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Protein

Single-stranded DNA-binding protein 3

Gene

SSBP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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: InterPro

GO - Biological processi

  1. head morphogenesis Source: Ensembl
  2. hematopoietic progenitor cell differentiation Source: Ensembl
  3. midbrain-hindbrain boundary initiation Source: Ensembl
  4. positive regulation of anterior head development Source: Ensembl
  5. positive regulation of cell proliferation Source: Ensembl
  6. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. prechordal plate formation Source: Ensembl
  8. protein complex assembly Source: Ensembl
  9. 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):
Sequence-specific single-stranded-DNA-binding protein
Gene namesi
Name:SSBP3
Synonyms:SSDP, SSDP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:15674. SSBP3.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38017.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Single-stranded DNA-binding protein 3PRO_0000123828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei347 – 3471Phosphoserine4 Publications
Modified residuei352 – 3521Phosphoserine2 Publications
Modified residuei360 – 3601Phosphothreonine2 Publications
Modified residuei381 – 3811Phosphoserine1 Publication
Modified residuei387 – 3871Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BWW4.
PaxDbiQ9BWW4.
PRIDEiQ9BWW4.

PTM databases

PhosphoSiteiQ9BWW4.

Expressioni

Tissue specificityi

Highly expressed in all hematopoietic tissues, including spleen, lymph node, peripheral blood, bone marrow, thymus, and fetal liver, with highest expression in thymus and fetal liver. Expression is also high in heart, brain, kidney, and skeletal muscle.

Gene expression databases

BgeeiQ9BWW4.
CleanExiHS_SSBP3.
ExpressionAtlasiQ9BWW4. baseline and differential.
GenevestigatoriQ9BWW4.

Interactioni

Protein-protein interaction databases

BioGridi117175. 30 interactions.
DIPiDIP-48897N.
IntActiQ9BWW4. 2 interactions.
STRINGi9606.ENSP00000360371.

Structurei

3D structure databases

ProteinModelPortaliQ9BWW4.
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.
InParanoidiQ9BWW4.
OMAiHNPNSMM.
PhylomeDBiQ9BWW4.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BWW4-1) [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:June 1, 2001 - v1
Checksum:iDBBB169D4EE10536
GO
Isoform 2 (identifier: Q9BWW4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-149: Missing.

Show »
Length:361
Mass (Da):37,697
Checksum:iCECDA59F18EFC0B2
GO
Isoform 3 (identifier: Q9BWW4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-169: Missing.

Show »
Length:368
Mass (Da):38,210
Checksum:i87D2E99D9C11B620
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei123 – 14927Missing in isoform 2. 1 PublicationVSP_006260Add
BLAST
Alternative sequencei150 – 16920Missing in isoform 3. 2 PublicationsVSP_006261Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY026310
, AY026293, AY026294, AY026295, AY026296, AY026297, AY026298, AY026299, AY026300, AY026301, AY026302, AY026303, AY026304, AY026305, AY026306, AY026307, AY026308, AY026309 Genomic DNA. Translation: AAK21984.1.
AY026310
, AY026293, AY026294, AY026295, AY026296, AY026297, AY026299, AY026300, AY026301, AY026302, AY026303, AY026304, AY026305, AY026306, AY026307, AY026308, AY026309 Genomic DNA. Translation: AAK21985.1.
AF500116 mRNA. Translation: AAM22101.1.
AK289474 mRNA. Translation: BAF82163.1.
CH471059 Genomic DNA. Translation: EAX06692.1.
AL035415, AL161644 Genomic DNA. Translation: CAI22487.1.
AL035415, AL161644 Genomic DNA. Translation: CAI22488.1.
AL161644, AL035415 Genomic DNA. Translation: CAI23562.1.
AL161644, AL035415 Genomic DNA. Translation: CAI23563.1.
BC003605 mRNA. Translation: AAH03605.1.
BC066365 mRNA. Translation: AAH66365.1.
CCDSiCCDS30726.1. [Q9BWW4-2]
CCDS590.1. [Q9BWW4-3]
CCDS591.1. [Q9BWW4-1]
RefSeqiNP_001009955.1. NM_001009955.3. [Q9BWW4-2]
NP_060540.2. NM_018070.4. [Q9BWW4-3]
NP_663768.1. NM_145716.3. [Q9BWW4-1]
UniGeneiHs.476706.
Hs.658676.

Genome annotation databases

EnsembliENST00000357475; ENSP00000350067; ENSG00000157216. [Q9BWW4-3]
ENST00000371319; ENSP00000360370; ENSG00000157216. [Q9BWW4-2]
ENST00000371320; ENSP00000360371; ENSG00000157216. [Q9BWW4-1]
GeneIDi23648.
KEGGihsa:23648.
UCSCiuc001cxe.4. human. [Q9BWW4-1]
uc001cxf.4. human. [Q9BWW4-3]
uc001cxg.4. human. [Q9BWW4-2]

Polymorphism databases

DMDMi27734581.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY026310
, AY026293, AY026294, AY026295, AY026296, AY026297, AY026298, AY026299, AY026300, AY026301, AY026302, AY026303, AY026304, AY026305, AY026306, AY026307, AY026308, AY026309 Genomic DNA. Translation: AAK21984.1.
AY026310
, AY026293, AY026294, AY026295, AY026296, AY026297, AY026299, AY026300, AY026301, AY026302, AY026303, AY026304, AY026305, AY026306, AY026307, AY026308, AY026309 Genomic DNA. Translation: AAK21985.1.
AF500116 mRNA. Translation: AAM22101.1.
AK289474 mRNA. Translation: BAF82163.1.
CH471059 Genomic DNA. Translation: EAX06692.1.
AL035415, AL161644 Genomic DNA. Translation: CAI22487.1.
AL035415, AL161644 Genomic DNA. Translation: CAI22488.1.
AL161644, AL035415 Genomic DNA. Translation: CAI23562.1.
AL161644, AL035415 Genomic DNA. Translation: CAI23563.1.
BC003605 mRNA. Translation: AAH03605.1.
BC066365 mRNA. Translation: AAH66365.1.
CCDSiCCDS30726.1. [Q9BWW4-2]
CCDS590.1. [Q9BWW4-3]
CCDS591.1. [Q9BWW4-1]
RefSeqiNP_001009955.1. NM_001009955.3. [Q9BWW4-2]
NP_060540.2. NM_018070.4. [Q9BWW4-3]
NP_663768.1. NM_145716.3. [Q9BWW4-1]
UniGeneiHs.476706.
Hs.658676.

3D structure databases

ProteinModelPortaliQ9BWW4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117175. 30 interactions.
DIPiDIP-48897N.
IntActiQ9BWW4. 2 interactions.
STRINGi9606.ENSP00000360371.

PTM databases

PhosphoSiteiQ9BWW4.

Polymorphism databases

DMDMi27734581.

Proteomic databases

MaxQBiQ9BWW4.
PaxDbiQ9BWW4.
PRIDEiQ9BWW4.

Protocols and materials databases

DNASUi23648.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357475; ENSP00000350067; ENSG00000157216. [Q9BWW4-3]
ENST00000371319; ENSP00000360370; ENSG00000157216. [Q9BWW4-2]
ENST00000371320; ENSP00000360371; ENSG00000157216. [Q9BWW4-1]
GeneIDi23648.
KEGGihsa:23648.
UCSCiuc001cxe.4. human. [Q9BWW4-1]
uc001cxf.4. human. [Q9BWW4-3]
uc001cxg.4. human. [Q9BWW4-2]

Organism-specific databases

CTDi23648.
GeneCardsiGC01M054692.
HGNCiHGNC:15674. SSBP3.
MIMi607390. gene.
neXtProtiNX_Q9BWW4.
PharmGKBiPA38017.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG245801.
GeneTreeiENSGT00390000009187.
HOGENOMiHOG000037785.
HOVERGENiHBG068487.
InParanoidiQ9BWW4.
OMAiHNPNSMM.
PhylomeDBiQ9BWW4.
TreeFamiTF318961.

Miscellaneous databases

ChiTaRSiSSBP3. human.
GeneWikiiSSBP3.
GenomeRNAii23648.
NextBioi46471.
PROiQ9BWW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BWW4.
CleanExiHS_SSBP3.
ExpressionAtlasiQ9BWW4. baseline and differential.
GenevestigatoriQ9BWW4.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel, evolutionarily conserved gene family with putative sequence-specific single-stranded DNA-binding activity."
    Castro P.D., Liang H., Liang J.C., Nagarajan L.
    Genomics 80:78-85(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  2. Bayarsaihan D.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 3).
    Tissue: Eye and Placenta.
  7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-352; THR-360; SER-381 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; THR-360 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSSBP3_HUMAN
AccessioniPrimary (citable) accession number: Q9BWW4
Secondary accession number(s): A8K0A9
, Q5T860, Q5T861, Q9BTM0, Q9BWW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.