O43823 (AKAP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
A-kinase anchor protein 8
Short name=AKAP-8

Alternative name(s):
A-kinase anchor protein 95 kDa
Short name=AKAP 95

Gene names

Name:	AKAP8
Synonyms:	AKAP95

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	692 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II).
Subunit structure	Binds to dimeric RII-alpha regulatory subunit of PKA during mitosis. Interacts (via C-terminus) with FIGN By similarity.
Subcellular location	Nucleus matrix. Note: Associated with the nuclear matrix. Redistributed and detached from condensed chromatin during mitosis.
Tissue specificity	Highly expressed in heart, liver, skeletal muscle, kidney and pancreas.
Sequence similarities	Belongs to the AKAP95 family. Contains 2 C2H2 AKAP95-type zinc fingers.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitosis Traceable author statement Ref.1. Source: ProtInc mitotic chromosome condensation Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara condensed chromosome Inferred from electronic annotation. Source: Compara female pronucleus Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	double-stranded DNA binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 692	692	A-kinase anchor protein 8		PRO_0000075381
Regions
	Zinc finger	390 – 414	25	C2H2 AKAP95-type 1
	Zinc finger	479 – 504	26	C2H2 AKAP95-type 2
	Region	572 – 589	18	RII-binding By similarity
	Motif	368 – 377	10	Nuclear localization signal Potential
	Compositional bias	107 – 118	12	Poly-Gly
Amino acid modifications
	Modified residue	112	1	Phosphoserine Ref.9
	Modified residue	323	1	Phosphoserine Ref.3 Ref.5 Ref.6 Ref.7 Ref.9
	Modified residue	328	1	Phosphoserine Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9
	Modified residue	339	1	Phosphoserine Ref.3 Ref.5 Ref.9
Natural variations
	Natural variant	664	1	Q → H in a breast cancer sample; somatic mutation. Ref.10		VAR_036534

Sequences

	Sequence		Length	Mass (Da)
	O43823 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: CBCD5F014FD94B66	FASTA	692	76,108
	10 20 30 40 50 60 MDQGYGGYGA WSAGPANTQG AYGTGVASWQ GYENYNYYGA QNTSVTTGAT YSYGPASWEA 70 80 90 100 110 120 AKANDGGLAA GAPAMHMASY GPEPCTDNSD SLIAKINQRL DMMSKEGGRG GSGGGGEGIQ 130 140 150 160 170 180 DRESSFRFQP FESYDSRPCL PEHNPYRPSY SYDYEFDLGS DRNGSFGGQY SECRDPARER 190 200 210 220 230 240 GSLDGFMRGR GQGRFQDRSN PGTFMRSDPF VPPAASSEPL STPWNELNYV GGRGLGGPSP 250 260 270 280 290 300 SRPPPSLFSQ SMAPDYGVMG MQGAGGYDST MPYGCGRSQP RMRDRDRPKR RGFDRFGPDG 310 320 330 340 350 360 TGRKRKQFQL YEEPDTKLAR VDSEGDFSEN DDAAGDFRSG DEEFKGEDEL CDSGRQRGEK 370 380 390 400 410 420 EDEDEDVKKR REKQRRRDRT RDRAADRIQF ACSVCKFRSF DDEEIQKHLQ SKFHKETLRF 430 440 450 460 470 480 ISTKLPDKTV EFLQEYIVNR NKKIEKRRQE LMEKETAKPK PDPFKGIGQE HFFKKIEAAH 490 500 510 520 530 540 CLACDMLIPA QPQLLQRHLH SVDHNHNRRL AAEQFKKTSL HVAKSVLNNR HIVKMLEKYL 550 560 570 580 590 600 KGEDPFTSET VDPEMEGDDN LGGEDKKETP EEVAADVLAE VITAAVRAVD GEGAPAPESS 610 620 630 640 650 660 GEPAEDEGPT DTAEAGSDPQ AEQLLEEQVP CGTAHEKGVP KARSEAAEAG NGAETMAAEA 670 680 690 ESAQTRVAPA PAAADAEVEQ TDAESKDAVP TE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95." Eide T., Coghlan V., Oerstavik S., Holsve C., Solberg R., Skaelhegg B.S., Lamb N.J.C., Langeberg L., Fernandez A., Scott J.D., Jahnsen T., Tasken K. Exp. Cell Res. 238:305-316(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cerebellum and Testis.
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND SER-339, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[4]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND SER-339, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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].
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-323; SER-328 AND SER-339, MASS SPECTROMETRY.
[10]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-664.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11997 mRNA. Translation: CAA72722.1. AC005785 Genomic DNA. Translation: AAC62838.1.
IPI	IPI00014474.
PIR	T13161.
RefSeq	NP_005849.1. NM_005858.3.
UniGene	Hs.594496.
3D structure databases
ProteinModelPortal	O43823.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43823. 9 interactions.
STRING	9606.ENSP00000269701.
PTM databases
PhosphoSite	O43823.
Proteomic databases
PaxDb	O43823.
PeptideAtlas	O43823.
PRIDE	O43823.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000269701; ENSP00000269701; ENSG00000105127.
GeneID	10270.
KEGG	hsa:10270.
UCSC	uc002nav.3. human.
Organism-specific databases
CTD	10270.
GeneCards	GC19M015464.
HGNC	HGNC:378. AKAP8.
HPA	HPA004776.
MIM	604692. gene.
neXtProt	NX_O43823.
PharmGKB	PA24672.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG47695.
HOGENOM	HOG000033876.
HOVERGEN	HBG053198.
InParanoid	O43823.
KO	K16525.
OMA	HLHSVDH.
OrthoDB	EOG4BG8VN.
Gene expression databases
ArrayExpress	O43823.
Bgee	O43823.
CleanEx	HS_AKAP8.
Genevestigator	O43823.
GermOnline	ENSG00000105127. Homo sapiens.
Family and domain databases
InterPro	IPR007071. AKAP95. IPR015880. Znf_C2H2-like. [Graphical view]
PANTHER	PTHR12190. PTHR12190. 1 hit.
Pfam	PF04988. AKAP95. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10270.
NextBio	38910.
SOURCE	Search...

Entry information

Entry name

AKAP8_HUMAN

Accession

Primary (citable) accession number: O43823

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 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.