Reviewed, UniProtKB/Swiss-Prot P31321 (KAP1_HUMAN)

Names and origin

Protein names

Recommended name:
    cAMP-dependent protein kinase type I-beta regulatory subunit

Gene names

Name:

PRKAR1B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	381 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)

Subunit structure	The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules.
Tissue specificity	Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.
Post-translational modification	The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.
Sequence similarities	Belongs to the cAMP-dependent kinase regulatory chain family. Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
PTM	Acetylation Disulfide bond Nitration Phosphoprotein
Gene Ontology (GO)
Biological process	hormone-mediated signaling Inferred from Experiment. Source: Reactome protein amino acid phosphorylation Ref.1 Non-traceable author statement. Source: UniProtKB regulation of protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cAMP-dependent protein kinase complex Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase regulator activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 381	380	cAMP-dependent protein kinase type I-beta regulatory subunit		PRO_0000205381
Regions
	Nucleotide binding	137 – 254	118	cAMP 1
	Nucleotide binding	255 – 381	127	cAMP 2
	Region	2 – 136	135	Dimerization and phosphorylation
	Motif	96 – 100	5	Pseudophosphorylation motif
Sites
	Binding site	202	1	cAMP 1
	Binding site	211	1	cAMP 1
	Binding site	326	1	cAMP 2
	Binding site	335	1	cAMP 2
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Probable
	Modified residue	3	1	Phosphoserine Ref.6
	Modified residue	21	1	Nitrated tyrosine
	Modified residue	77	1	Phosphoserine Ref.7
	Modified residue	83	1	Phosphoserine Ref.6 Ref.7
	Disulfide bond	18		Interchain (with C-39) By similarity
	Disulfide bond	39		Interchain (with C-18) By similarity
Experimental info
	Sequence conflict	270	1	A → R in AAC37564. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P31321-1 [UniParc]. Last modified May 5, 2009. Version 4. Checksum: 1ED7BFEC30897191	FASTA	381	43,073
	10 20 30 40 50 60 MASPPACPSE EDESLKGCEL YVQLHGIQQV LKDCIVHLCI SKPERPMKFL REHFEKLEKE 70 80 90 100 110 120 ENRQILARQK SNSQSDSHDE EVSPTPPNPV VKARRRRGGV SAEVYTEEDA VSYVRKVIPK 130 140 150 160 170 180 DYKTMTALAK AISKNVLFAH LDDNERSDIF DAMFPVTHIA GETVIQQGNE GDNFYVVDQG 190 200 210 220 230 240 EVDVYVNGEW VTNISEGGSF GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL 250 260 270 280 290 300 RKRKMYEEFL SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA 310 320 330 340 350 360 SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL DRPRFERVLG 370 380 PCSEILKRNI QRYNSFISLT V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, cDNA structure and tissue-specific expression of the human regulatory subunit RI beta of cAMP-dependent protein kinases." Solberg R., Tasken K., Keiserud A., Jahnsen T. Biochem. Biophys. Res. Commun. 176:166-172(1991) [PubMed: 1708242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human regulatory subunit RI beta of cAMP-dependent protein kinases: expression, holoenzyme formation and microinjection into living cells." Solberg R., Tasken K., Wen W., Coghlan V.M., Meinkoth J.L., Scott J.D., Jahnsen T., Taylor S.S. Exp. Cell Res. 214:595-605(1994) [PubMed: 7925653] [Abstract] Cited for: SEQUENCE REVISION TO 98-100. Tissue: Testis.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala and Brain.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Cervix.
[5]	"Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry." Zhan X., Desiderio D.M. Anal. Biochem. 354:279-289(2006) [PubMed: 16777052] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-21, MASS SPECTROMETRY. Tissue: Pituitary adenoma.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-83, MASS SPECTROMETRY.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M65066 mRNA. Translation: AAC37564.1. AK315951 mRNA. Translation: BAH14322.1. AK315990 mRNA. Translation: BAH14361.1. BC026734 mRNA. Translation: AAH26734.1. BC036828 mRNA. Translation: AAH36828.2.
IPI	IPI00554488.
PIR	OKHUR1. JH0392.
RefSeq	NP_002726.1.
UniGene	Hs.520851
3D structure databases
HSSP	HSSP built from PDB template 1RGS based on UniProtKB P00514.
SMR	P31321. Positions 14-63, 112-378.
ModBase	Search...
PTM databases
PhosphoSite	P31321.
Genome annotation databases
Ensembl	ENSG00000188191. Homo sapiens. [Contig view]
GeneID	5575.
Organism-specific databases
GeneCards	GC07M000555.
H-InvDB	HIX0017594.
HGNC	HGNC:9390. PRKAR1B.
MIM	176911. gene.
PharmGKB	PA33756.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P31321.
HOVERGEN	P31321.
Enzyme and pathway databases
Reactome	REACT_1505. Integration of energy metabolism.
Gene expression databases
ArrayExpress	P31321.
Bgee	P31321.
CleanEx	HS_PRKAR1B.
GermOnline	ENSG00000188191. Homo sapiens.
Family and domain databases
InterPro	IPR003117. cAMP-dep_prot_kin_reg_I/II_a/b. IPR002373. cAMP/cGMP_kin. IPR000595. cNMP_bd. IPR018488. cNMP_bd_CS. IPR012198. PK_regulatory. IPR014710. RmlC-like_jellyroll. [Graphical view]
Gene3D	G3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.
Pfam	PF00027. cNMP_binding. 2 hits. PF02197. RIIa. 1 hit. [Graphical view]
PIRSF	PIRSF000548. PK_regulatory. 1 hit.
PRINTS	PR00103. CAMPKINASE.
SMART	SM00100. cNMP. 2 hits. SM00394. RIIa. 1 hit. [Graphical view]
PROSITE	PS00888. CNMP_BINDING_1. 2 hits. PS00889. CNMP_BINDING_2. 2 hits. PS50042. CNMP_BINDING_3. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	21612.
SOURCE	Search...

Entry information

Entry name

KAP1_HUMAN

Accession

Primary (citable) accession number: P31321
Secondary accession number(s): Q8N422

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	May 5, 2009
Last modified:	June 16, 2009
This is version 86 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)