Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04837 (SSBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Single-stranded DNA-binding protein, mitochondrial

Short name=Mt-SSB
Short name=MtSSB
Alternative name(s):
PWP1-interacting protein 17
Gene names
Name:SSBP1
Synonyms:SSBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds preferentially and cooperatively to ss-DNA. Probably involved in mitochondrial DNA replication. Associates with mitochondrial DNA. HAMAP-Rule MF_00984

Subunit structure

Homotetramer By similarity. Interacts with MPG/AAG, through inhibition of its glycosylase activity it potentially prevents formation of DNA breaks in ssDNA, ensuring that base removal primarily occurs in dsDNA. Ref.9

Subcellular location

Mitochondrion. Mitochondrion matrixmitochondrion nucleoid Ref.6.

Sequence similarities

Contains 1 SSB domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

revP046183EBI-353460,EBI-6164309From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1616Mitochondrion Ref.4
Chain17 – 148132Single-stranded DNA-binding protein, mitochondrial HAMAP-Rule MF_00984
PRO_0000033263

Regions

Domain30 – 141112SSB

Amino acid modifications

Modified residue791Phosphoserine Ref.5
Modified residue1131N6-acetyllysine Ref.7
Modified residue1221N6-succinyllysine By similarity

Secondary structure

................... 148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04837 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 98EE9E396D5636C2

FASTA14817,260
        10         20         30         40         50         60 
MFRRPVLQVL RQFVRHESET TTSLVLERSL NRVHLLGRVG QDPVLRQVEG KNPVTIFSLA 

        70         80         90        100        110        120 
TNEMWRSGDS EVYQLGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGSRIYL EGKIDYGEYM 

       130        140 
DKNNVRRQAT TIIADNIIFL SDQTKEKE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of human and rat cDNAs encoding the mitochondrial single-stranded DNA-binding protein (SSB)."
Tiranti V., Rocchi M., Didonato S., Zeviani M.
Gene 126:219-225(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"hPWP1-interacting protein 17 (ssDNA BP)."
Honore B.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Tissue: Cervix.
[4]"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
Xu G., Shin S.B., Jaffrey S.R.
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 17-29.
Tissue: Leukemic T-cell.
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[6]"The layered structure of human mitochondrial DNA nucleoids."
Bogenhagen D.F., Rousseau D., Burke S.
J. Biol. Chem. 283:3665-3675(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"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-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts with mitochondrial single-stranded binding protein (mtSSB)."
van Loon B., Samson L.D.
DNA Repair 12:177-187(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH MPG.
[10]"Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4-A resolution."
Yang C., Curth U., Urbanke C., Kang C.
Nat. Struct. Biol. 4:153-157(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-141.
[11]"Crystal structure of human mitochondrial single-stranded DNA-binding protein (HMTSSB)."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 16-148.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94556 mRNA. Translation: AAA36332.1.
AF277319 mRNA. Translation: AAK69112.1.
BC000895 mRNA. Translation: AAH00895.1.
CCDSCCDS5866.1.
PIRJN0568.
RefSeqNP_001243439.1. NM_001256510.1.
NP_001243440.1. NM_001256511.1.
NP_001243441.1. NM_001256512.1.
NP_001243442.1. NM_001256513.1.
NP_003134.1. NM_003143.2.
UniGeneHs.490394.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S3OX-ray2.47A/B17-148[»]
2DUDX-ray2.70A/B16-148[»]
3ULLX-ray2.40A/B17-148[»]
ProteinModelPortalQ04837.
SMRQ04837. Positions 26-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112620. 79 interactions.
IntActQ04837. 26 interactions.
MINTMINT-3025472.
STRING9606.ENSP00000265304.

PTM databases

PhosphoSiteQ04837.

2D gel databases

UCD-2DPAGEQ04837.

Proteomic databases

MaxQBQ04837.
PaxDbQ04837.
PeptideAtlasQ04837.
PRIDEQ04837.

Protocols and materials databases

DNASU6742.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265304; ENSP00000265304; ENSG00000106028.
ENST00000465582; ENSP00000420485; ENSG00000106028.
ENST00000481508; ENSP00000419665; ENSG00000106028.
ENST00000484178; ENSP00000419388; ENSG00000106028.
ENST00000498107; ENSP00000419541; ENSG00000106028.
ENST00000570667; ENSP00000460028; ENSG00000262771.
ENST00000571430; ENSP00000459367; ENSG00000262771.
ENST00000574199; ENSP00000461884; ENSG00000262771.
ENST00000575059; ENSP00000458815; ENSG00000262771.
ENST00000576834; ENSP00000459208; ENSG00000262771.
GeneID6742.
KEGGhsa:6742.
UCSCuc003vwo.2. human.

Organism-specific databases

CTD6742.
GeneCardsGC07P141442.
HGNCHGNC:11317. SSBP1.
HPAHPA002866.
MIM600439. gene.
neXtProtNX_Q04837.
PharmGKBPA36141.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0629.
HOVERGENHBG001181.
InParanoidQ04837.
KOK03111.
OMARNPVTIF.
PhylomeDBQ04837.
TreeFamTF314629.

Enzyme and pathway databases

ReactomeREACT_200751. Organelle biogenesis and maintenance.

Gene expression databases

ArrayExpressQ04837.
BgeeQ04837.
CleanExHS_SSBP1.
GenevestigatorQ04837.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00984. SSB.
InterProIPR012340. NA-bd_OB-fold.
IPR000424. Primosome_PriB/ssb.
IPR011344. ssDNA-bd.
[Graphical view]
PANTHERPTHR10302. PTHR10302. 1 hit.
PfamPF00436. SSB. 1 hit.
[Graphical view]
PIRSFPIRSF002070. SSB. 1 hit.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00621. ssb. 1 hit.
PROSITEPS50935. SSB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSSBP1. human.
EvolutionaryTraceQ04837.
GeneWikiSSBP1.
GenomeRNAi6742.
NextBio26300.
PROQ04837.
SOURCESearch...

Entry information

Entry nameSSBP_HUMAN
AccessionPrimary (citable) accession number: Q04837
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM