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P68181

- KAPCB_MOUSE

UniProt

P68181 - KAPCB_MOUSE

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Protein
cAMP-dependent protein kinase catalytic subunit beta
Gene
Prkacb, Pkacb
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis By similarity.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Activated by cAMP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATP By similarity
Active sitei167 – 1671Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 589ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. cAMP-dependent protein kinase activity Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: UniProtKB
  2. negative regulation of meiotic cell cycle Source: Ensembl
  3. negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
  4. neural tube closure Source: MGI
  5. protein phosphorylation Source: UniProtKB
  6. regulation of protein processing Source: MGI
  7. response to clozapine Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_203795. DARPP-32 events.
REACT_213852. PKA-mediated phosphorylation of CREB.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase catalytic subunit beta (EC:2.7.11.11)
Short name:
PKA C-beta
Gene namesi
Name:Prkacb
Synonyms:Pkacb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:97594. Prkacb.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity. Nucleus By similarity
Note: Translocates into the nucleus (monomeric catalytic subunit) By similarity. The inactive holoenzyme is found in the cytoplasm By similarity.

GO - Cellular componenti

  1. cAMP-dependent protein kinase complex Source: UniProtKB
  2. centrosome Source: Ensembl
  3. ciliary base Source: MGI
  4. cytosol Source: Reactome
  5. nucleus Source: UniProtKB-SubCell
  6. perinuclear region of cytoplasm Source: Ensembl
  7. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit beta
PRO_0000086061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei3 – 31Deamidated asparagine By similarity
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei49 – 491Phosphothreonine By similarity
Modified residuei69 – 691Phosphotyrosine1 Publication
Modified residuei140 – 1401Phosphoserine By similarity
Modified residuei196 – 1961Phosphothreonine By similarity
Modified residuei198 – 1981Phosphothreonine By similarity
Modified residuei202 – 2021Phosphothreonine By similarity
Modified residuei331 – 3311Phosphotyrosine By similarity
Modified residuei339 – 3391Phosphoserine By similarity

Post-translational modificationi

Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form By similarity.

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP68181.
PRIDEiP68181.

PTM databases

PhosphoSiteiP68181.

Expressioni

Tissue specificityi

Isoform 1 is found in all tissues examined, with the highest expression in the brain and very low levels in the testis. Isoform 2 is strongly expressed in the brain, in the prelimbic and insular cortex. Isoform 3 is also found only in the brain, but at very low levels.1 Publication

Gene expression databases

ArrayExpressiP68181.
BgeeiP68181.
CleanExiMM_PRKACB.
GenevestigatoriP68181.

Interactioni

Subunit structurei

A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The cAMP-dependent protein kinase catalytic subunit binds PJA2 By similarity.

Protein-protein interaction databases

BioGridi202193. 2 interactions.
IntActiP68181. 5 interactions.
MINTiMINT-4099395.

Structurei

3D structure databases

ProteinModelPortaliP68181.
SMRiP68181. Positions 15-351.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 298255Protein kinase
Add
BLAST
Domaini299 – 35153AGC-kinase C-terminal
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074358.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
KOiK04345.
OMAiGKEFCEF.
OrthoDBiEOG7VX8WD.
PhylomeDBiP68181.
TreeFamiTF313399.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P68181-1) [UniParc]FASTAAdd to Basket

Also known as: Beta1

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

MGNTAIAKKG SEVESVKEFL AKAKEDFLRK WENPPPSNAG LEDFERKKTL    50
GTGSFGRVML VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVE 100
FPFLVRLEYS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ 150
IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY IQVTDFGFAK RVKGRTWTLC 200
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK 250
IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT 300
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEEIRVSI TEKCGKEFCE 350
F 351
Length:351
Mass (Da):40,708
Last modified:January 23, 2007 - v2
Checksum:iEBAC9B8041DF9F47
GO
Isoform 2 (identifier: P68181-2) [UniParc]FASTAAdd to Basket

Also known as: Beta2

The sequence of this isoform differs from the canonical sequence as follows:
     2-13: Missing.
     14-15: ES → MN

Show »
Length:339
Mass (Da):39,581
Checksum:i358F1764027B55F5
GO
Isoform 3 (identifier: P68181-3) [UniParc]FASTAAdd to Basket

Also known as: Beta3

The sequence of this isoform differs from the canonical sequence as follows:
     2-12: Missing.
     13-16: VESV → MGLL

Show »
Length:340
Mass (Da):39,651
Checksum:i3EC91AF8D1418BB7
GO
Isoform 4 (identifier: P68181-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-16: GNTAIAKKGSEVESV → MAAHKELSSG...EHTASWDKSM

Note: No experimental confirmation available.

Show »
Length:399
Mass (Da):46,145
Checksum:i36FF9CACFDA225BE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 1615GNTAI…EVESV → MAAHKELSSGQHSGTPTALQ KLEGFASRLFHRHSRGTAQE HRAALEDDGLRASEHTASWD KSM in isoform 4.
VSP_017376Add
BLAST
Alternative sequencei2 – 1312Missing in isoform 2.
VSP_017373Add
BLAST
Alternative sequencei2 – 1211Missing in isoform 3.
VSP_017372Add
BLAST
Alternative sequencei13 – 164VESV → MGLL in isoform 3.
VSP_017375
Alternative sequencei14 – 152ES → MN in isoform 2.
VSP_017374

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02626 mRNA. Translation: AAA39941.1.
AK048319 mRNA. Translation: BAC33301.1.
AK139419 mRNA. Translation: BAE24005.1.
AK148728 mRNA. Translation: BAE28648.1.
AK150122 mRNA. Translation: BAE29323.1.
AK150134 mRNA. Translation: BAE29331.1.
AK163585 mRNA. Translation: BAE37407.1.
BC054533 mRNA. Translation: AAH54533.1.
M21096 Genomic DNA. Translation: AAA39938.1.
AF022239 Genomic DNA. No translation available.
X61434 mRNA. Translation: CAA43676.1.
CCDSiCCDS17906.1. [P68181-1]
PIRiA24596. OKMSCB.
RefSeqiNP_001157670.1. NM_001164198.1.
NP_001157671.1. NM_001164199.1.
NP_001157672.1. NM_001164200.1.
NP_035230.1. NM_011100.4. [P68181-1]
UniGeneiMm.16766.

Genome annotation databases

EnsembliENSMUST00000005164; ENSMUSP00000005164; ENSMUSG00000005034.
ENSMUST00000102515; ENSMUSP00000099573; ENSMUSG00000005034. [P68181-1]
ENSMUST00000106137; ENSMUSP00000101743; ENSMUSG00000005034.
ENSMUST00000106138; ENSMUSP00000101744; ENSMUSG00000005034.
GeneIDi18749.
KEGGimmu:18749.
UCSCiuc008rrs.2. mouse. [P68181-2]
uc008rrt.2. mouse. [P68181-3]
uc008rru.1. mouse. [P68181-4]
uc008rrv.2. mouse. [P68181-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02626 mRNA. Translation: AAA39941.1 .
AK048319 mRNA. Translation: BAC33301.1 .
AK139419 mRNA. Translation: BAE24005.1 .
AK148728 mRNA. Translation: BAE28648.1 .
AK150122 mRNA. Translation: BAE29323.1 .
AK150134 mRNA. Translation: BAE29331.1 .
AK163585 mRNA. Translation: BAE37407.1 .
BC054533 mRNA. Translation: AAH54533.1 .
M21096 Genomic DNA. Translation: AAA39938.1 .
AF022239 Genomic DNA. No translation available.
X61434 mRNA. Translation: CAA43676.1 .
CCDSi CCDS17906.1. [P68181-1 ]
PIRi A24596. OKMSCB.
RefSeqi NP_001157670.1. NM_001164198.1.
NP_001157671.1. NM_001164199.1.
NP_001157672.1. NM_001164200.1.
NP_035230.1. NM_011100.4. [P68181-1 ]
UniGenei Mm.16766.

3D structure databases

ProteinModelPortali P68181.
SMRi P68181. Positions 15-351.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202193. 2 interactions.
IntActi P68181. 5 interactions.
MINTi MINT-4099395.

Chemistry

BindingDBi P68181.

PTM databases

PhosphoSitei P68181.

Proteomic databases

PaxDbi P68181.
PRIDEi P68181.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005164 ; ENSMUSP00000005164 ; ENSMUSG00000005034 .
ENSMUST00000102515 ; ENSMUSP00000099573 ; ENSMUSG00000005034 . [P68181-1 ]
ENSMUST00000106137 ; ENSMUSP00000101743 ; ENSMUSG00000005034 .
ENSMUST00000106138 ; ENSMUSP00000101744 ; ENSMUSG00000005034 .
GeneIDi 18749.
KEGGi mmu:18749.
UCSCi uc008rrs.2. mouse. [P68181-2 ]
uc008rrt.2. mouse. [P68181-3 ]
uc008rru.1. mouse. [P68181-4 ]
uc008rrv.2. mouse. [P68181-1 ]

Organism-specific databases

CTDi 5567.
MGIi MGI:97594. Prkacb.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074358.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
KOi K04345.
OMAi GKEFCEF.
OrthoDBi EOG7VX8WD.
PhylomeDBi P68181.
TreeFami TF313399.

Enzyme and pathway databases

Reactomei REACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_203795. DARPP-32 events.
REACT_213852. PKA-mediated phosphorylation of CREB.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.

Miscellaneous databases

NextBioi 294913.
PROi P68181.
SOURCEi Search...

Gene expression databases

ArrayExpressi P68181.
Bgeei P68181.
CleanExi MM_PRKACB.
Genevestigatori P68181.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
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 SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
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. "Evidence for a second isoform of the catalytic subunit of cAMP-dependent protein kinase."
    Uhler M.D., Chrivia J.C., McKnight G.S.
    J. Biol. Chem. 261:15360-15363(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1; 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Adrenal gland and Head.
  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/6.
    Tissue: Brain.
  4. "Characterization of genomic clones coding for the C alpha and C beta subunits of mouse cAMP-dependent protein kinase."
    Chrivia J.C., Uhler M.D., McKnight G.S.
    J. Biol. Chem. 263:5739-5744(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15 (ISOFORM 1).
  5. "Two novel brain-specific splice variants of the murine Cbeta gene of cAMP-dependent protein kinase."
    Guthrie C.R., Skalhegg B.S., McKnight G.S.
    J. Biol. Chem. 272:29560-29565(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7 (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 (ISOFORM 3), FUNCTION, MYRISTOYLATION AT GLY-2, TISSUE SPECIFICITY.
  6. "A collection of cDNA clones with specific expression patterns in mouse brain."
    Kato K.
    Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-351.
    Strain: BALB/c.
    Tissue: Brain.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKAPCB_MOUSE
AccessioniPrimary (citable) accession number: P68181
Secondary accession number(s): P05206
, Q3TQH5, Q3UDD0, Q3UTH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 108 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. 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

Similar proteinsi