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Q69ZA1

- CDK13_MOUSE

UniProt

Q69ZA1 - CDK13_MOUSE

Protein

Cyclin-dependent kinase 13

Gene

Cdk13

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis.1 Publication

    Catalytic activityi

    ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei734 – 7341ATPPROSITE-ProRule annotation
    Active sitei837 – 8371Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi711 – 7199ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin binding Source: UniProtKB
    3. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    4. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

    GO - Biological processi

    1. alternative mRNA splicing, via spliceosome Source: UniProtKB
    2. hemopoiesis Source: UniProtKB
    3. phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase 13 (EC:2.7.11.22, EC:2.7.11.23)
    Alternative name(s):
    CDC2-related protein kinase 5
    Cell division cycle 2-like protein kinase 5
    Cell division protein kinase 13
    Gene namesi
    Name:Cdk13
    Synonyms:Cdc2l5, Kiaa1791
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1916812. Cdk13.

    Subcellular locationi

    Nucleus speckle By similarity

    GO - Cellular componenti

    1. cyclin K-CDK13 complex Source: Ensembl
    2. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
    3. nuclear speck Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15111511Cyclin-dependent kinase 13PRO_0000085712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei316 – 3161PhosphoserineBy similarity
    Modified residuei318 – 3181PhosphoserineBy similarity
    Modified residuei326 – 3261PhosphoserineBy similarity
    Modified residuei341 – 3411PhosphoserineBy similarity
    Modified residuei343 – 3431PhosphoserineBy similarity
    Modified residuei384 – 3841PhosphoserineBy similarity
    Modified residuei396 – 3961PhosphoserineBy similarity
    Modified residuei398 – 3981PhosphoserineBy similarity
    Modified residuei401 – 4011PhosphoserineBy similarity
    Modified residuei438 – 4381Phosphoserine1 Publication
    Modified residuei440 – 4401PhosphoserineBy similarity
    Modified residuei526 – 5261PhosphoserineBy similarity
    Modified residuei557 – 5571N6-acetyllysineBy similarity
    Modified residuei871 – 8711PhosphothreonineBy similarity
    Modified residuei1048 – 10481PhosphoserineBy similarity
    Modified residuei1245 – 12451PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ69ZA1.
    PaxDbiQ69ZA1.
    PRIDEiQ69ZA1.

    PTM databases

    PhosphoSiteiQ69ZA1.

    Expressioni

    Gene expression databases

    BgeeiQ69ZA1.
    GenevestigatoriQ69ZA1.

    Interactioni

    Subunit structurei

    Interacts with C1QBP By similarity. Interacts with CCNK, CCNL1 and CCNL2.By similarity2 Publications

    Protein-protein interaction databases

    IntActiQ69ZA1. 1 interaction.
    MINTiMINT-4113604.
    STRINGi10090.ENSMUSP00000036013.

    Structurei

    3D structure databases

    ProteinModelPortaliQ69ZA1.
    SMRiQ69ZA1. Positions 696-1024.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini705 – 998294Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114964.
    HOGENOMiHOG000049118.
    HOVERGENiHBG050851.
    InParanoidiQ69ZA1.
    KOiK08819.
    OMAiKERHREH.
    OrthoDBiEOG76DTSM.
    TreeFamiTF101060.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q69ZA1-1) [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

    MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ     50
    PPPPPPPLLF LAAPGAAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRPG 100
    GRQKRRRGPR AGQEAEKRRV FSLPQPQQDG GGGASSGGGV TPLVEYEDVS 150
    SQSEQGLLLG GASAATAATA AGGTGGNGGS PASSSGTQRR AEGSERRPRR 200
    DRRSSSGRSK ERHREHRRRD GTRSGSEASK ARSRHGHSGE ERAEAAKSGS 250
    SSSSGGRRKS ASATSSSSSS RKDRDLKAHR SRTKSSKEPP SAYKEPPKAY 300
    REDKSEPKAY RRRQRSLSPL GGRDESPVSH RASQSLRSRK SPSPAGGGSS 350
    PYSRRLPRSP SPYSRRRSPS YSRHSSYERG GDVSPSPYSS SSWRRSRSPY 400
    SPVLRRSAKS RSRSPYSSRH SRSRSRHRLS RSRSRHSSIS PSTLTLKSSL 450
    AAELNKNKKA RAAEAARAAE AAKAAEAAKA AEAAAKAAKA SNASTPTKGN 500
    TETGASVSQT NHVKEVKKLK TEHAPSPSSG GTVKSDKAKT KPPLQVTKVD 550
    NNLTVEKATK KTVVGKESKP AATKEEPVST KEKSKPLTPS TGAKEKEQHV 600
    ALVTSTLPPL PLPPMLPEDK DADSLRGNIS VKAVKKEVEK KLRCLLADLP 650
    LPPELPGGDD LSKSPEEKKT AAQLHSKRRP KICGPRYGEI KEKDIDWGKR 700
    CVDKFDIIGI IGEGTYGQVY KARDKDTGEM VALKKVRLDN EKEGFPITAI 750
    REIKILRQLT HQSIINMKEI VTDKEDALDF KKDKGAFYLV FEYMDHDLMG 800
    LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC SNILLNNRGQ 850
    IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC 900
    GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM 950
    KPKKQYRRKL REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD 1000
    VEPSKMPPPD LPLWQDCHEL WSKKRRRQKQ MGMTDDLSTI KAPRKDLSLG 1050
    LDDSRTNTPQ GVLPPAQLKS QSNSNVAPVI TGPGQPLNHS ELAILLNLLQ 1100
    SKSSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE KQTDPSTPQQ 1150
    ESSKSLGGVQ PSQTIQPKVE TDAAQAAVQS AFAVLLTQLI KAQQSKQKDA 1200
    MLEERENGSG HEAPLQLRPP LEPSTPGSGQ DDLIQHQDRR ILELTPEPDR 1250
    PRILPPDQRP PEPPEPPPVT EEDLDYRTEN QHVPTTSSSL TDPHAGVKAA 1300
    LLQLLAQHQP QDDPKREGGI DYPTGDTYVP SSDYKDNFGS SFSAAPYVSS 1350
    DGLGSSSAAA PLEARSFIGN SDIQSLDNYS TASSHTGGPP QTSAFTESFA 1400
    SSVAGYGDIY LNAGPMLFSG DKDHRFEYSH GPITVLTNSN DPSTGPESTH 1450
    PLPAKMHNYN YGGNLQENPG GPSLMHGQTW TSPAQGPGYS QGYRGHISTS 1500
    AGRGRGRGLP Y 1511
    Length:1,511
    Mass (Da):164,553
    Last modified:July 27, 2011 - v3
    Checksum:iEAF4438ABB5063CE
    GO
    Isoform 2 (identifier: Q69ZA1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1079-1138: Missing.

    Show »
    Length:1,451
    Mass (Da):158,133
    Checksum:i83560368EE52A192
    GO

    Sequence cautioni

    The sequence BAC29077.1 differs from that shown. Reason: Frameshift at positions 633 and 666.
    The sequence AAH32179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC29077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD32543.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731A → V in BAD32543. (PubMed:15368895)Curated
    Sequence conflicti103 – 1031Q → R in BAD32543. (PubMed:15368895)Curated
    Sequence conflicti637 – 6371E → K in BAC29077. (PubMed:16141072)Curated
    Sequence conflicti1009 – 10091P → L in BAD32543. (PubMed:15368895)Curated
    Sequence conflicti1206 – 12061E → K in AAH32179. (PubMed:15489334)Curated
    Sequence conflicti1400 – 14001A → P in AAH51093. (PubMed:15489334)Curated
    Sequence conflicti1464 – 14641N → D in BAC29077. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1079 – 113860Missing in isoform 2. 2 PublicationsVSP_013580Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK173265 mRNA. Translation: BAD32543.1. Different initiation.
    AC154219 Genomic DNA. No translation available.
    AC154828 Genomic DNA. No translation available.
    AK035493 mRNA. Translation: BAC29077.1. Sequence problems.
    BC032179 mRNA. Translation: AAH32179.1. Different initiation.
    BC051093 mRNA. Translation: AAH51093.1.
    CCDSiCCDS36604.1. [Q69ZA1-1]
    RefSeqiNP_001074527.1. NM_001081058.2. [Q69ZA1-1]
    NP_081394.1. NM_027118.1. [Q69ZA1-2]
    UniGeneiMm.193924.

    Genome annotation databases

    EnsembliENSMUST00000042365; ENSMUSP00000036013; ENSMUSG00000041297. [Q69ZA1-1]
    GeneIDi69562.
    KEGGimmu:69562.
    UCSCiuc007poc.2. mouse. [Q69ZA1-1]
    uc007pod.2. mouse. [Q69ZA1-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK173265 mRNA. Translation: BAD32543.1 . Different initiation.
    AC154219 Genomic DNA. No translation available.
    AC154828 Genomic DNA. No translation available.
    AK035493 mRNA. Translation: BAC29077.1 . Sequence problems.
    BC032179 mRNA. Translation: AAH32179.1 . Different initiation.
    BC051093 mRNA. Translation: AAH51093.1 .
    CCDSi CCDS36604.1. [Q69ZA1-1 ]
    RefSeqi NP_001074527.1. NM_001081058.2. [Q69ZA1-1 ]
    NP_081394.1. NM_027118.1. [Q69ZA1-2 ]
    UniGenei Mm.193924.

    3D structure databases

    ProteinModelPortali Q69ZA1.
    SMRi Q69ZA1. Positions 696-1024.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q69ZA1. 1 interaction.
    MINTi MINT-4113604.
    STRINGi 10090.ENSMUSP00000036013.

    PTM databases

    PhosphoSitei Q69ZA1.

    Proteomic databases

    MaxQBi Q69ZA1.
    PaxDbi Q69ZA1.
    PRIDEi Q69ZA1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000042365 ; ENSMUSP00000036013 ; ENSMUSG00000041297 . [Q69ZA1-1 ]
    GeneIDi 69562.
    KEGGi mmu:69562.
    UCSCi uc007poc.2. mouse. [Q69ZA1-1 ]
    uc007pod.2. mouse. [Q69ZA1-2 ]

    Organism-specific databases

    CTDi 8621.
    MGIi MGI:1916812. Cdk13.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114964.
    HOGENOMi HOG000049118.
    HOVERGENi HBG050851.
    InParanoidi Q69ZA1.
    KOi K08819.
    OMAi KERHREH.
    OrthoDBi EOG76DTSM.
    TreeFami TF101060.

    Miscellaneous databases

    NextBioi 329780.
    PROi Q69ZA1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q69ZA1.
    Genevestigatori Q69ZA1.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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 PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Embryonic tail.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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 295-1511 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Urinary bladder.
    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] OF 891-1511 (ISOFORMS 1 AND 2).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "CDK13/CDC2L5 interacts with L-type cyclins and regulates alternative splicing."
      Chen H.H., Wong Y.H., Geneviere A.M., Fann M.J.
      Biochem. Biophys. Res. Commun. 354:735-740(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCNL1 AND CCNL2.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    8. "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes."
      Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P., Luo Z., Cimermancic P., Ule J., Peterlin B.M.
      Genes Dev. 25:2158-2172(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNK.

    Entry informationi

    Entry nameiCDK13_MOUSE
    AccessioniPrimary (citable) accession number: Q69ZA1
    Secondary accession number(s): E9QKZ6
    , Q80V11, Q8BZG1, Q8K0A4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 105 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