Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q69ZA1

- CDK13_MOUSE

UniProt

Q69ZA1 - CDK13_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cyclin-dependent kinase 13

Gene

Cdk13

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

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. poly(A) RNA binding Source: Ensembl
  5. 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
Complete GO annotation...

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. extracellular space Source: Ensembl
  3. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  4. nuclear speck Source: UniProtKB
Complete GO annotation...

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.
ExpressionAtlasiQ69ZA1. baseline and differential.
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 696-1026.
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.
GeneTreeiENSGT00760000119290.
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.
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

        10         20         30         40         50
MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ
60 70 80 90 100
PPPPPPPLLF LAAPGAAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRPG
110 120 130 140 150
GRQKRRRGPR AGQEAEKRRV FSLPQPQQDG GGGASSGGGV TPLVEYEDVS
160 170 180 190 200
SQSEQGLLLG GASAATAATA AGGTGGNGGS PASSSGTQRR AEGSERRPRR
210 220 230 240 250
DRRSSSGRSK ERHREHRRRD GTRSGSEASK ARSRHGHSGE ERAEAAKSGS
260 270 280 290 300
SSSSGGRRKS ASATSSSSSS RKDRDLKAHR SRTKSSKEPP SAYKEPPKAY
310 320 330 340 350
REDKSEPKAY RRRQRSLSPL GGRDESPVSH RASQSLRSRK SPSPAGGGSS
360 370 380 390 400
PYSRRLPRSP SPYSRRRSPS YSRHSSYERG GDVSPSPYSS SSWRRSRSPY
410 420 430 440 450
SPVLRRSAKS RSRSPYSSRH SRSRSRHRLS RSRSRHSSIS PSTLTLKSSL
460 470 480 490 500
AAELNKNKKA RAAEAARAAE AAKAAEAAKA AEAAAKAAKA SNASTPTKGN
510 520 530 540 550
TETGASVSQT NHVKEVKKLK TEHAPSPSSG GTVKSDKAKT KPPLQVTKVD
560 570 580 590 600
NNLTVEKATK KTVVGKESKP AATKEEPVST KEKSKPLTPS TGAKEKEQHV
610 620 630 640 650
ALVTSTLPPL PLPPMLPEDK DADSLRGNIS VKAVKKEVEK KLRCLLADLP
660 670 680 690 700
LPPELPGGDD LSKSPEEKKT AAQLHSKRRP KICGPRYGEI KEKDIDWGKR
710 720 730 740 750
CVDKFDIIGI IGEGTYGQVY KARDKDTGEM VALKKVRLDN EKEGFPITAI
760 770 780 790 800
REIKILRQLT HQSIINMKEI VTDKEDALDF KKDKGAFYLV FEYMDHDLMG
810 820 830 840 850
LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC SNILLNNRGQ
860 870 880 890 900
IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC
910 920 930 940 950
GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM
960 970 980 990 1000
KPKKQYRRKL REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD
1010 1020 1030 1040 1050
VEPSKMPPPD LPLWQDCHEL WSKKRRRQKQ MGMTDDLSTI KAPRKDLSLG
1060 1070 1080 1090 1100
LDDSRTNTPQ GVLPPAQLKS QSNSNVAPVI TGPGQPLNHS ELAILLNLLQ
1110 1120 1130 1140 1150
SKSSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE KQTDPSTPQQ
1160 1170 1180 1190 1200
ESSKSLGGVQ PSQTIQPKVE TDAAQAAVQS AFAVLLTQLI KAQQSKQKDA
1210 1220 1230 1240 1250
MLEERENGSG HEAPLQLRPP LEPSTPGSGQ DDLIQHQDRR ILELTPEPDR
1260 1270 1280 1290 1300
PRILPPDQRP PEPPEPPPVT EEDLDYRTEN QHVPTTSSSL TDPHAGVKAA
1310 1320 1330 1340 1350
LLQLLAQHQP QDDPKREGGI DYPTGDTYVP SSDYKDNFGS SFSAAPYVSS
1360 1370 1380 1390 1400
DGLGSSSAAA PLEARSFIGN SDIQSLDNYS TASSHTGGPP QTSAFTESFA
1410 1420 1430 1440 1450
SSVAGYGDIY LNAGPMLFSG DKDHRFEYSH GPITVLTNSN DPSTGPESTH
1460 1470 1480 1490 1500
PLPAKMHNYN YGGNLQENPG GPSLMHGQTW TSPAQGPGYS QGYRGHISTS
1510
AGRGRGRGLP Y
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 696-1026.
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 ENSGT00760000119290.
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.
ExpressionAtlasi Q69ZA1. baseline and differential.
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.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 106 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