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Q08943

- SSRP1_MOUSE

UniProt

Q08943 - SSRP1_MOUSE

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Protein

FACT complex subunit SSRP1

Gene

Ssrp1

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

Functioni

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA. Also acts as a transcriptional coactivator for p63/TP63.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei450 – 4512Cleavage; by caspase-3 and/or caspase-7By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi547 – 61569HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. DNA replication Source: UniProtKB-KW
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_226490. RNA Polymerase II Transcription Elongation.
REACT_255009. RNA Polymerase II Pre-transcription Events.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit SSRP1
Alternative name(s):
Facilitates chromatin transcription complex subunit SSRP1
Recombination signal sequence recognition protein 1
Structure-specific recognition protein 1
T160
Gene namesi
Name:Ssrp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:107912. Ssrp1.

Subcellular locationi

Nucleus. Nucleusnucleolus By similarity. Chromosome
Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci (By similarity).By similarity

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. cytoplasm Source: Ensembl
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryos die soon after implantation while preimplantation blastocysts are defective for cell outgrowth.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 708707FACT complex subunit SSRP1PRO_0000048607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei170 – 1701PhosphothreonineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei413 – 4131N6-acetyllysineBy similarity
Modified residuei444 – 4441Phosphoserine3 Publications
Modified residuei510 – 5101Phosphoserine; by CK2By similarity
Modified residuei542 – 5421N6-acetyllysine1 Publication
Modified residuei657 – 6571Phosphoserine; by CK2By similarity
Modified residuei659 – 6591PhosphoserineBy similarity
Modified residuei667 – 6671PhosphoserineBy similarity
Modified residuei668 – 6681PhosphoserineBy similarity
Modified residuei671 – 6711PhosphoserineBy similarity
Modified residuei672 – 6721PhosphoserineBy similarity
Modified residuei673 – 6731PhosphoserineBy similarity
Modified residuei688 – 6881Phosphoserine; by CK2By similarity

Post-translational modificationi

Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity (By similarity).By similarity
Ubiquitinated. Polyubiquitinated following caspase cleavage resulting in degradation of the N-terminal ubiquitinated part of the cleaved protein (By similarity).By similarity
Sumoylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ08943.
PaxDbiQ08943.
PRIDEiQ08943.

PTM databases

PhosphoSiteiQ08943.

Expressioni

Gene expression databases

BgeeiQ08943.
CleanExiMM_SSRP1.
ExpressionAtlasiQ08943. baseline and differential.
GenevestigatoriQ08943.

Interactioni

Subunit structurei

Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. Binds to histone H3-H4 tetramers, but not to intact nucleosomes. Interacts with isoform gamma of p63/TP63. Interacts with FYTTD1/UIF, SRF and NEK9 (By similarity). Interacts with MYOG (via C-terminal region).By similarity1 Publication

Protein-protein interaction databases

BioGridi203512. 3 interactions.
IntActiQ08943. 3 interactions.
MINTiMINT-4135570.

Structurei

3D structure databases

ProteinModelPortaliQ08943.
SMRiQ08943. Positions 1-170, 197-427, 486-616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi439 – 49658Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi497 – 51115Ser-richAdd
BLAST
Compositional biasi512 – 53423Arg/Lys-rich (basic)Add
BLAST
Compositional biasi623 – 64018Arg/Lys-rich (basic)Add
BLAST
Compositional biasi641 – 70868Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the SSRP1 family.Curated
Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5165.
GeneTreeiENSGT00560000076898.
HOGENOMiHOG000180790.
HOVERGENiHBG002932.
InParanoidiQ08943.
KOiK09272.
OMAiIIQLDGF.
OrthoDBiEOG7B31MG.
PhylomeDBiQ08943.
TreeFamiTF315228.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR009071. HMG_box_dom.
IPR011993. PH_like_dom.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q08943-1) [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
MAETLEFNDI FQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE
60 70 80 90 100
GIWRRVALGH GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK
110 120 130 140 150
DLCVKGWNWG TVKFGGQLLS FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF
160 170 180 190 200
HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA FAQNVLSKAD VIQATGDAIC
210 220 230 240 250
IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL RLFLLPHKDQ
260 270 280 290 300
RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG
310 320 330 340 350
RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG
360 370 380 390 400
LLYPLERGFI YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ
410 420 430 440 450
YTFSSIEREE YGKLFDFVNA KKLNIKNRGL KEGINPGYDD YADSDEDQHD
460 470 480 490 500
AYLERMKEEG KIREENANDS SDDSGEETDE SFNPGEEEED VAEEFDSNAS
510 520 530 540 550
ASSSSNEGDS DREEKKREQL KRAKMAKDRK SRRKSSEAKK GKDPNAPKRP
560 570 580 590 600
MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA
610 620 630 640 650
EDARREYEKA MKEYEGGRGD SSKRDKSKKK KKVKAKMEKK STPSRGSSSK
660 670 680 690 700
SSSRQLSDSF KSKEFVSSDE SSSGENKSKK KRRRSEDSEE ELASTPPSSE

DSASGSDE
Length:708
Mass (Da):80,860
Last modified:July 11, 2006 - v2
Checksum:i8259C1A6E9899843
GO
Isoform 2 (identifier: Q08943-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     621-621: S → SSKRDK

Note: No experimental confirmation available.

Show »
Length:713
Mass (Da):81,475
Checksum:i4216D673573637ED
GO

Sequence cautioni

The sequence AAH42502.1 differs from that shown. Reason: Frameshift at position 697. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 282RQ → PS in AAB19500. (PubMed:1678855)Curated
Sequence conflicti54 – 541R → P in AAB19500. (PubMed:1678855)Curated
Sequence conflicti138 – 1447QCTTGKN → SVPQARI in AAB19500. (PubMed:1678855)Curated
Sequence conflicti156 – 1561A → P in AAB19500. (PubMed:1678855)Curated
Sequence conflicti589 – 5902SK → HE in AAH96682. (PubMed:15489334)Curated
Sequence conflicti604 – 6041R → S in AAH96682. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei621 – 6211S → SSKRDK in isoform 2. 1 PublicationVSP_019626

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50213 mRNA. Translation: AAB19500.2.
AK146446 mRNA. Translation: BAE27178.1.
AK146585 mRNA. Translation: BAE27280.1.
AK146607 mRNA. Translation: BAE27299.1.
AK151584 mRNA. Translation: BAE30524.1.
AK158552 mRNA. Translation: BAE34555.1.
BC042502 mRNA. Translation: AAH42502.1. Frameshift.
BC096682 mRNA. Translation: AAH96682.1.
CCDSiCCDS38165.1. [Q08943-1]
PIRiA41265.
RefSeqiNP_001129553.1. NM_001136081.2. [Q08943-1]
NP_892035.2. NM_182990.4. [Q08943-1]
XP_006499133.1. XM_006499070.1. [Q08943-1]
UniGeneiMm.219793.
Mm.491456.

Genome annotation databases

EnsembliENSMUST00000077798; ENSMUSP00000076971; ENSMUSG00000027067. [Q08943-1]
ENSMUST00000168266; ENSMUSP00000127058; ENSMUSG00000027067. [Q08943-1]
GeneIDi20833.
KEGGimmu:20833.
UCSCiuc008kju.1. mouse. [Q08943-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50213 mRNA. Translation: AAB19500.2 .
AK146446 mRNA. Translation: BAE27178.1 .
AK146585 mRNA. Translation: BAE27280.1 .
AK146607 mRNA. Translation: BAE27299.1 .
AK151584 mRNA. Translation: BAE30524.1 .
AK158552 mRNA. Translation: BAE34555.1 .
BC042502 mRNA. Translation: AAH42502.1 . Frameshift.
BC096682 mRNA. Translation: AAH96682.1 .
CCDSi CCDS38165.1. [Q08943-1 ]
PIRi A41265.
RefSeqi NP_001129553.1. NM_001136081.2. [Q08943-1 ]
NP_892035.2. NM_182990.4. [Q08943-1 ]
XP_006499133.1. XM_006499070.1. [Q08943-1 ]
UniGenei Mm.219793.
Mm.491456.

3D structure databases

ProteinModelPortali Q08943.
SMRi Q08943. Positions 1-170, 197-427, 486-616.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203512. 3 interactions.
IntActi Q08943. 3 interactions.
MINTi MINT-4135570.

PTM databases

PhosphoSitei Q08943.

Proteomic databases

MaxQBi Q08943.
PaxDbi Q08943.
PRIDEi Q08943.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000077798 ; ENSMUSP00000076971 ; ENSMUSG00000027067 . [Q08943-1 ]
ENSMUST00000168266 ; ENSMUSP00000127058 ; ENSMUSG00000027067 . [Q08943-1 ]
GeneIDi 20833.
KEGGi mmu:20833.
UCSCi uc008kju.1. mouse. [Q08943-1 ]

Organism-specific databases

CTDi 6749.
MGIi MGI:107912. Ssrp1.

Phylogenomic databases

eggNOGi COG5165.
GeneTreei ENSGT00560000076898.
HOGENOMi HOG000180790.
HOVERGENi HBG002932.
InParanoidi Q08943.
KOi K09272.
OMAi IIQLDGF.
OrthoDBi EOG7B31MG.
PhylomeDBi Q08943.
TreeFami TF315228.

Enzyme and pathway databases

Reactomei REACT_226490. RNA Polymerase II Transcription Elongation.
REACT_255009. RNA Polymerase II Pre-transcription Events.

Miscellaneous databases

ChiTaRSi Ssrp1. mouse.
NextBioi 299579.
PROi Q08943.
SOURCEi Search...

Gene expression databases

Bgeei Q08943.
CleanExi MM_SSRP1.
ExpressionAtlasi Q08943. baseline and differential.
Genevestigatori Q08943.

Family and domain databases

Gene3Di 1.10.30.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR013719. DUF1747.
IPR009071. HMG_box_dom.
IPR011993. PH_like_dom.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view ]
Pfami PF00505. HMG_box. 1 hit.
PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view ]
PRINTSi PR00887. SSRCOGNITION.
SMARTi SM00398. HMG. 1 hit.
[Graphical view ]
SUPFAMi SSF47095. SSF47095. 1 hit.
PROSITEi PS50118. HMG_BOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "HMG1-related DNA-binding protein isolated with V-(D)-J recombination signal probes."
    Shirakata M., Hueppi K., Usada S., Okazaki K., Yoshida K., Sakano H.
    Mol. Cell. Biol. 11:4528-4536(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: B-cell.
  2. "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: Bone marrow, Heart, Liver, Stomach and Visual cortex.
  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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-708 (ISOFORM 1).
    Strain: C57BL/6J and FVB/N-3.
    Tissue: Mammary gland and Mammary tumor.
  4. "The high-mobility-group box protein SSRP1/T160 is essential for cell viability in day 3.5 mouse embryos."
    Cao S., Bendall H., Hicks G.G., Nashabi A., Sakano H., Shinkai Y., Gariglio M., Oltz E.M., Ruley H.E.
    Mol. Cell. Biol. 23:5301-5307(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. "Myogenin recruits the histone chaperone facilitates chromatin transcription (FACT) to promote nucleosome disassembly at muscle-specific genes."
    Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J., Davie J.K.
    J. Biol. Chem. 288:7676-7687(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYOG.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSSRP1_MOUSE
AccessioniPrimary (citable) accession number: Q08943
Secondary accession number(s): Q3U9Z2
, Q3UJ75, Q4V9U4, Q8CGA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 11, 2006
Last modified: November 26, 2014
This is version 128 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