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Q9D032 (SSBP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Single-stranded DNA-binding protein 3
Alternative name(s):
Lck-associated signal transducer
Sequence-specific single-stranded-DNA-binding protein
Gene names
Name:Ssbp3
Synonyms:Last, Ssdp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in transcription regulation of the alpha 2(I) collagen gene where it binds to the single-stranded polypyrimidine sequences in the promoter region By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 1 LisH domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhead development

Inferred from genetic interaction PubMed 15857913. Source: UniProtKB

head morphogenesis

Inferred from mutant phenotype PubMed 15857913. Source: UniProtKB

hematopoietic progenitor cell differentiation

Inferred from mutant phenotype PubMed 24029230. Source: MGI

midbrain-hindbrain boundary initiation

Inferred from mutant phenotype PubMed 15857913. Source: UniProtKB

positive regulation of anterior head development

Inferred from mutant phenotype PubMed 15857913. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15857913. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15857913. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 15857913. Source: UniProtKB

prechordal plate formation

Inferred from mutant phenotype PubMed 15857913. Source: UniProtKB

protein complex assembly

Inferred from mutant phenotype PubMed 15857913. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 15857913. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 19323994. Source: MGI

single-stranded DNA binding

Inferred from sequence alignment PubMed 10524251. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D032-1)

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: Q9D032-2)

The sequence of this isoform differs from the canonical sequence as follows:
     122-148: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Single-stranded DNA-binding protein 3
PRO_0000123829

Regions

Domain16 – 4833LisH
Compositional bias98 – 319222Pro-rich
Compositional bias158 – 369212Gly-rich

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3471Phosphoserine Ref.6
Modified residue3521Phosphoserine By similarity
Modified residue3601Phosphothreonine Ref.6
Modified residue3811Phosphoserine By similarity
Modified residue3871Phosphoserine By similarity

Natural variations

Alternative sequence122 – 14827Missing in isoform 2.
VSP_006262

Experimental info

Sequence conflict2431A → D in AAG43403. Ref.1
Sequence conflict2431A → V in BAB27882. Ref.4
Sequence conflict3351L → V in AAG43403. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: DBBB169D4EE10536

FASTA38840,421
        10         20         30         40         50         60 
MFAKGKGSAV PSDGQAREKL ALYVYEYLLH VGAQKSAQTF LSEIRWEKNI TLGEPPGFLH 

        70         80         90        100        110        120 
SWWCVFWDLY CAAPERRDTC EHSSEAKAFH DYSAAAAPSP VLGNIPPNDG MPGGPIPPGF 

       130        140        150        160        170        180 
FQGPPGSQPS PHAQPPPHNP SSMMGPHSQP FMSPRYAGGP RPPIRMGNQP PGGVPGTQPL 

       190        200        210        220        230        240 
LPNSMDPTRQ QGHPNMGGSM QRMNPPRGMG PMGPGPQNYG SGMRPPPNSL GPAMPGINMG 

       250        260        270        280        290        300 
PGAGRPWPNP NSANSIPYSS SSPGTYVGPP GGGGPPGTPI MPSPADSTNS SDNIYTMINP 

       310        320        330        340        350        360 
VPPGGSRSNF PMGPGSDGPM GGMGGMEPHH MNGSLGSGDI DGLPKNSPNN ISGISNPPGT 

       370        380 
PRDDGELGGN FLHSFQNDNY SPSMTMSV 

« Hide

Isoform 2 [UniParc].

Checksum: CECDA59F18EFC0B2
Show »

FASTA36137,697

References

« Hide 'large scale' references
[1]"LAST, a novel protein binding to the SH2 domain of Lck/Src, mediates signaling events of the Src-type tyrosine kinase."
Park C., Choi Y.B., Park D., Hur E.M., Yun Y.D.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: T-cell lymphoma.
[2]"SSDP1 gene encodes a protein with a conserved N-terminal FORWARD domain."
Bayarsaihan D.
Biochim. Biophys. Acta 1599:152-155(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Ssdp proteins bind to LIM-interacting co-factors and regulate the activity of LIM-homeodomain protein complexes in vivo."
van Meyel D.J., Thomas J.B., Agulnick A.D.
Development 130:1915-1925(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C3H.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF170906 mRNA. Translation: AAG43403.1.
AF500117 mRNA. Translation: AAM22102.1.
AY167987 mRNA. Translation: AAN87333.1.
AK011853 mRNA. Translation: BAB27882.1.
BC003430 mRNA. Translation: AAH03430.1.
CCDSCCDS18427.1. [Q9D032-1]
CCDS18428.1. [Q9D032-2]
RefSeqNP_076161.2. NM_023672.2. [Q9D032-1]
NP_940840.1. NM_198438.1. [Q9D032-2]
UniGeneMm.195635.
Mm.474861.

3D structure databases

ProteinModelPortalQ9D032.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215389. 27 interactions.
DIPDIP-42843N.
IntActQ9D032. 1 interaction.
MINTMINT-2568056.

PTM databases

PhosphoSiteQ9D032.

Proteomic databases

MaxQBQ9D032.
PaxDbQ9D032.
PRIDEQ9D032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030367; ENSMUSP00000030367; ENSMUSG00000061887. [Q9D032-1]
ENSMUST00000072753; ENSMUSP00000072536; ENSMUSG00000061887. [Q9D032-2]
GeneID72475.
KEGGmmu:72475.
UCSCuc008tyx.1. mouse. [Q9D032-1]

Organism-specific databases

CTD23648.
MGIMGI:1919725. Ssbp3.

Phylogenomic databases

eggNOGNOG245801.
GeneTreeENSGT00390000009187.
HOGENOMHOG000037785.
HOVERGENHBG068487.
InParanoidQ9D032.
OMAHNPNSMM.
OrthoDBEOG7V4B0F.
PhylomeDBQ9D032.
TreeFamTF318961.

Gene expression databases

ArrayExpressQ9D032.
BgeeQ9D032.
CleanExMM_SSBP3.
GenevestigatorQ9D032.

Family and domain databases

InterProIPR006594. LisH_dimerisation.
IPR008116. SSDP_DNA-bd.
[Graphical view]
PRINTSPR01743. SSDNABINDING.
SMARTSM00667. LisH. 1 hit.
[Graphical view]
PROSITEPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSSBP3. mouse.
NextBio336302.
PROQ9D032.
SOURCESearch...

Entry information

Entry nameSSBP3_MOUSE
AccessionPrimary (citable) accession number: Q9D032
Secondary accession number(s): Q99LC6, Q9EQP3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: January 16, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot