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Q61136

- PRP4B_MOUSE

UniProt

Q61136 - PRP4B_MOUSE

Protein

Serine/threonine-protein kinase PRP4 homolog

Gene

Prpf4b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei717 – 7171ATPPROSITE-ProRule annotation
    Active sitei815 – 8151Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi693 – 7019ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein kinase activity Source: MGI
    3. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. RNA splicing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PRP4 homolog (EC:2.7.11.1)
    Alternative name(s):
    PRP4 pre-mRNA-processing factor 4 homolog
    Pre-mRNA protein kinase
    Gene namesi
    Name:Prpf4b
    Synonyms:Cbp143, Prp4h, Prp4k, Prp4m, Prpk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:109584. Prpf4b.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: Ensembl
    2. chromosome Source: MGI

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10071006Serine/threonine-protein kinase PRP4 homologPRO_0000086587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei21 – 211PhosphoserineBy similarity
    Modified residuei24 – 241PhosphoserineBy similarity
    Modified residuei33 – 331PhosphoserineBy similarity
    Modified residuei88 – 881Phosphoserine1 Publication
    Modified residuei94 – 941Phosphoserine1 Publication
    Modified residuei100 – 1001N6-acetyllysine1 Publication
    Modified residuei141 – 1411PhosphotyrosineBy similarity
    Modified residuei143 – 1431PhosphoserineBy similarity
    Modified residuei145 – 1451PhosphoserineBy similarity
    Modified residuei240 – 2401PhosphoserineBy similarity
    Modified residuei242 – 2421PhosphoserineBy similarity
    Modified residuei258 – 2581PhosphoserineBy similarity
    Modified residuei278 – 2781PhosphoserineBy similarity
    Modified residuei294 – 2941PhosphoserineBy similarity
    Modified residuei328 – 3281PhosphoserineBy similarity
    Modified residuei354 – 3541PhosphoserineBy similarity
    Modified residuei356 – 3561PhosphoserineBy similarity
    Modified residuei366 – 3661PhosphoserineBy similarity
    Modified residuei368 – 3681PhosphoserineBy similarity
    Modified residuei385 – 3851PhosphothreonineBy similarity
    Modified residuei387 – 3871PhosphoserineBy similarity
    Modified residuei427 – 4271PhosphoserineBy similarity
    Modified residuei431 – 4311Phosphoserine1 Publication
    Modified residuei437 – 4371Phosphoserine1 Publication
    Modified residuei518 – 5181PhosphoserineBy similarity
    Modified residuei519 – 5191PhosphoserineBy similarity
    Modified residuei520 – 5201PhosphoserineBy similarity
    Modified residuei565 – 5651PhosphoserineBy similarity
    Modified residuei569 – 5691PhosphoserineBy similarity
    Modified residuei576 – 5761Phosphoserine1 Publication
    Modified residuei578 – 5781Phosphoserine1 Publication
    Modified residuei580 – 5801Phosphoserine1 Publication
    Modified residuei717 – 7171N6-acetyllysineBy similarity
    Modified residuei849 – 8491Phosphotyrosine2 Publications
    Modified residuei852 – 8521PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by Clk1.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ61136.
    PaxDbiQ61136.
    PRIDEiQ61136.

    PTM databases

    PhosphoSiteiQ61136.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61136.
    BgeeiQ61136.
    GenevestigatoriQ61136.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex By similarity. Interacts with Clk1 C-terminus.By similarity

    Protein-protein interaction databases

    BioGridi202400. 2 interactions.
    IntActiQ61136. 3 interactions.
    MINTiMINT-1751441.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61136.
    SMRiQ61136. Positions 603-1005.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini687 – 1006320Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi40 – 497458Arg/Lys-rich (basic)Add
    BLAST
    Compositional biasi41 – 7939His-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00580000081366.
    HOVERGENiHBG055182.
    InParanoidiB2RUN6.
    KOiK08827.
    OMAiRSEIDKE.
    OrthoDBiEOG76HQ1K.
    TreeFamiTF315246.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q61136-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAATEPPSLR EQAEMDDADN SEKSVNEENG EVSEDQSQNK HSRHKKKKHK     50
    HRSKHKKHKH SSEEDRDKKH KHKHKHKKHK RKEVIEASDK EGLSPAKRTK 100
    LDDLALLEDL EKQRALIKAE LDNELMEGKV QSGMGLILQG YESGSEEEGE 150
    IHEKARNGNR SSTRSSSTRG KLEITDNKNS AKKRSKSRSK ERTRHRSDKR 200
    KSKGAGEMLR EKANRSKSKE RRKSKSPSKR SKSQDQARKS KSPPLRRRSQ 250
    EKVGKARSPA EEKMKSEEKG KIKDRKKSPI VNERSRDRSK KSKSPVDLRD 300
    KSKDRRSRSK ERKSKRSEID KEKKPIKSPS KDASSGKENR SPSRRPGRSP 350
    KRRSLSPKLR DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK 400
    RREPERRRLS SPRTRPRDDI LGRCERSKDA SPINRWSPTR RRSRSPIRRR 450
    SRSPLRRSRS PRRRSRSPRR RDRSRRSRSR LRRRSRSRGG HRRRSRSKVK 500
    EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ RRIQRQAIVQ 550
    KYKYLAEDSN ISVPSEPSSP QSSTRSRSPS PDDILERVAA DVKEYERENV 600
    DTFEASVKAK HNLMTVEQNN GSSQKKILAP DMFTESDDMF AAYFDSARLR 650
    AAGIGKDFKE NPNLRDNWTD AEGYYRVNIG EVLDKRYNVY GYTGQGVFSN 700
    VVRARDNARA NQEVAVKIIR NNELMQKTGL KELEFLKKLN DADPDDKFHC 750
    LRLFRHFYHK QHLCLVFEPL SMNLREVLKK YGKDVGLHIK AVRSYSQQLF 800
    LALKLLKRCN ILHADIKPDN ILVNESKTIL KLCDFGSASH VADNDITPYL 850
    VSRFYRAPEI IIGKSYDYGI DMWSVGCTLY ELYTGKILFP GKTNNHMLKL 900
    AMDLKGKMPN KMIRKGVFKD QHFDQNLNFM YIEVDKVTER EKVTVMSTIN 950
    PTKDLLADLI GCQRLPEDQR KKVHQLKDLL DQILMLDPAK RISINQALQH 1000
    AFIQEKI 1007
    Length:1,007
    Mass (Da):116,976
    Last modified:July 27, 2011 - v3
    Checksum:i18E1B7371E17AB4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1873SKS → IPG in AAC32042. (PubMed:9701556)Curated
    Sequence conflicti223 – 2231K → I in AAC32042. (PubMed:9701556)Curated
    Sequence conflicti478 – 4781R → K in AAM19102. (PubMed:12077342)Curated
    Sequence conflicti478 – 4781R → K in AAC32042. (PubMed:9701556)Curated
    Sequence conflicti633 – 6331F → L in AAB03269. (PubMed:9102632)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF283466 mRNA. Translation: AAM19102.1.
    AK020579 mRNA. Translation: BAB32137.3.
    AK021274 mRNA. Translation: BAB32358.3.
    AK083926 mRNA. Translation: BAC39069.1.
    CH466546 Genomic DNA. Translation: EDL40895.1.
    BC141272 mRNA. Translation: AAI41273.1.
    BC141273 mRNA. Translation: AAI41274.1.
    AF033663 mRNA. Translation: AAC32042.1.
    U48737 mRNA. Translation: AAB03269.1.
    CCDSiCCDS26448.1.
    RefSeqiNP_038858.2. NM_013830.2.
    UniGeneiMm.10027.
    Mm.482253.

    Genome annotation databases

    EnsembliENSMUST00000077853; ENSMUSP00000077019; ENSMUSG00000021413.
    GeneIDi19134.
    KEGGimmu:19134.
    UCSCiuc007qbp.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF283466 mRNA. Translation: AAM19102.1 .
    AK020579 mRNA. Translation: BAB32137.3 .
    AK021274 mRNA. Translation: BAB32358.3 .
    AK083926 mRNA. Translation: BAC39069.1 .
    CH466546 Genomic DNA. Translation: EDL40895.1 .
    BC141272 mRNA. Translation: AAI41273.1 .
    BC141273 mRNA. Translation: AAI41274.1 .
    AF033663 mRNA. Translation: AAC32042.1 .
    U48737 mRNA. Translation: AAB03269.1 .
    CCDSi CCDS26448.1.
    RefSeqi NP_038858.2. NM_013830.2.
    UniGenei Mm.10027.
    Mm.482253.

    3D structure databases

    ProteinModelPortali Q61136.
    SMRi Q61136. Positions 603-1005.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202400. 2 interactions.
    IntActi Q61136. 3 interactions.
    MINTi MINT-1751441.

    PTM databases

    PhosphoSitei Q61136.

    Proteomic databases

    MaxQBi Q61136.
    PaxDbi Q61136.
    PRIDEi Q61136.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000077853 ; ENSMUSP00000077019 ; ENSMUSG00000021413 .
    GeneIDi 19134.
    KEGGi mmu:19134.
    UCSCi uc007qbp.2. mouse.

    Organism-specific databases

    CTDi 8899.
    MGIi MGI:109584. Prpf4b.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00580000081366.
    HOVERGENi HBG055182.
    InParanoidi B2RUN6.
    KOi K08827.
    OMAi RSEIDKE.
    OrthoDBi EOG76HQ1K.
    TreeFami TF315246.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 3474.

    Miscellaneous databases

    NextBioi 295762.
    PROi Q61136.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61136.
    Bgeei Q61136.
    Genevestigatori Q61136.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mammalian PRP4 kinase copurifies and interacts with components of both the U5 snRNP and the N-CoR deacetylase complexes."
      Dellaire G., Makarov E.M., Cowger J.J.M., Longman D., Sutherland H.G.E., Luehrmann R., Torchia J., Bickmore W.A.
      Mol. Cell. Biol. 22:5141-5156(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Strain: C57BL/6J.
      Tissue: Hippocampus, Spinal ganglion and Urinary bladder.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. "Capturing novel mouse genes encoding chromosomal and other nuclear proteins."
      Tate P., Lee M., Tweedie S., Skarnes W.C., Bickmore W.A.
      J. Cell Sci. 111:2575-2585(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 185-1007.
    6. "Functional analysis of the fission yeast Prp4 protein kinase involved in pre-mRNA splicing and isolation of a putative mammalian homologue."
      Gross T., Lutzelberger M., Wiegmann H., Klingenhoff A., Shenoy S., Kaeufer N.F.
      Nucleic Acids Res. 25:1028-1035(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 512-1007.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578 AND SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    11. "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-88; SER-94; SER-431; SER-437 AND TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "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-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPRP4B_MOUSE
    AccessioniPrimary (citable) accession number: Q61136
    Secondary accession number(s): B2RUN6
    , O88378, Q8BND8, Q8R4Y5, Q9CTL9, Q9CTT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 134 of the entry and version 3 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3