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Reviewed, UniProtKB/Swiss-Prot P22694 (KAPCB_HUMAN)

Last modified February 9, 2010. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    cAMP-dependent protein kinase catalytic subunit beta
      Short name=PKA C-beta
    EC=2.7.11.11
Gene names
Name: PRKACB
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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. Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Activated by cAMP.

Subunit structure

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.

Subcellular location

Cytoplasm 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.

Tissue specificity

Isoform 1 is most abundant in the brain, with low level expression in kidney. Isoform 2 is predominantly expressed in thymus, spleen and kidney. Isoform 3 and isoform 4 are only expressed in the brain. Ref.9

Post-translational modification

Asn-3 is partially deaminated to Asp giving rise to 2 major isoelectric variants, called CB and CA respectively By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAD92426.1 differs from that shown. Reason: Frameshift at position 322.

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Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22694-1)

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.
Isoform 2 (identifier: P22694-2)

Also known as: Beta2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MGNAATAKKGSEVESV → MAAYREPPCN...EHTALWDRSM
Isoform 3 (identifier: P22694-3)

Also known as: Beta3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
     13-16: VESV → MGLL
Note: Incomplete sequence.
Isoform 4 (identifier: P22694-4)

Also known as: Beta4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.
     14-14: E → M
Note: Incomplete sequence.
Isoform 5 (identifier: P22694-5)

Also known as: Beta4ab;

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MGNAATAKKGSEVE → MSARKSSDASACSSSEI
Note: Incomplete sequence.
Isoform 6 (identifier: P22694-6)

Also known as: Beta4abc;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGNAATAKKGSEVES → MSARKSSDASACSSSEISDSF
Isoform 7 (identifier: P22694-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MGNAATAKKGSEVE → MGLSRKSSDASACSSSEI
Note: No experimental confirmation available.
Isoform 8 (identifier: P22694-8)

The sequence of this isoform differs from the canonical sequence as follows:
     256-257: VR → NF
     258-351: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 351350cAMP-dependent protein kinase catalytic subunit beta
PRO_0000086060

Regions

Domain44 – 298255Protein kinase
Domain299 – 35153AGC-kinase C-terminal
Nucleotide binding50 – 589ATP By similarity

Sites

Active site1671Proton acceptor By similarity
Binding site731ATP By similarity

Amino acid modifications

Modified residue31Deamidated asparagine By similarity
Modified residue691Phosphotyrosine By similarity
Modified residue1981Phosphothreonine By similarity
Modified residue2671N6-acetyllysine Ref.12
Modified residue3391Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence1 – 1616MGNAA…EVESV → MAAYREPPCNQYTGTTTALQ KLEGFASRLFHRHSKGTAHD QKTALENDSLHFSEHTALWD RSM in isoform 2.
VSP_017364
Alternative sequence1 – 1515MGNAA…SEVES → MSARKSSDASACSSSEISDS F in isoform 6.
VSP_017365
Alternative sequence1 – 1414MGNAA…GSEVE → MSARKSSDASACSSSEI in isoform 5.
VSP_017366
Alternative sequence1 – 1414MGNAA…GSEVE → MGLSRKSSDASACSSSEI in isoform 7.
VSP_017367
Alternative sequence1 – 1313Missing in isoform 4.
VSP_017368
Alternative sequence1 – 1212Missing in isoform 3.
VSP_017369
Alternative sequence13 – 164VESV → MGLL in isoform 3.
VSP_017370
Alternative sequence141E → M in isoform 4.
VSP_017371
Alternative sequence256 – 2572VR → NF in isoform 8.
VSP_036556
Alternative sequence258 – 35194Missing in isoform 8.
VSP_036557
Natural variant1061R → Q: dbSNP rs36117118. Ref.13
VAR_040594

Experimental info

Sequence conflict801V → G in CAI56774. Ref.3
Sequence conflict1591H → N in AAH35058. Ref.8
Sequence conflict1631L → I in AAH35058. Ref.8
Sequence conflict2331A → V in CAI56774. Ref.3
Sequence conflict2611H → N in AAH35058. Ref.8

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta1) [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5C7443FBBA1C9BEC

FASTA35140,623
        10         20         30         40         50         60 
MGNAATAKKG SEVESVKEFL AKAKEDFLKK WENPTQNNAG LEDFERKKTL GTGSFGRVML 

        70         80         90        100        110        120 
VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVRLEYA FKDNSNLYMV 

       130        140        150        160        170        180 
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY 

       190        200        210        220        230        240 
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF 

       250        260        270        280        290        300 
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT 

       310        320        330        340        350 
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCAKEFGE F

« Hide

Isoform 2 (Beta2).

Checksum: 49EFAF3E426468FC
Show »

FASTA39846,236
Isoform 3 (Beta3).

Checksum: AD0D54B6EEB01501
Show »

FASTA33939,477
Isoform 4 (Beta4).

Checksum: CFB30E746FD025F5
Show »

FASTA33839,379
Isoform 5 (Beta4ab).

Checksum: 7BB4E4E199E5B0B4
Show »

FASTA35440,947
Isoform 6 (Beta4abc).

Checksum: FC923359146B9466
Show »

FASTA35741,296
Isoform 7.

Checksum: 02D5CA2B459BDDF1
Show »

FASTA35541,046
Isoform 8.

Checksum: 38FCBB18E1BF2761
Show »

FASTA25729,696

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References

« Hide 'large scale' references
[1]"Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis -- representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase."
Beebe S.J., Oyen O., Sandberg M., Froysa A., Hansson V., Jahnsen T.
Mol. Endocrinol. 4:465-475(1990) [PubMed: 2342480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[2]The German cDNA consortium
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
Tissue: Retina and Salivary gland.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Trachea.
[5]SeattleSNPs variation discovery resource
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 8).
Tissue: Brain.
[9]"Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase."
Orstavik S., Reinton N., Frengen E., Langeland B.T., Jahnsen T., Skalhegg B.S.
Eur. J. Biochem. 268:5066-5073(2001) [PubMed: 11589697] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-30 (ISOFORMS 2; 5 AND 6), NUCLEOTIDE SEQUENCE [MRNA] OF 1-16 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-13 (ISOFORM 4), TISSUE SPECIFICITY.
[10]"c-MYC activates protein kinase A (PKA) by direct transcriptional activation of the PKA catalytic subunit beta (PKA-CB) gene."
Wu K.-J., Mattioli M., Morse H.C., Dalla-Favera R.
Oncogene 21:7872-7882(2002) [PubMed: 12420224] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-15 (ISOFORM 1), FUNCTION.
[11]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, MASS SPECTROMETRY.
[13]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-106.
+Additional computationally mapped references.

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Web resources

SeattleSNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34181 mRNA. Translation: AAA60170.1.
BX537705 mRNA. Translation: CAD97818.1.
BX641026 mRNA. Translation: CAE46017.1.
AB209189 mRNA. Translation: BAD92426.1. Sequence problems.
CR936631 mRNA. Translation: CAI56774.1.
AK304375 mRNA. Translation: BAG65213.1.
DQ667174 Genomic DNA. Translation: ABG25919.1.
AL359504, AL450063 Genomic DNA. Translation: CAI14540.1.
AL359504, AL450063 Genomic DNA. Translation: CAI14541.1.
AL450063, AL359504 Genomic DNA. Translation: CAI16844.1.
AL450063, AL359504 Genomic DNA. Translation: CAI16845.1.
AL450063 Genomic DNA. Translation: CAI16846.1.
CH471097 Genomic DNA. Translation: EAW73248.1.
BC016285 mRNA. Translation: AAH16285.1.
BC035058 mRNA. Translation: AAH35058.1.
AY927364 mRNA. Translation: AAX19487.1.
AY927365 mRNA. Translation: AAX19488.1.
AY927366 mRNA. Translation: AAX19489.1.
AY927367 mRNA. Translation: AAX19490.1.
AY927368 mRNA. Translation: AAX19491.1.
AF538872 Genomic DNA. Translation: AAN16454.1.
IPIIPI00376119.
IPI00395654.
IPI00414365.
IPI00645788.
IPI00737155.
IPI00738231.
IPI00739094.
IPI00739595.
PIROKHUCB. A34724.
RefSeqNP_002722.1.
NP_891993.1.
NP_997461.1.
UniGeneHs.487325

3D structure databases

SMRP22694. Positions 14-351.
ModBaseSearch...

Protein-protein interaction databases

STRINGP22694.

PTM databases

PhosphoSiteP22694.

Proteomic databases

PRIDEP22694.

Genome annotation databases

EnsemblENST00000370689; ENSP00000359723; ENSG00000142875; Homo sapiens. [Genome view]
GeneID5567.
KEGGhsa:5567.
UCSCuc001djj.1. human.
uc001djl.1. human.
uc001djn.1. human.
uc001djp.1. human.

Organism-specific databases

CTD5567.
GeneCardsGC01P084255.
H-InvDBHIX0017291.
HGNCHGNC:9381. PRKACB.
HPACAB010363.
MIM176892. gene.
PharmGKBPA33749.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06368.
HOVERGENP22694.
OMAMAAHKEL.
OrthoDBEOG9MKR1W.
PhylomeDBP22694.

Enzyme and pathway databases

BRENDA2.7.11.11. 247.
Pathway_Interaction_DBp75ntrpathway. p75(NTR)-mediated signaling.
ReactomeREACT_11061. Signalling by NGF.
REACT_13685. Synaptic Transmission.
REACT_1505. Integration of energy metabolism.
REACT_15295. Opioid Signalling.
REACT_15380. Diabetes pathways.
REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpressP22694.
BgeeP22694.
GenevestigatorP22694.
GermOnlineENSG00000142875. Homo sapiens.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. 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]
ProtoNetSearch...

Other Resources

NextBio21570.
SOURCESearch...

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Entry information

Entry nameKAPCB_HUMAN
AccessionPrimary (citable) accession number: P22694
Secondary accession number(s): B4E2Q1 expand/collapse secondary AC list , Q14VH1, Q59GC0, Q5BNE9, Q5BNF0, Q5BNF1, Q5BNF2, Q5BNF3, Q5CZ92, Q5T1K3, Q7Z3M1, Q8IYR5, Q8IZQ0, Q96B09
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

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Human chromosome 1: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

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Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents