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Protein

Serine/arginine repetitive matrix protein 1

Gene

Srrm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine repetitive matrix protein 1
Alternative name(s):
Plenty-of-prolines 101
Gene namesi
Name:Srrm1
Synonyms:Pop101
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1858303. Srrm1.

Subcellular locationi

  • Nucleus matrix PROSITE-ProRule annotation
  • Nucleus speckle PROSITE-ProRule annotation

GO - Cellular componenti

  • nuclear matrix Source: MGI
  • nuclear speck Source: UniProtKB-SubCell
  • spliceosomal complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 946946Serine/arginine repetitive matrix protein 1PRO_0000076327Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei7 – 71Citrulline1 Publication
Modified residuei140 – 1401N6-acetyllysineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources
Modified residuei227 – 2271PhosphoserineBy similarity
Cross-linki231 – 231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei241 – 2411PhosphothreonineBy similarity
Cross-linki249 – 249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei260 – 2601PhosphoserineCombined sources
Modified residuei387 – 3871PhosphoserineBy similarity
Modified residuei389 – 3891PhosphoserineBy similarity
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei404 – 4041PhosphothreonineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei414 – 4141PhosphothreonineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity
Modified residuei427 – 4271PhosphoserineCombined sources
Modified residuei429 – 4291PhosphoserineCombined sources
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei448 – 4481PhosphoserineBy similarity
Modified residuei450 – 4501PhosphoserineBy similarity
Modified residuei461 – 4611PhosphoserineBy similarity
Modified residuei463 – 4631PhosphoserineBy similarity
Modified residuei476 – 4761PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei524 – 5241PhosphoserineBy similarity
Modified residuei526 – 5261PhosphoserineBy similarity
Modified residuei528 – 5281PhosphoserineBy similarity
Modified residuei530 – 5301PhosphoserineBy similarity
Modified residuei561 – 5611PhosphoserineBy similarity
Modified residuei563 – 5631PhosphoserineBy similarity
Modified residuei572 – 5721PhosphoserineCombined sources
Modified residuei574 – 5741PhosphoserineCombined sources
Modified residuei593 – 5931PhosphothreonineBy similarity
Modified residuei600 – 6001PhosphothreonineBy similarity
Modified residuei602 – 6021PhosphoserineBy similarity
Modified residuei615 – 6151PhosphotyrosineBy similarity
Modified residuei616 – 6161PhosphoserineCombined sources
Modified residuei624 – 6241PhosphoserineBy similarity
Modified residuei626 – 6261PhosphoserineBy similarity
Modified residuei633 – 6331PhosphothreonineCombined sources
Modified residuei635 – 6351PhosphoserineCombined sources
Modified residuei645 – 6451PhosphoserineBy similarity
Modified residuei647 – 6471PhosphoserineBy similarity
Modified residuei655 – 6551PhosphoserineBy similarity
Modified residuei657 – 6571PhosphoserineCombined sources
Modified residuei713 – 7131PhosphoserineCombined sources
Modified residuei714 – 7141PhosphoserineCombined sources
Modified residuei723 – 7231PhosphoserineCombined sources
Modified residuei725 – 7251PhosphoserineCombined sources
Modified residuei731 – 7311PhosphoserineCombined sources
Modified residuei733 – 7331PhosphoserineCombined sources
Modified residuei736 – 7361PhosphothreonineBy similarity
Modified residuei779 – 7791PhosphoserineCombined sources
Modified residuei781 – 7811PhosphoserineBy similarity
Modified residuei789 – 7891PhosphoserineBy similarity
Modified residuei793 – 7931PhosphoserineBy similarity
Modified residuei795 – 7951PhosphoserineCombined sources
Modified residuei797 – 7971PhosphoserineCombined sources
Modified residuei810 – 8101PhosphoserineCombined sources
Modified residuei814 – 8141PhosphoserineCombined sources
Modified residuei816 – 8161PhosphoserineCombined sources
Modified residuei818 – 8181PhosphoserineCombined sources
Modified residuei819 – 8191PhosphothreonineCombined sources
Modified residuei822 – 8221PhosphoserineCombined sources
Modified residuei832 – 8321PhosphoserineCombined sources
Modified residuei834 – 8341PhosphothreonineCombined sources
Modified residuei836 – 8361PhosphoserineCombined sources
Modified residuei838 – 8381PhosphoserineCombined sources
Modified residuei843 – 8431PhosphoserineCombined sources
Modified residuei913 – 9131PhosphothreonineCombined sources
Modified residuei915 – 9151PhosphoserineCombined sources
Modified residuei943 – 9431PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ52KI8.
MaxQBiQ52KI8.
PaxDbiQ52KI8.
PeptideAtlasiQ52KI8.
PRIDEiQ52KI8.

PTM databases

iPTMnetiQ52KI8.
PhosphoSiteiQ52KI8.

Expressioni

Gene expression databases

BgeeiQ52KI8.
CleanExiMM_SRRM1.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, PRPF8, NCBP1, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with BAT1, CPSF1, RBM8A, RNPS1, and ALYREF/THOC4. Seems to be a compound of RNA export complexes that are released from speckles in a ATP-dependent manner (By similarity).By similarity

Protein-protein interaction databases

BioGridi206179. 2 interactions.
IntActiQ52KI8. 2 interactions.
MINTiMINT-1867213.
STRINGi10090.ENSMUSP00000125003.

Structurei

3D structure databases

ProteinModelPortaliQ52KI8.
SMRiQ52KI8. Positions 27-134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 126100PWIPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156Necessary for mRNA 3'-end cleavage and cytoplasmic accumulationBy similarityAdd
BLAST
Regioni1 – 151151Necessary for DNA and RNA-bindingBy similarityAdd
BLAST
Regioni298 – 707410Necessary for speckles and matrix localizationBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi163 – 767605Arg-richAdd
BLAST
Compositional biasi276 – 500225Ser-richAdd
BLAST
Compositional biasi309 – 415107Pro-richAdd
BLAST
Compositional biasi562 – 839278Pro-richAdd
BLAST
Compositional biasi850 – 87627Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 PWI domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2146. Eukaryota.
ENOG4111IMU. LUCA.
HOGENOMiHOG000168326.
HOVERGENiHBG054044.
InParanoidiQ52KI8.
KOiK13171.

Family and domain databases

Gene3Di1.20.1390.10. 1 hit.
InterProiIPR002483. PWI_dom.
[Graphical view]
PfamiPF01480. PWI. 1 hit.
[Graphical view]
SMARTiSM00311. PWI. 1 hit.
[Graphical view]
SUPFAMiSSF101233. SSF101233. 1 hit.
PROSITEiPS51025. PWI. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q52KI8-1) [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
MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP
60 70 80 90 100
WITKRVTEIL GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE
110 120 130 140 150
FMGELWPLLL SAQENIAGIP SAFLELKKEE IKQRQIEQEK LASLKKQDED
160 170 180 190 200
KDKRDKEEKE SSREKRERSR SPRRRKSRSP SPRRRSSPVR RERKRSHSRS
210 220 230 240 250
PRHRTKSRSP SPAPEKKEKS PELPEPSVRM KDSSVQEATS TSDILKAPKP
260 270 280 290 300
EPVPEPKEPS PEKNSKKEKE KTRPRSRSRS KSRSRTRSRS PSHTRPRRRH
310 320 330 340 350
RSRSRSYSPR RRPSPRRRPS PRRRTPPRRM PPPPRHRRSR SPGRRRRRSS
360 370 380 390 400
ASLSGSSSSS SSSRSRSPPK KPPKRTSSPP RKTRRLSPSA SPPRRRHRPS
410 420 430 440 450
SPATPPPKTR HSPTPQQSNR TRKSRVSVSP GRTSGKVTKH KGTEKRESPS
460 470 480 490 500
PAPKPRKVEL SESEEDKGSK MAAADSVQQR RQYRRQNQQS SSDSGSSSTS
510 520 530 540 550
EDERPKRSHV KNGEVGRRRR HSPSRSASPS PRKRQKETSP RMQMGKRWQS
560 570 580 590 600
PVTKSSRRRR SPSPPPARRR RSPSPAPPPP PPPPPPRRRR SPTPPPRRRT
610 620 630 640 650
PSPPPRRRSP SPRRYSPPIQ RRYSPSPPPK RRTASPPPPP KRRASPSPPP
660 670 680 690 700
KRRVSHSPPP KQRSPTVTKR RSPSLSSKHR KGSSPGRSTR EARSPQPNKR
710 720 730 740 750
HSPSPRPRAP QTSSPPPVRR GASASPQGRQ SPSPSTRPIR RVSRTPEPKK
760 770 780 790 800
IKKTAMATQR NIRRVSKSPK ADSLSRAASP SPQSVRRVSS SRSVSGSPEP
810 820 830 840 850
AAKKPPAPPS PVQSQSPSTN WSPAVPAKKA KSPTPSLSPA RNSDQEGGGK
860 870 880 890 900
KKKKKKDKKH KKDKKHKKHK KHKKEKAVTI ATPATAAPAA VSAATTTSAQ
910 920 930 940
EEPAAAPEPR KETESEAEDD NLDDLERHLR EKALRSMRKA QVSPQS
Length:946
Mass (Da):106,862
Last modified:September 21, 2011 - v2
Checksum:i41F77542412A9536
GO
Isoform 2 (identifier: Q52KI8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     733-755: Missing.
     911-946: KETESEAEDDNLDDLERHLREKALRSMRKAQVSPQS → EVFTPPLPAV

Show »
Length:897
Mass (Da):101,103
Checksum:iC648F17FBD19FED1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871S → Y in BAB25575 (PubMed:16141072).Curated
Sequence conflicti521 – 5211H → L in AAC17422 (Ref. 1) Curated
Sequence conflicti754 – 7618TAMATQRN → AASPSTRP in AAH94322 (PubMed:15489334).Curated
Sequence conflicti767 – 77610KSPKADSLSR → RTPEPKKIKK in AAH94322 (PubMed:15489334).Curated
Sequence conflicti851 – 8511K → R in AAC17422 (Ref. 1) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei733 – 75523Missing in isoform 2. 1 PublicationVSP_016524Add
BLAST
Alternative sequencei911 – 94636KETES…VSPQS → EVFTPPLPAV in isoform 2. 1 PublicationVSP_016525Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062655 mRNA. Translation: AAC17422.1.
AL627078 Genomic DNA. No translation available.
AL627185 Genomic DNA. No translation available.
BC094322 mRNA. Translation: AAH94322.1.
AK008284 mRNA. Translation: BAB25575.1.
RefSeqiNP_058079.2. NM_016799.3.
UniGeneiMm.1963.

Genome annotation databases

GeneIDi51796.
KEGGimmu:51796.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062655 mRNA. Translation: AAC17422.1.
AL627078 Genomic DNA. No translation available.
AL627185 Genomic DNA. No translation available.
BC094322 mRNA. Translation: AAH94322.1.
AK008284 mRNA. Translation: BAB25575.1.
RefSeqiNP_058079.2. NM_016799.3.
UniGeneiMm.1963.

3D structure databases

ProteinModelPortaliQ52KI8.
SMRiQ52KI8. Positions 27-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206179. 2 interactions.
IntActiQ52KI8. 2 interactions.
MINTiMINT-1867213.
STRINGi10090.ENSMUSP00000125003.

PTM databases

iPTMnetiQ52KI8.
PhosphoSiteiQ52KI8.

Proteomic databases

EPDiQ52KI8.
MaxQBiQ52KI8.
PaxDbiQ52KI8.
PeptideAtlasiQ52KI8.
PRIDEiQ52KI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi51796.
KEGGimmu:51796.

Organism-specific databases

CTDi10250.
MGIiMGI:1858303. Srrm1.

Phylogenomic databases

eggNOGiKOG2146. Eukaryota.
ENOG4111IMU. LUCA.
HOGENOMiHOG000168326.
HOVERGENiHBG054044.
InParanoidiQ52KI8.
KOiK13171.

Miscellaneous databases

ChiTaRSiSrrm1. mouse.
PROiQ52KI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ52KI8.
CleanExiMM_SRRM1.

Family and domain databases

Gene3Di1.20.1390.10. 1 hit.
InterProiIPR002483. PWI_dom.
[Graphical view]
PfamiPF01480. PWI. 1 hit.
[Graphical view]
SMARTiSM00311. PWI. 1 hit.
[Graphical view]
SUPFAMiSSF101233. SSF101233. 1 hit.
PROSITEiPS51025. PWI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Vayssiere B.M., Camonis J.H.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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 1).
    Strain: C57BL/6J and NMRI.
    Tissue: Mammary tumor.
  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] OF 1-265 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Small intestine.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572 AND SER-574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572; SER-713; SER-779; SER-810; SER-816; SER-822; THR-913 AND SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427; SER-429; SER-795 AND SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-220; SER-260; SER-572; SER-574; SER-616; SER-714; SER-723; SER-725; SER-731; SER-810; SER-816; SER-822; THR-913 AND SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-260; SER-391; SER-427; SER-429; SER-572; THR-633; SER-635; SER-657; SER-713; SER-714; SER-723; SER-725; SER-733; SER-779; SER-797; SER-810; SER-814; SER-816; SER-818; THR-819; SER-822; SER-832; THR-834; SER-836; SER-838; SER-843; THR-913 AND SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "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-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. Cited for: CITRULLINATION AT ARG-7.

Entry informationi

Entry nameiSRRM1_MOUSE
AccessioniPrimary (citable) accession number: Q52KI8
Secondary accession number(s): E9QNW8, O70495, Q9CVG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: September 21, 2011
Last modified: July 6, 2016
This is version 106 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

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 one 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.