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Protein

PAS domain-containing serine/threonine-protein kinase

Gene

Pask

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

Functioni

Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Protein kinase activity is inhibited by the first PAS domain: binding of an unidentified ligand desinhibits the protein kinase activity. May be activated by autophosphorylation on Thr-1221 and Thr-1225. Autophosphorylation is enhanced upon phosphatidylinositol monophosphate (phosphatidylinositol 4-phosphate) binding and inhibited upon phosphatidylinositol bi- and tri-phosphate binding. In contrast, phosphorylation of target proteins is inhibited upon all phosphatidylinositol-binding (phosphatidylinositol mono- bi- and tri-phosphate) (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1088 – 10881ATPPROSITE-ProRule annotation
Active sitei1188 – 11881Proton acceptorPROSITE-ProRule annotation
Binding sitei1206 – 12061ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1065 – 10739ATPPROSITE-ProRule annotation
Nucleotide bindingi1142 – 11498ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • negative regulation of glycogen biosynthetic process Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of energy homeostasis Source: UniProtKB
  • regulation of glucagon secretion Source: UniProtKB
  • regulation of respiratory gaseous exchange Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
PAS domain-containing serine/threonine-protein kinase (EC:2.7.11.1)
Short name:
PAS-kinase
Short name:
PASKIN
Gene namesi
Name:Pask
Synonyms:Kiaa0135
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2155936. Pask.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal conditions: mice show normal development, growth and reproduction. Fertility and sperm production and motility are not affected in males. Under high-fat diet, mice seem to be protected from deleterious effects, including obesity, liver triglyceride accumulation and insulin resistance (PubMed:17878307). In contrast, the lean phenotype appears only after feeding a high-fat diet: under normal chow diet, body weight, fat composition, oxygen consumption are not distinguishable from wild-type mice (PubMed:17192472). The only difference between these 2 experiments is that mice were backcrossed into C57BL/6 5 times in the first study (PubMed:17878307), while the 10th backcross was used in the second study (PubMed:17192472). Female but not male mice show an increased ventilatory response to acute hypoxia and fail to reach ventilatory acclimatization to chronic hypoxia.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13831383PAS domain-containing serine/threonine-protein kinasePRO_0000086481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei31 – 311PhosphothreonineCombined sources
Modified residuei1221 – 12211Phosphothreonine; by autocatalysisBy similarity
Modified residuei1225 – 12251Phosphothreonine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated on Thr-1221 and Thr-1225. Autophosphorylation is activated by phospholipids (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CEE6.
MaxQBiQ8CEE6.
PaxDbiQ8CEE6.
PRIDEiQ8CEE6.

PTM databases

iPTMnetiQ8CEE6.
PhosphoSiteiQ8CEE6.

Expressioni

Tissue specificityi

Ubiquitously expressed. Strongly up-regulated in postmeiotic germ cells during spermatogenesis.1 Publication

Gene expression databases

BgeeiQ8CEE6.
CleanExiMM_PASK.
ExpressionAtlasiQ8CEE6. baseline and differential.
GenevisibleiQ8CEE6. MM.

Interactioni

Protein-protein interaction databases

BioGridi234624. 1 interaction.
STRINGi10090.ENSMUSP00000027493.

Structurei

3D structure databases

ProteinModelPortaliQ8CEE6.
SMRiQ8CEE6. Positions 129-235, 1013-1355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 18872PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini333 – 40068PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 1311253Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain mediates binding to phosphatidylinositol.By similarity

Sequence similaritiesi

Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1152. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000115456.
HOVERGENiHBG047936.
InParanoidiQ8CEE6.
KOiK08801.
OMAiVANDKAC.
OrthoDBiEOG76HQ0W.
TreeFamiTF323242.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13426. PAS_9. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
SSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50112. PAS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CEE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDRGPPVFA EDWKCLSESP PVQEGPAAQA TFEPSKPLSI AHKHLSRKNG
60 70 80 90 100
LSRLCQSRMA LSEDRWSSYC LSSLAAQNIC TSKLHCAAAP EYADPTAGPL
110 120 130 140 150
GSTSCCSLLR GLASGCSGSL LSTPVCNPNK AVFTVDAKTT EILVANDKAC
160 170 180 190 200
SLLGYSSHDL IGQKLAQFFL KSDSEVVEAL SEEHVEADGH AAVVFGTVVD
210 220 230 240 250
IVSRIGEKIP VSVWIKRLQQ DRGLCCVVVL EPVERVSAWV AFQSDGTITS
260 270 280 290 300
CDSLFAHLHG FTSPKDVVGQ CVIDLIPSMQ LPPPGQHIPK SLKIQRSVGR
310 320 330 340 350
ARDGTTFPLS LKLKSKPSGR AVADSEAASE PGYQASVWVF CTISGLITLL
360 370 380 390 400
PDGTIYGVNH SFALMLFGYG KTELLGKNIT FLIPGFYHYM DLTYDSSVQL
410 420 430 440 450
PDLVNCLDIG RKSGPGEMNS DAQHNWELAS GAQGPRIDVV LARDHMPSQD
460 470 480 490 500
ETLKLVGGQV SSRTQTRLET GYKILPSSAC QPSLGVDSNP EDGEQSLLTD
510 520 530 540 550
QQSIPKRNLP AHGGQNQLDT SEISLPVLKE HLLSEIQKNI SEESPLTHRK
560 570 580 590 600
WLSKVQQNPT KGSLPIHEEQ LLFAGQHIHV LGKEDPSAAE SYRESLLEES
610 620 630 640 650
KSKPVDAKLF ASCEDSEPLV SVKDRGSSVD TCNLHQEAQL ELMGVSSPNP
660 670 680 690 700
WADATMPEPH TTGQIAGGSL TYCPQYRSEW ASQQRGQDSA PSPSGMACVL
710 720 730 740 750
LGTPTLDEPW PGVRNDREEL QTCLIKEQLS KSSCEGNLGI SRVELVPEEH
760 770 780 790 800
PPFTAPVSFC DLGGRDLHAS RSGSSSACYA LATDLPGVLE AVEAQEADVN
810 820 830 840 850
SYSWNLKELF LKDQTDRTPS HCSCTTSELS EAPSLSVVGS DLDVGILHRQ
860 870 880 890 900
TSDILVDREM LLLTGTYFDL SEGQRFQEMG AGHDRAELSN ISLVSSEHYE
910 920 930 940 950
TSDIESPGCD PPLPDPGPND MCLSAEKPRP SAQITSTPVA RGATSLQQEI
960 970 980 990 1000
QEGIYSGSCY HRDGLQLSIQ FEVKRVELQG SATLFCCWLV KDLFHSHRDS
1010 1020 1030 1040 1050
ATRTRLFLAS LPSSTHSMPE LSGSSFGEVL RAKPWFEESP TPAELEGLAA
1060 1070 1080 1090 1100
CEGEYDYKYN TISPLGSGAF GFVWTAVEKE CNKEVVVKFI KKEKVLEDCW
1110 1120 1130 1140 1150
IEDPKLGRVT LEIAILSKVD HANIIKVLDI FENQEFFQLV MEKHGSGMDL
1160 1170 1180 1190 1200
FAFIDHHPCL DEPLASFIFR QLVSAVGYLH SQGIIHRDIK DENIVIAEDF
1210 1220 1230 1240 1250
TIKLIDFGSA AYLERGKLFY TFCGTIEYCA PEVLIGNPYR GPELEMWSLG
1260 1270 1280 1290 1300
VTLYTLIFEE NPFCEVEETM EAVIHPPFLV SQELMSLLSG LLQPCPEQRT
1310 1320 1330 1340 1350
TLEKLIRDPW VTQPVNLASY TWEEVCRTNQ PESGLLSAAS LEIGSRSPSE
1360 1370 1380
MAQREGLCGP PAPRETRGDQ HCLHLKDPSL PVS
Length:1,383
Mass (Da):151,250
Last modified:July 27, 2011 - v3
Checksum:iD020885E8C2C2E19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti587 – 5871S → L in BAC25951 (PubMed:16141072).Curated
Sequence conflicti832 – 8321A → V in CAC45054 (PubMed:11688972).Curated
Sequence conflicti832 – 8321A → V in BAC97873 (PubMed:14621295).Curated
Sequence conflicti1186 – 11861H → R in BAC25951 (PubMed:16141072).Curated
Sequence conflicti1293 – 12931Q → H in BAC25951 (PubMed:16141072).Curated
Sequence conflicti1296 – 12961P → L in CAC45054 (PubMed:11688972).Curated
Sequence conflicti1330 – 13301Q → H in BAC25951 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ318757 Genomic DNA. Translation: CAC45054.2.
AK028435 mRNA. Translation: BAC25951.1.
AK129063 mRNA. Translation: BAC97873.1.
AC124669 Genomic DNA. No translation available.
CCDSiCCDS15186.1.
RefSeqiNP_543126.2. NM_080850.2.
XP_006529728.1. XM_006529665.2.
XP_006529729.1. XM_006529666.2.
XP_006529730.1. XM_006529667.2.
UniGeneiMm.379454.

Genome annotation databases

EnsembliENSMUST00000027493; ENSMUSP00000027493; ENSMUSG00000026274.
GeneIDi269224.
KEGGimmu:269224.
UCSCiuc007cdt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ318757 Genomic DNA. Translation: CAC45054.2.
AK028435 mRNA. Translation: BAC25951.1.
AK129063 mRNA. Translation: BAC97873.1.
AC124669 Genomic DNA. No translation available.
CCDSiCCDS15186.1.
RefSeqiNP_543126.2. NM_080850.2.
XP_006529728.1. XM_006529665.2.
XP_006529729.1. XM_006529666.2.
XP_006529730.1. XM_006529667.2.
UniGeneiMm.379454.

3D structure databases

ProteinModelPortaliQ8CEE6.
SMRiQ8CEE6. Positions 129-235, 1013-1355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234624. 1 interaction.
STRINGi10090.ENSMUSP00000027493.

PTM databases

iPTMnetiQ8CEE6.
PhosphoSiteiQ8CEE6.

Proteomic databases

EPDiQ8CEE6.
MaxQBiQ8CEE6.
PaxDbiQ8CEE6.
PRIDEiQ8CEE6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027493; ENSMUSP00000027493; ENSMUSG00000026274.
GeneIDi269224.
KEGGimmu:269224.
UCSCiuc007cdt.2. mouse.

Organism-specific databases

CTDi23178.
MGIiMGI:2155936. Pask.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1152. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000115456.
HOVERGENiHBG047936.
InParanoidiQ8CEE6.
KOiK08801.
OMAiVANDKAC.
OrthoDBiEOG76HQ0W.
TreeFamiTF323242.

Miscellaneous databases

ChiTaRSiPask. mouse.
NextBioi392746.
PROiQ8CEE6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CEE6.
CleanExiMM_PASK.
ExpressionAtlasiQ8CEE6. baseline and differential.
GenevisibleiQ8CEE6. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13426. PAS_9. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
SSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50112. PAS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian PASKIN, a PAS-serine/threonine kinase related to bacterial oxygen sensors."
    Hofer T., Spielmann P., Stengel P., Stier B., Katschinski D.M., Desbaillets I., Gassmann M., Wenger R.H.
    Biochem. Biophys. Res. Commun. 288:757-764(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  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: Liver.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. 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., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  6. "Involvement of Per-Arnt-Sim (PAS) kinase in the stimulation of preproinsulin and pancreatic duodenum homeobox 1 gene expression by glucose."
    da Silva Xavier G., Rutter J., Rutter G.A.
    Proc. Natl. Acad. Sci. U.S.A. 101:8319-8324(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Glucose-stimulated insulin production in mice deficient for the PAS kinase PASKIN."
    Borter E., Niessen M., Zuellig R., Spinas G.A., Spielmann P., Camenisch G., Wenger R.H.
    Diabetes 56:113-117(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Ventilatory responses to acute and chronic hypoxia are altered in female but not male Paskin-deficient mice."
    Soliz J., Soulage C., Borter E., van Patot M.T., Gassmann M.
    Am. J. Physiol. 295:R649-R658(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.
  11. "Per-arnt-sim (PAS) domain-containing protein kinase is downregulated in human islets in type 2 diabetes and regulates glucagon secretion."
    da Silva Xavier G., Farhan H., Kim H., Caxaria S., Johnson P., Hughes S., Bugliani M., Marselli L., Marchetti P., Birzele F., Sun G., Scharfmann R., Rutter J., Siniakowicz K., Weir G., Parker H., Reimann F., Gribble F.M., Rutter G.A.
    Diabetologia 54:819-827(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPASK_MOUSE
AccessioniPrimary (citable) accession number: Q8CEE6
Secondary accession number(s): E9QM58, Q91YD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 123 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

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.