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Q08943

- SSRP1_MOUSE

UniProt

Q08943 - SSRP1_MOUSE

Protein

FACT complex subunit SSRP1

Gene

Ssrp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (11 Jul 2006)
      Previous versions | rss
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    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

    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

    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.

    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-SubCell
    2. cytoplasm Source: Ensembl
    3. nucleolus Source: UniProtKB-SubCell

    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

    ArrayExpressiQ08943.
    BgeeiQ08943.
    CleanExiMM_SSRP1.
    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.
    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

    MAETLEFNDI FQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE    50
    GIWRRVALGH GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK 100
    DLCVKGWNWG TVKFGGQLLS FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF 150
    HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA FAQNVLSKAD VIQATGDAIC 200
    IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL RLFLLPHKDQ 250
    RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG 300
    RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG 350
    LLYPLERGFI YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ 400
    YTFSSIEREE YGKLFDFVNA KKLNIKNRGL KEGINPGYDD YADSDEDQHD 450
    AYLERMKEEG KIREENANDS SDDSGEETDE SFNPGEEEED VAEEFDSNAS 500
    ASSSSNEGDS DREEKKREQL KRAKMAKDRK SRRKSSEAKK GKDPNAPKRP 550
    MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA 600
    EDARREYEKA MKEYEGGRGD SSKRDKSKKK KKVKAKMEKK STPSRGSSSK 650
    SSSRQLSDSF KSKEFVSSDE SSSGENKSKK KRRRSEDSEE ELASTPPSSE 700
    DSASGSDE 708
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    KOi K09272.
    OMAi IIQLDGF.
    OrthoDBi EOG7B31MG.
    PhylomeDBi Q08943.
    TreeFami TF315228.

    Enzyme and pathway databases

    Reactomei REACT_226490. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    NextBioi 299579.
    PROi Q08943.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08943.
    Bgeei Q08943.
    CleanExi MM_SSRP1.
    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

    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: October 1, 2014
    This is version 126 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