DNA-binding protein A - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P16989 (DBPA_HUMAN)

Last modified June 16, 2009. Version 97. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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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
Gene Ontology (GO)
Biological process	negative regulation of transcription from RNA polymerase II promoter Ref.3 Traceable author statement. Source: ProtInc response to cold Ref.3 Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.2 Traceable author statement. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA polymerase II transcription factor activity Ref.3 Traceable author statement. Source: ProtInc double-stranded DNA binding Ref.1 Traceable author statement. Source: ProtInc transcription corepressor activity Ref.3 Traceable author statement. Source: ProtInc transcription factor activity Ref.3 Non-traceable author statement. Source: ProtInc
Complete GO annotation...

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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

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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

CSD

Amino acid modifications

Modified residue

Phosphoserine Ref.6 Ref.7 Ref.9

Modified residue

134

Phosphoserine Ref.9 Ref.8

Modified residue

201

Phosphoserine Ref.9

Modified residue

203

Phosphoserine Ref.9

Modified residue

204

Phosphoserine Ref.9

Modified residue

287

Phosphotyrosine By similarity

Natural variations

Alternative sequence

192 – 260

Missing in isoform 2.

VSP_001135

Alternative sequence

340 – 372

RPPNA…QSSAE → PSS in isoform 3.

VSP_001136

Natural variant

T → A: dbSNP rs1126501. Ref.1 Ref.2 Ref.5

VAR_013114

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Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified May 16, 2006. Version 4. Checksum: AA8517AC3B7D35CC Show »	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 « Hide
Isoform 2. Checksum: 29E708D6FCB442CD Show »	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 « Hide
Isoform 3. Checksum: 255258C4B4E80A4F Show »	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 « Hide

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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]	"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] (ISOFORM 1), VARIANT ALA-75. Tissue: Lung, Lymph and Muscle.
[6]	"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: Epithelium.
[7]	"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: T-cell.
[8]	"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: Epithelium.
[9]	"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.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M24069 mRNA. Translation: AAA35749.1. Different initiation. L29071 L29070 Genomic DNA. Translation: AAA79243.1. X95325 mRNA. Translation: CAA64631.1. X72712 mRNA. Translation: CAA51261.1. BC008801 mRNA. Translation: AAH08801.1. BC015564 mRNA. Translation: AAH15564.1. BC021926 mRNA. Translation: AAH21926.1.
IPI	IPI00031801. IPI00219147. IPI00219148.
PIR	I53354. S69501.
RefSeq	NP_003642.3.
UniGene	Hs.221889
3D structure databases
HSSP	HSSP built from PDB template 1HZA based on UniProtKB P41016.
SMR	P16989. Positions 84-160.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16989. 2 interactions.
PTM databases
PhosphoSite	P16989.
Proteomic databases
PRIDE	P16989.
Genome annotation databases
Ensembl	ENSG00000060138. Homo sapiens. [Contig view]
GeneID	8531.
KEGG	hsa:8531.
Organism-specific databases
GeneCards	GC12M010742.
H-InvDB	HIX0010429.
HGNC	HGNC:2428. CSDA.
MIM	603437. gene.
PharmGKB	PA26929.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P16989.
HOVERGEN	P16989.
OMA	P16989. QDPAPKS.
Gene expression databases
ArrayExpress	P16989.
Bgee	P16989.
CleanEx	HS_CSDA.
GermOnline	ENSG00000060138. Homo sapiens.
Family and domain databases
InterPro	IPR019844. Cold-shock_conserved_site. IPR011129. Cold_shock_prot. IPR002059. CSP_DNA_bd. IPR012340. NA-bd_OB-fold. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF00313. CSD. 1 hit. [Graphical view]
PRINTS	PR00050. COLDSHOCK.
ProDom	PD000621. Cold_shock. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00357. CSP. 1 hit. [Graphical view]
PROSITE	PS00352. COLD_SHOCK. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	31948.
PMAP-CutDB	P16989.
SOURCE	Search...

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Entry information

Entry name

DBPA_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	May 16, 2006
Last modified:	June 16, 2009
This is version 97 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents