSG00000149474.
GeneID	57325.
KEGG	hsa:57325.
UCSC	uc002wqk.3. human.
Organism-specific databases
CTD	57325.
GeneCards	GC20P018066.
HGNC	HGNC:15904. CSRP2BP.
HPA	CAB034224.
neXtProt	NX_Q9H8E8.
PharmGKB	PA26969.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG295186.
HOGENOM	HOG000230880.
HOVERGEN	HBG051142.
InParanoid	Q9H8E8.
OMA	KEDICAF.
OrthoDB	EOG4XSKPB.
PhylomeDB	Q9H8E8.
Gene expression databases
ArrayExpress	Q9H8E8.
Bgee	Q9H8E8.
CleanEx	HS_CSRP2BP.
Genevestigator	Q9H8E8.
GermOnline	ENSG00000149474. Homo sapiens.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GNAT_dom. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57325.
NextBio	63428.

Entry information

Entry name

CSR2B_HUMAN

Accession

Primary (citable) accession number: Q9H8E8
Secondary accession number(s): A2A2I5 , Q96GW6, Q96IH3, Q9HBF0, Q9UIY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.