Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9D032

- SSBP3_MOUSE

UniProt

Q9D032 - SSBP3_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Single-stranded DNA-binding protein 3

Gene

Ssbp3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. single-stranded DNA binding Source: MGI

GO - Biological processi

  1. head development Source: UniProtKB
  2. head morphogenesis Source: UniProtKB
  3. hematopoietic progenitor cell differentiation Source: MGI
  4. midbrain-hindbrain boundary initiation Source: UniProtKB
  5. positive regulation of anterior head development Source: UniProtKB
  6. positive regulation of cell proliferation Source: UniProtKB
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  9. prechordal plate formation Source: UniProtKB
  10. protein complex assembly Source: UniProtKB
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Single-stranded DNA-binding protein 3
Alternative name(s):
Lck-associated signal transducer
Sequence-specific single-stranded-DNA-binding protein
Gene namesi
Name:Ssbp3
Synonyms:Last, Ssdp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1919725. Ssbp3.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
  2. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Single-stranded DNA-binding protein 3PRO_0000123829Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei347 – 3471Phosphoserine1 Publication
Modified residuei352 – 3521PhosphoserineBy similarity
Modified residuei360 – 3601Phosphothreonine1 Publication
Modified residuei381 – 3811PhosphoserineBy similarity
Modified residuei387 – 3871PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9D032.
PaxDbiQ9D032.
PRIDEiQ9D032.

PTM databases

PhosphoSiteiQ9D032.

Expressioni

Gene expression databases

BgeeiQ9D032.
CleanExiMM_SSBP3.
ExpressionAtlasiQ9D032. baseline and differential.
GenevestigatoriQ9D032.

Interactioni

Protein-protein interaction databases

BioGridi215389. 27 interactions.
DIPiDIP-42843N.
IntActiQ9D032. 1 interaction.
MINTiMINT-2568056.

Structurei

3D structure databases

ProteinModelPortaliQ9D032.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 4833LisHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi98 – 319222Pro-richAdd
BLAST
Compositional biasi158 – 369212Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 LisH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG245801.
GeneTreeiENSGT00390000009187.
HOGENOMiHOG000037785.
HOVERGENiHBG068487.
InParanoidiQ9D032.
OMAiHNPNSMM.
OrthoDBiEOG7V4B0F.
PhylomeDBiQ9D032.
TreeFamiTF318961.

Family and domain databases

InterProiIPR006594. LisH_dimerisation.
IPR008116. SSDP_DNA-bd.
[Graphical view]
PRINTSiPR01743. SSDNABINDING.
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9D032-1) [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

        10         20         30         40         50
MFAKGKGSAV PSDGQAREKL ALYVYEYLLH VGAQKSAQTF LSEIRWEKNI
60 70 80 90 100
TLGEPPGFLH SWWCVFWDLY CAAPERRDTC EHSSEAKAFH DYSAAAAPSP
110 120 130 140 150
VLGNIPPNDG MPGGPIPPGF FQGPPGSQPS PHAQPPPHNP SSMMGPHSQP
160 170 180 190 200
FMSPRYAGGP RPPIRMGNQP PGGVPGTQPL LPNSMDPTRQ QGHPNMGGSM
210 220 230 240 250
QRMNPPRGMG PMGPGPQNYG SGMRPPPNSL GPAMPGINMG PGAGRPWPNP
260 270 280 290 300
NSANSIPYSS SSPGTYVGPP GGGGPPGTPI MPSPADSTNS SDNIYTMINP
310 320 330 340 350
VPPGGSRSNF PMGPGSDGPM GGMGGMEPHH MNGSLGSGDI DGLPKNSPNN
360 370 380
ISGISNPPGT PRDDGELGGN FLHSFQNDNY SPSMTMSV
Length:388
Mass (Da):40,421
Last modified:January 16, 2004 - v2
Checksum:iDBBB169D4EE10536
GO
Isoform 2 (identifier: Q9D032-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:361
Mass (Da):37,697
Checksum:iCECDA59F18EFC0B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431A → D in AAG43403. 1 PublicationCurated
Sequence conflicti243 – 2431A → V in BAB27882. (PubMed:16141072)Curated
Sequence conflicti335 – 3351L → V in AAG43403. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei122 – 14827Missing in isoform 2. 4 PublicationsVSP_006262Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18427.1. [Q9D032-1]
CCDS18428.1. [Q9D032-2]
RefSeqiNP_076161.2. NM_023672.2. [Q9D032-1]
NP_940840.1. NM_198438.1. [Q9D032-2]
UniGeneiMm.195635.
Mm.474861.

Genome annotation databases

EnsembliENSMUST00000030367; ENSMUSP00000030367; ENSMUSG00000061887. [Q9D032-1]
ENSMUST00000072753; ENSMUSP00000072536; ENSMUSG00000061887. [Q9D032-2]
GeneIDi72475.
KEGGimmu:72475.
UCSCiuc008tyx.1. mouse. [Q9D032-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS18427.1. [Q9D032-1 ]
CCDS18428.1. [Q9D032-2 ]
RefSeqi NP_076161.2. NM_023672.2. [Q9D032-1 ]
NP_940840.1. NM_198438.1. [Q9D032-2 ]
UniGenei Mm.195635.
Mm.474861.

3D structure databases

ProteinModelPortali Q9D032.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 215389. 27 interactions.
DIPi DIP-42843N.
IntActi Q9D032. 1 interaction.
MINTi MINT-2568056.

PTM databases

PhosphoSitei Q9D032.

Proteomic databases

MaxQBi Q9D032.
PaxDbi Q9D032.
PRIDEi Q9D032.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030367 ; ENSMUSP00000030367 ; ENSMUSG00000061887 . [Q9D032-1 ]
ENSMUST00000072753 ; ENSMUSP00000072536 ; ENSMUSG00000061887 . [Q9D032-2 ]
GeneIDi 72475.
KEGGi mmu:72475.
UCSCi uc008tyx.1. mouse. [Q9D032-1 ]

Organism-specific databases

CTDi 23648.
MGIi MGI:1919725. Ssbp3.

Phylogenomic databases

eggNOGi NOG245801.
GeneTreei ENSGT00390000009187.
HOGENOMi HOG000037785.
HOVERGENi HBG068487.
InParanoidi Q9D032.
OMAi HNPNSMM.
OrthoDBi EOG7V4B0F.
PhylomeDBi Q9D032.
TreeFami TF318961.

Miscellaneous databases

ChiTaRSi Ssbp3. mouse.
NextBioi 336302.
PROi Q9D032.
SOURCEi Search...

Gene expression databases

Bgeei Q9D032.
CleanExi MM_SSBP3.
ExpressionAtlasi Q9D032. baseline and differential.
Genevestigatori Q9D032.

Family and domain databases

InterProi IPR006594. LisH_dimerisation.
IPR008116. SSDP_DNA-bd.
[Graphical view ]
PRINTSi PR01743. SSDNABINDING.
SMARTi SM00667. LisH. 1 hit.
[Graphical view ]
PROSITEi PS50896. LISH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSSBP3_MOUSE
AccessioniPrimary (citable) accession number: Q9D032
Secondary accession number(s): Q99LC6, Q9EQP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: January 16, 2004
Last modified: November 26, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3