P22694 (KAPCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase catalytic subunit beta
Short name=PKA C-beta
EC=2.7.11.11

Gene names

Name:

PRKACB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. 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. Ref.10 Ref.13
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. The cAMP-dependent protein kinase catalytic subunit binds PJA2 By similarity.
Subcellular location	Cytoplasm. Cell membrane. Nucleus By similarity. Note: Translocates into the nucleus (monomeric catalytic subunit) By similarity. The inactive holoenzyme is found in the cytoplasm By similarity. Ref.13
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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of phospholipase C activity Traceable author statement. Source: Reactome activation of protein kinase A activity Traceable author statement. Source: Reactome adenylate cyclase-modulating G-protein coupled receptor signaling pathway Traceable author statement Ref.10. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome cellular response to glucagon stimulus Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement. Source: Reactome epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome gluconeogenesis Traceable author statement. Source: Reactome intracellular protein kinase cascade Traceable author statement. Source: Reactome negative regulation of meiotic cell cycle Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of insulin secretion Traceable author statement. Source: Reactome response to clozapine Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome synaptic transmission Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome triglyceride catabolic process Traceable author statement. Source: Reactome water transport Traceable author statement. Source: Reactome
Cellular_component	cAMP-dependent protein kinase complex Traceable author statement Ref.10. Source: UniProtKB centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from direct assay Ref.10. Source: UniProtKB cAMP-dependent protein kinase activity Inferred from direct assay Ref.10. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.10. Source: UniProtKB ubiquitin protein ligase binding Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GPKOW	Q92917	4	EBI-5258763,EBI-746309
HSP90AB1	P08238	2	EBI-2679622,EBI-352572

Alternative products

This entry describes 10 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.

Isoform 9 (identifier: P22694-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGNAATAKKGSEVES → MGLSRKSSDASACSSSEISDSF

Note: No experimental confirmation available.

Isoform 10 (identifier: P22694-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MGNAATAKKGSEVE → MSARKSSDASACSSSEI
     79-111: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 351	350	cAMP-dependent protein kinase catalytic subunit beta		PRO_0000086060
Regions
	Domain	44 – 298	255	Protein kinase
	Domain	299 – 351	53	AGC-kinase C-terminal
	Nucleotide binding	50 – 58	9	ATP By similarity
Sites
	Active site	167	1	Proton acceptor By similarity
	Binding site	73	1	ATP By similarity
Amino acid modifications
	Modified residue	3	1	Deamidated asparagine By similarity
	Modified residue	69	1	Phosphotyrosine By similarity
	Modified residue	198	1	Phosphothreonine By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity
Natural variations
	Alternative sequence	1 – 16	16	MGNAA…EVESV → MAAYREPPCNQYTGTTTALQ KLEGFASRLFHRHSKGTAHD QKTALENDSLHFSEHTALWD RSM in isoform 2.		VSP_017364
	Alternative sequence	1 – 15	15	MGNAA…SEVES → MSARKSSDASACSSSEISDS F in isoform 6.		VSP_017365
	Alternative sequence	1 – 15	15	MGNAA…SEVES → MGLSRKSSDASACSSSEISD SF in isoform 9.		VSP_043372
	Alternative sequence	1 – 14	14	MGNAA…GSEVE → MSARKSSDASACSSSEI in isoform 5 and isoform 10.		VSP_017366
	Alternative sequence	1 – 14	14	MGNAA…GSEVE → MGLSRKSSDASACSSSEI in isoform 7.		VSP_017367
	Alternative sequence	1 – 13	13	Missing in isoform 4.		VSP_017368
	Alternative sequence	1 – 12	12	Missing in isoform 3.		VSP_017369
	Alternative sequence	13 – 16	4	VESV → MGLL in isoform 3.		VSP_017370
	Alternative sequence	14	1	E → M in isoform 4.		VSP_017371
	Alternative sequence	79 – 111	33	Missing in isoform 10.		VSP_046238
	Alternative sequence	256 – 257	2	VR → NF in isoform 8.		VSP_036556
	Alternative sequence	258 – 351	94	Missing in isoform 8.		VSP_036557
	Natural variant	106	1	R → Q. Ref.14 Corresponds to variant rs36117118 [ dbSNP | Ensembl ].		VAR_040594
Experimental info
	Sequence conflict	80	1	V → G in CAI56774. Ref.3
	Sequence conflict	159	1	H → N in AAH35058. Ref.8
	Sequence conflict	163	1	L → I in AAH35058. Ref.8
	Sequence conflict	233	1	A → V in CAI56774. Ref.3
	Sequence conflict	261	1	H → N in AAH35058. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Beta1) [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5C7443FBBA1C9BEC	FASTA	351	40,623
	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
	Isoform 2 (Beta2) [UniParc]. Checksum: 49EFAF3E426468FC	FASTA	398	46,236
	10 20 30 40 50 60 MAAYREPPCN QYTGTTTALQ KLEGFASRLF HRHSKGTAHD QKTALENDSL HFSEHTALWD 70 80 90 100 110 120 RSMKEFLAKA KEDFLKKWEN PTQNNAGLED FERKKTLGTG SFGRVMLVKH KATEQYYAMK 130 140 150 160 170 180 ILDKQKVVKL KQIEHTLNEK RILQAVNFPF LVRLEYAFKD NSNLYMVMEY VPGGEMFSHL 190 200 210 220 230 240 RRIGRFSEPH ARFYAAQIVL TFEYLHSLDL IYRDLKPENL LIDHQGYIQV TDFGFAKRVK 250 260 270 280 290 300 GRTWTLCGTP EYLAPEIILS KGYNKAVDWW ALGVLIYEMA AGYPPFFADQ PIQIYEKIVS 310 320 330 340 350 360 GKVRFPSHFS SDLKDLLRNL LQVDLTKRFG NLKNGVSDIK THKWFATTDW IAIYQRKVEA 370 380 390 PFIPKFRGSG DTSNFDDYEE EDIRVSITEK CAKEFGEF
	Isoform 3 (Beta3) [UniParc]. Checksum: AD0D54B6EEB01501	FASTA	339	39,477
	10 20 30 40 50 60 MGLLKEFLAK AKEDFLKKWE NPTQNNAGLE DFERKKTLGT GSFGRVMLVK HKATEQYYAM 70 80 90 100 110 120 KILDKQKVVK LKQIEHTLNE KRILQAVNFP FLVRLEYAFK DNSNLYMVME YVPGGEMFSH 130 140 150 160 170 180 LRRIGRFSEP HARFYAAQIV LTFEYLHSLD LIYRDLKPEN LLIDHQGYIQ VTDFGFAKRV 190 200 210 220 230 240 KGRTWTLCGT PEYLAPEIIL SKGYNKAVDW WALGVLIYEM AAGYPPFFAD QPIQIYEKIV 250 260 270 280 290 300 SGKVRFPSHF SSDLKDLLRN LLQVDLTKRF GNLKNGVSDI KTHKWFATTD WIAIYQRKVE 310 320 330 APFIPKFRGS GDTSNFDDYE EEDIRVSITE KCAKEFGEF
	Isoform 4 (Beta4) [UniParc]. Checksum: CFB30E746FD025F5	FASTA	338	39,379
	10 20 30 40 50 60 MSVKEFLAKA KEDFLKKWEN PTQNNAGLED FERKKTLGTG SFGRVMLVKH KATEQYYAMK 70 80 90 100 110 120 ILDKQKVVKL KQIEHTLNEK RILQAVNFPF LVRLEYAFKD NSNLYMVMEY VPGGEMFSHL 130 140 150 160 170 180 RRIGRFSEPH ARFYAAQIVL TFEYLHSLDL IYRDLKPENL LIDHQGYIQV TDFGFAKRVK 190 200 210 220 230 240 GRTWTLCGTP EYLAPEIILS KGYNKAVDWW ALGVLIYEMA AGYPPFFADQ PIQIYEKIVS 250 260 270 280 290 300 GKVRFPSHFS SDLKDLLRNL LQVDLTKRFG NLKNGVSDIK THKWFATTDW IAIYQRKVEA 310 320 330 PFIPKFRGSG DTSNFDDYEE EDIRVSITEK CAKEFGEF
	Isoform 5 (Beta4ab) [UniParc]. Checksum: 7BB4E4E199E5B0B4	FASTA	354	40,947
	10 20 30 40 50 60 MSARKSSDAS ACSSSEISVK EFLAKAKEDF LKKWENPTQN NAGLEDFERK KTLGTGSFGR 70 80 90 100 110 120 VMLVKHKATE QYYAMKILDK QKVVKLKQIE HTLNEKRILQ AVNFPFLVRL EYAFKDNSNL 130 140 150 160 170 180 YMVMEYVPGG EMFSHLRRIG RFSEPHARFY AAQIVLTFEY LHSLDLIYRD LKPENLLIDH 190 200 210 220 230 240 QGYIQVTDFG FAKRVKGRTW TLCGTPEYLA PEIILSKGYN KAVDWWALGV LIYEMAAGYP 250 260 270 280 290 300 PFFADQPIQI YEKIVSGKVR FPSHFSSDLK DLLRNLLQVD LTKRFGNLKN GVSDIKTHKW 310 320 330 340 350 FATTDWIAIY QRKVEAPFIP KFRGSGDTSN FDDYEEEDIR VSITEKCAKE FGEF
	Isoform 6 (Beta4abc) [UniParc]. Checksum: FC923359146B9466	FASTA	357	41,296
	10 20 30 40 50 60 MSARKSSDAS ACSSSEISDS FVKEFLAKAK EDFLKKWENP TQNNAGLEDF ERKKTLGTGS 70 80 90 100 110 120 FGRVMLVKHK ATEQYYAMKI LDKQKVVKLK QIEHTLNEKR ILQAVNFPFL VRLEYAFKDN 130 140 150 160 170 180 SNLYMVMEYV PGGEMFSHLR RIGRFSEPHA RFYAAQIVLT FEYLHSLDLI YRDLKPENLL 190 200 210 220 230 240 IDHQGYIQVT DFGFAKRVKG RTWTLCGTPE YLAPEIILSK GYNKAVDWWA LGVLIYEMAA 250 260 270 280 290 300 GYPPFFADQP IQIYEKIVSG KVRFPSHFSS DLKDLLRNLL QVDLTKRFGN LKNGVSDIKT 310 320 330 340 350 HKWFATTDWI AIYQRKVEAP FIPKFRGSGD TSNFDDYEEE DIRVSITEKC AKEFGEF
	Isoform 7 [UniParc]. Checksum: 02D5CA2B459BDDF1	FASTA	355	41,046
	10 20 30 40 50 60 MGLSRKSSDA SACSSSEISV KEFLAKAKED FLKKWENPTQ NNAGLEDFER KKTLGTGSFG 70 80 90 100 110 120 RVMLVKHKAT EQYYAMKILD KQKVVKLKQI EHTLNEKRIL QAVNFPFLVR LEYAFKDNSN 130 140 150 160 170 180 LYMVMEYVPG GEMFSHLRRI GRFSEPHARF YAAQIVLTFE YLHSLDLIYR DLKPENLLID 190 200 210 220 230 240 HQGYIQVTDF GFAKRVKGRT WTLCGTPEYL APEIILSKGY NKAVDWWALG VLIYEMAAGY 250 260 270 280 290 300 PPFFADQPIQ IYEKIVSGKV RFPSHFSSDL KDLLRNLLQV DLTKRFGNLK NGVSDIKTHK 310 320 330 340 350 WFATTDWIAI YQRKVEAPFI PKFRGSGDTS NFDDYEEEDI RVSITEKCAK EFGEF
	Isoform 8 [UniParc]. Checksum: 38FCBB18E1BF2761	FASTA	257	29,696
	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 ADQPIQIYEK IVSGKNF
	Isoform 9 [UniParc]. Checksum: B5E2A85075455EBA	FASTA	358	41,395
	10 20 30 40 50 60 MGLSRKSSDA SACSSSEISD SFVKEFLAKA KEDFLKKWEN PTQNNAGLED FERKKTLGTG 70 80 90 100 110 120 SFGRVMLVKH KATEQYYAMK ILDKQKVVKL KQIEHTLNEK RILQAVNFPF LVRLEYAFKD 130 140 150 160 170 180 NSNLYMVMEY VPGGEMFSHL RRIGRFSEPH ARFYAAQIVL TFEYLHSLDL IYRDLKPENL 190 200 210 220 230 240 LIDHQGYIQV TDFGFAKRVK GRTWTLCGTP EYLAPEIILS KGYNKAVDWW ALGVLIYEMA 250 260 270 280 290 300 AGYPPFFADQ PIQIYEKIVS GKVRFPSHFS SDLKDLLRNL LQVDLTKRFG NLKNGVSDIK 310 320 330 340 350 THKWFATTDW IAIYQRKVEA PFIPKFRGSG DTSNFDDYEE EDIRVSITEK CAKEFGEF
	Isoform 10 [UniParc]. Checksum: 7FF5EB27D1706E88	FASTA	321	36,979
	10 20 30 40 50 60 MSARKSSDAS ACSSSEISVK EFLAKAKEDF LKKWENPTQN NAGLEDFERK KTLGTGSFGR 70 80 90 100 110 120 VMLVKHKATE QYYAMKILDK QKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ 130 140 150 160 170 180 IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI 190 200 210 220 230 240 ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL 250 260 270 280 290 300 RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD 310 320 YEEEDIRVSI TEKCAKEFGE F

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9 AND 10). Tissue: Brain, Thalamus and 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. , 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] [Europe PMC] [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. , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-15 (ISOFORM 1), FUNCTION.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Control of PKA stability and signalling by the RING ligase praja2." Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R., Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A. Nat. Cell Biol. 13:412-422(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PJA2.
[14]	"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. , 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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-106.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

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. AK091420 mRNA. Translation: BAG52356.1. AK296482 mRNA. Translation: BAG59122.1. 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.
IPI	IPI00376119. IPI00395654. IPI00414365. IPI00645788. IPI00737155. IPI00738231. IPI00739094. IPI00739595. IPI01018756.
PIR	OKHUCB. A34724.
RefSeq	NP_001229786.1. NM_001242857.1. NP_001229787.1. NM_001242858.1. NP_001229788.1. NM_001242859.1. NP_001229789.1. NM_001242860.1. NP_001229790.1. NM_001242861.1. NP_001229791.1. NM_001242862.1. NP_002722.1. NM_002731.2. NP_891993.1. NM_182948.2. NP_997461.1. NM_207578.1.
UniGene	Hs.487325.
3D structure databases
ProteinModelPortal	P22694.
ModBase	Search...
Protein-protein interaction databases
IntAct	P22694. 30 interactions.
MINT	MINT-1178341.
PTM databases
PhosphoSite	P22694.
Polymorphism databases
DMDM	125210.
Proteomic databases
PaxDb	P22694.
PRIDE	P22694.
Protocols and materials databases
DNASU	5567.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370682; ENSP00000359716; ENSG00000142875. ENST00000370685; ENSP00000359719; ENSG00000142875. ENST00000370688; ENSP00000359722; ENSG00000142875. ENST00000370689; ENSP00000359723; ENSG00000142875. ENST00000394838; ENSP00000378314; ENSG00000142875. ENST00000394839; ENSP00000378315; ENSG00000142875.
GeneID	5567.
KEGG	hsa:5567.
UCSC	uc001dji.3. human. uc001djj.3. human. uc001djl.3. human. uc001djn.3. human. uc001djp.3. human. uc010oru.2. human.
Organism-specific databases
CTD	5567.
GeneCards	GC01P084543.
HGNC	HGNC:9381. PRKACB.
HPA	CAB010363. HPA029754.
MIM	176892. gene.
neXtProt	NX_P22694.
PharmGKB	PA33749.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
KO	K04345.
OMA	MAAHKEL.
OrthoDB	EOG4RXZ0C.
Enzyme and pathway databases
BRENDA	2.7.11.11. 2681.
Pathway_Interaction_DB	p75ntrpathway. p75(NTR)-mediated signaling.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease. REACT_13685. Neuronal System. REACT_15518. Transmembrane transport of small molecules. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P22694.
Bgee	P22694.
Genevestigator	P22694.
GermOnline	ENSG00000142875. Homo sapiens.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
BindingDB	P22694.
ChEMBL	CHEMBL2918.
ChiTaRS	PRKACB. human.
GenomeRNAi	5567.
NextBio	21570.
SOURCE	Search...

Entry information

Entry name

KAPCB_HUMAN

Accession

Primary (citable) accession number: P22694
Secondary accession number(s): B1APG4 , B4DKB0, B4E2Q1, 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:	May 1, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.