P16989 (DBPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-binding protein A

Alternative name(s):
Cold shock domain-containing protein A
Single-strand DNA-binding protein NF-GMB

Gene names

Name:	CSDA
Synonyms:	DBPA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to the GM-CSF promoter. Seems to act as a repressor. Binds also to full length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression By similarity.
Subunit structure	Found in a mRNP complex with YBX2 By similarity.
Subcellular location	Cytoplasm. Nucleus.
Tissue specificity	Highly expressed in skeletal muscle and heart.
Sequence similarities	Contains 1 CSD (cold-shock) domain.
Sequence caution	The sequence AAA35749.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc response to cold Traceable author statement. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	double-stranded DNA binding Traceable author statement. Source: ProtInc sequence-specific DNA binding transcription factor activity Non-traceable author statement. Source: ProtInc transcription corepressor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P16989-1)

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: P16989-2)

The sequence of this isoform differs from the canonical sequence as follows:
     192-260: Missing.

Isoform 3 (identifier: P16989-3)

The sequence of this isoform differs from the canonical sequence as follows:
     340-372: RPPNAPSQDGKEAKAGEAPTENPAPPTQQSSAE → PSS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 372	372	DNA-binding protein A		PRO_0000100214
Regions
	Domain	93 – 157	65	CSD
Amino acid modifications
	Modified residue	2	1	Phosphoserine Ref.12
	Modified residue	34	1	Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12
	Modified residue	38	1	Phosphoserine Ref.12
	Modified residue	79	1	Phosphoserine Ref.12
	Modified residue	134	1	Phosphoserine Ref.10 Ref.11 Ref.13
	Modified residue	201	1	Phosphoserine Ref.11 Ref.13
	Modified residue	203	1	Phosphoserine Ref.11 Ref.12 Ref.13
	Modified residue	204	1	Phosphoserine Ref.11 Ref.13
	Modified residue	287	1	Phosphotyrosine By similarity
	Modified residue	369	1	Phosphoserine Ref.12
	Modified residue	370	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	192 – 260	69	Missing in isoform 2.		VSP_001135
	Alternative sequence	340 – 372	33	RPPNA…QSSAE → PSS in isoform 3.		VSP_001136
	Natural variant	75	1	T → A. Ref.1 Ref.2 Ref.7 Corresponds to variant rs1126501 [ dbSNP | Ensembl ].		VAR_013114

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 16, 2006. Version 4. Checksum: AA8517AC3B7D35CC	FASTA	372	40,090
	10 20 30 40 50 60 MSEAGEATTT TTTTLPQAPT EAAAAAPQDP APKSPVGSGA PQAAAPAPAA HVAGNPGGDA 70 80 90 100 110 120 APAATGTAAA ASLATAAGSE DAEKKVLATK VLGTVKWFNV RNGYGFINRN DTKEDVFVHQ 130 140 150 160 170 180 TAIKKNNPRK YLRSVGDGET VEFDVVEGEK GAEAANVTGP DGVPVEGSRY AADRRRYRRG 190 200 210 220 230 240 YYGRRRGPPR NYAGEEEEEG SGSSEGFDPP ATDRQFSGAR NQLRRPQYRP QYRQRRFPPY 250 260 270 280 290 300 HVGQTFDRRS RVLPHPNRIQ AGEIGEMKDG VPEGAQLQGP VHRNPTYRPR YRSRGPPRPR 310 320 330 340 350 360 PAPAVGEAED KENQQATSGP NQPSVRRGYR RPYNYRRRPR PPNAPSQDGK EAKAGEAPTE 370 NPAPPTQQSS AE
	Isoform 2 [UniParc]. Checksum: 29E708D6FCB442CD	FASTA	303	31,947
	10 20 30 40 50 60 MSEAGEATTT TTTTLPQAPT EAAAAAPQDP APKSPVGSGA PQAAAPAPAA HVAGNPGGDA 70 80 90 100 110 120 APAATGTAAA ASLATAAGSE DAEKKVLATK VLGTVKWFNV RNGYGFINRN DTKEDVFVHQ 130 140 150 160 170 180 TAIKKNNPRK YLRSVGDGET VEFDVVEGEK GAEAANVTGP DGVPVEGSRY AADRRRYRRG 190 200 210 220 230 240 YYGRRRGPPR NAGEIGEMKD GVPEGAQLQG PVHRNPTYRP RYRSRGPPRP RPAPAVGEAE 250 260 270 280 290 300 DKENQQATSG PNQPSVRRGY RRPYNYRRRP RPPNAPSQDG KEAKAGEAPT ENPAPPTQQS SAE
	Isoform 3 [UniParc]. Checksum: 255258C4B4E80A4F	FASTA	342	37,021
	10 20 30 40 50 60 MSEAGEATTT TTTTLPQAPT EAAAAAPQDP APKSPVGSGA PQAAAPAPAA HVAGNPGGDA 70 80 90 100 110 120 APAATGTAAA ASLATAAGSE DAEKKVLATK VLGTVKWFNV RNGYGFINRN DTKEDVFVHQ 130 140 150 160 170 180 TAIKKNNPRK YLRSVGDGET VEFDVVEGEK GAEAANVTGP DGVPVEGSRY AADRRRYRRG 190 200 210 220 230 240 YYGRRRGPPR NYAGEEEEEG SGSSEGFDPP ATDRQFSGAR NQLRRPQYRP QYRQRRFPPY 250 260 270 280 290 300 HVGQTFDRRS RVLPHPNRIQ AGEIGEMKDG VPEGAQLQGP VHRNPTYRPR YRSRGPPRPR 310 320 330 340 PAPAVGEAED KENQQATSGP NQPSVRRGYR RPYNYRRRPP SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two human genes isolated by a novel method encode DNA-binding proteins containing a common region of homology." Sakura H., Maekawa T., Imamoto F., Yasuda K., Ishii S. Gene 73:499-507(1988) [PubMed: 2977358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT ALA-75.
[2]	"Characterization of the gene for dbpA, a family member of the nucleic-acid-binding proteins containing a cold-shock domain." Kudo S., Mattei M.-G., Fukuda M. Eur. J. Biochem. 231:72-82(1995) [PubMed: 7628487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANT ALA-75. Tissue: Placenta.
[3]	"Cold shock domain proteins repress transcription from the GM-CSF promoter." Coles L.S., Diamond P., Occhiodoro F., Vadas M.A., Shannon M.F. Nucleic Acids Res. 24:2311-2317(1996) [PubMed: 8710501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	Moschonas N.K. Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Blood.
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-75. Tissue: Kidney, Lung, Lymph and Muscle.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-134; SER-201; SER-203 AND SER-204, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-34; SER-38; SER-79; SER-203; SER-369 AND SER-370, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-201; SER-203 AND SER-204, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M24069 mRNA. Translation: AAA35749.1. Different initiation. L29071 , L29064, L29065, L29066, L29067, L29068, L29069, L29070 Genomic DNA. Translation: AAA79243.1. X95325 mRNA. Translation: CAA64631.1. X72712 mRNA. Translation: CAA51261.1. AK314846 mRNA. Translation: BAG37363.1. CH471094 Genomic DNA. Translation: EAW96201.1. CH471094 Genomic DNA. Translation: EAW96203.1. BC008801 mRNA. Translation: AAH08801.1. BC015564 mRNA. Translation: AAH15564.1. BC015913 mRNA. Translation: AAH15913.1. BC021926 mRNA. Translation: AAH21926.1.
IPI	IPI00031801. IPI00219147. IPI00219148.
PIR	I53354. S69501.
RefSeq	NP_001138898.1. NM_001145426.1. NP_003642.3. NM_003651.4.
UniGene	Hs.221889.
3D structure databases
ProteinModelPortal	P16989.
SMR	P16989. Positions 84-160.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42489N.
IntAct	P16989. 12 interactions.
MINT	MINT-1152000.
STRING	P16989.
PTM databases
PhosphoSite	P16989.
Polymorphism databases
DMDM	97536050.
Proteomic databases
PRIDE	P16989.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000228251; ENSP00000228251; ENSG00000060138.
GeneID	8531.
KEGG	hsa:8531.
Organism-specific databases
CTD	8531.
GeneCards	GC12M010851.
H-InvDB	HIX0010429.
HGNC	HGNC:2428. CSDA.
HPA	HPA034838.
MIM	603437. gene.
neXtProt	NX_P16989.
PharmGKB	PA26929.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14156.
HOGENOM	HBG506905.
HOVERGEN	HBG008757.
InParanoid	P16989.
OMA	PQYRRRF.
OrthoDB	EOG46DM3W.
PhylomeDB	P16989.
Gene expression databases
ArrayExpress	P16989.
Bgee	P16989.
CleanEx	HS_CSDA.
Genevestigator	P16989.
GermOnline	ENSG00000060138. Homo sapiens.
Family and domain databases
InterPro	IPR019844. Cold-shock_CS. IPR011129. Cold_shock_prot. IPR002059. CSP_DNA-bd. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K06099.
Pfam	PF00313. CSD. 1 hit. [Graphical view]
PRINTS	PR00050. COLDSHOCK.
SMART	SM00357. CSP. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
PROSITE	PS00352. COLD_SHOCK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	31948.
PMAP-CutDB	P16989.
SOURCE	Search...

Entry information

Entry name

DBPA_HUMAN

Accession

Primary (citable) accession number: P16989
Secondary accession number(s): B2RBW6 , Q14121, Q969N6, Q96B76

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	May 16, 2006
Last modified:	January 25, 2012
This is version 127 of the entry and version 4 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.