Q92667 (AKAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
A-kinase anchor protein 1, mitochondrial

Alternative name(s):
A-kinase anchor protein 149 kDa
Short name=AKAP 149
Dual specificity A-kinase-anchoring protein 1
Short name=D-AKAP-1
Protein kinase A-anchoring protein 1
Short name=PRKA1
Spermatid A-kinase anchor protein 84
Short name=S-AKAP84

Gene names

Name:	AKAP1
Synonyms:	AKAP149, PRKA1

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	903 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	Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.
Subcellular location	Mitochondrion outer membrane Potential.
Tissue specificity	AKAP149 is highly expressed in prostate and small intestine whereas S-AKAP84 is expressed in kidney, pancreas, liver, lung and brain. AKAP149 is also expressed in colon carcinoma.
Domain	RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
Sequence similarities	Contains 1 KH domain. Contains 1 Tudor domain.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide Transmembrane
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAATS1	Q7Z4T9-4	3	EBI-2120060,EBI-2119735
MYCBP	Q99417	2	EBI-2120060,EBI-716185

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92667-1)

Also known as: AKAP149;

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: Q92667-2)

Also known as: S-AKAP84;

The sequence of this isoform differs from the canonical sequence as follows:
     572-593: GSDRNSMDSVDSCCSLKKTESF → VAAPPPGKRGTLITRCPGFFEC
     594-903: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 29	29	Mitochondrion Potential
	Chain	30 – 903	874	A-kinase anchor protein 1, mitochondrial		PRO_0000016659
Regions
	Domain	607 – 671	65	KH
	Domain	758 – 817	60	Tudor
	Region	344 – 357	14	PKA-RII subunit binding domain
Amino acid modifications
	Modified residue	70	1	Phosphothreonine Ref.9
	Modified residue	105	1	Phosphoserine By similarity
	Modified residue	107	1	Phosphoserine By similarity
	Modified residue	169	1	Phosphoserine Ref.7
	Modified residue	429	1	Phosphoserine Ref.8
	Modified residue	447	1	Phosphothreonine Ref.11
	Modified residue	533	1	Phosphothreonine Ref.8 Ref.9
Natural variations
	Alternative sequence	572 – 593	22	GSDRN…KTESF → VAAPPPGKRGTLITRCPGFF EC in isoform 2.		VSP_002845
	Alternative sequence	594 – 903	310	Missing in isoform 2.		VSP_002846
	Natural variant	18	1	A → V. Corresponds to variant rs17761023 [ dbSNP | Ensembl ].		VAR_049676
	Natural variant	60	1	V → M. Corresponds to variant rs2230770 [ dbSNP | Ensembl ].		VAR_024512
	Natural variant	102	1	C → Y. Corresponds to variant rs2230771 [ dbSNP | Ensembl ].		VAR_049677
	Natural variant	124	1	R → C. Corresponds to variant rs17833723 [ dbSNP | Ensembl ].		VAR_049678
Experimental info
	Sequence conflict	795	1	D → H in AAH00729. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (AKAP149) [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 0C906FAFFB0DBAF7	FASTA	903	97,342
	10 20 30 40 50 60 MAIQFRSLFP LALPGMLALL GWWWFFSRKK GHVSSHDEQQ VEAGAVQLRA DPAIKEPLPV 70 80 90 100 110 120 EDVCPKVVST PPSVTEPPEK ELSTVSKLPA EPPALLQTHP PCRRSESSGI LPNTTDMRLR 130 140 150 160 170 180 PGTRRDDSTK LELALTGGEA KSIPLECPLS SPKGVLFSSK SAEVCKQDSP FSRVPRKVQP 190 200 210 220 230 240 GYPVVPAEKR SSGERARETG GAEGTGDAVL GEKVLEEALL SREHVLELEN SKGPSLASLE 250 260 270 280 290 300 GEEDKGKSSS SQVVGPVQEE EYVAEKLPSR FIESAHTELA KDDAAPAPPV ADAKAQDRGV 310 320 330 340 350 360 EGELGNEESL DRNEEGLDRN EEGLDRNEES LDRNEEGLDR NEEIKRAAFQ IISQVISEAT 370 380 390 400 410 420 EQVLATTVGK VAGRVCQASQ LQGQKEESCV PVHQKTVLGP DTAEPATAEA AVAPPDAGLP 430 440 450 460 470 480 LPGLPAEGSP PPKTYVSCLK SLLSSPTKDS KPNISAHHIS LASCLALTTP SEELPDRAGI 490 500 510 520 530 540 LVEDATCVTC MSDSSQSVPL VASPGHCSDS FSTSGLEDSC TETSSSPRDK AITPPLPEST 550 560 570 580 590 600 VPFSNGVLKG ELSDLGAEDG WTMDAEADHS GGSDRNSMDS VDSCCSLKKT ESFQNAQAGS 610 620 630 640 650 660 NPKKVDLIIW EIEVPKHLVG RLIGKQGRYV SFLKQTSGAK IYISTLPYTQ SVQICHIEGS 670 680 690 700 710 720 QHHVDKALNL IGKKFKELNL TNIYAPPLPS LALPSLPMTS WLMLPDGITV EVIVVNQVNA 730 740 750 760 770 780 GHLFVQQHTH PTFHALRSLD QQMYLCYSQP GIPTLPTPVE ITVICAAPGA DGAWWRAQVV 790 800 810 820 830 840 ASYEETNEVE IRYVDYGGYK RVKVDVLRQI RSDFVTLPFQ GAEVLLDSVM PLSDDDQFSP 850 860 870 880 890 900 EADAAMSEMT GNTALLAQVT SYSPTGLPLI QLWSVVGDEV VLINRSLVER GLAQWVDSYY TSL
	Isoform 2 (S-AKAP84) [UniParc]. Checksum: 3F2FC6A1381EFEC1	FASTA	593	62,921
	10 20 30 40 50 60 MAIQFRSLFP LALPGMLALL GWWWFFSRKK GHVSSHDEQQ VEAGAVQLRA DPAIKEPLPV 70 80 90 100 110 120 EDVCPKVVST PPSVTEPPEK ELSTVSKLPA EPPALLQTHP PCRRSESSGI LPNTTDMRLR 130 140 150 160 170 180 PGTRRDDSTK LELALTGGEA KSIPLECPLS SPKGVLFSSK SAEVCKQDSP FSRVPRKVQP 190 200 210 220 230 240 GYPVVPAEKR SSGERARETG GAEGTGDAVL GEKVLEEALL SREHVLELEN SKGPSLASLE 250 260 270 280 290 300 GEEDKGKSSS SQVVGPVQEE EYVAEKLPSR FIESAHTELA KDDAAPAPPV ADAKAQDRGV 310 320 330 340 350 360 EGELGNEESL DRNEEGLDRN EEGLDRNEES LDRNEEGLDR NEEIKRAAFQ IISQVISEAT 370 380 390 400 410 420 EQVLATTVGK VAGRVCQASQ LQGQKEESCV PVHQKTVLGP DTAEPATAEA AVAPPDAGLP 430 440 450 460 470 480 LPGLPAEGSP PPKTYVSCLK SLLSSPTKDS KPNISAHHIS LASCLALTTP SEELPDRAGI 490 500 510 520 530 540 LVEDATCVTC MSDSSQSVPL VASPGHCSDS FSTSGLEDSC TETSSSPRDK AITPPLPEST 550 560 570 580 590 VPFSNGVLKG ELSDLGAEDG WTMDAEADHS GVAAPPPGKR GTLITRCPGF FEC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain." Trendelenburg G., Hummel M., Riecken E.-O., Hanski C. Biochem. Biophys. Res. Commun. 225:313-319(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon.
[2]	"Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells." Lin R.-Y., Moss S.B., Rubin C.S. J. Biol. Chem. 270:27804-27811(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[4]	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].
[5]	"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). Tissue: Brain.
[6]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-429 AND THR-533, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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 THR-70 AND THR-533, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"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 THR-447, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97335 mRNA. Translation: CAA66000.1. U34074 mRNA. Translation: AAC50279.1. AK292416 mRNA. Translation: BAF85105.1. CH471109 Genomic DNA. Translation: EAW94515.1. CH471109 Genomic DNA. Translation: EAW94516.1. CH471109 Genomic DNA. Translation: EAW94518.1. BC000729 mRNA. Translation: AAH00729.1.
IPI	IPI00158627. IPI00942186.
PIR	I39173.
RefSeq	NP_001229831.1. NM_001242902.1. NP_001229832.1. NM_001242903.1. NP_003479.1. NM_003488.3.
UniGene	Hs.463506.
3D structure databases
ProteinModelPortal	Q92667.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92667. 6 interactions.
MINT	MINT-2411938.
STRING	9606.ENSP00000337736.
PTM databases
PhosphoSite	Q92667.
Polymorphism databases
DMDM	8134304.
Proteomic databases
PaxDb	Q92667.
PRIDE	Q92667.
Protocols and materials databases
DNASU	8165.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000314126; ENSP00000314075; ENSG00000121057. ENST00000337714; ENSP00000337736; ENSG00000121057. ENST00000481416; ENSP00000433212; ENSG00000121057. ENST00000539273; ENSP00000443139; ENSG00000121057. ENST00000571629; ENSP00000459968; ENSG00000121057. ENST00000572557; ENSP00000459895; ENSG00000121057.
GeneID	8165.
KEGG	hsa:8165.
UCSC	uc002iux.3. human.
Organism-specific databases
CTD	8165.
GeneCards	GC17P055162.
HGNC	HGNC:367. AKAP1.
HPA	CAB019286. HPA008691.
MIM	602449. gene.
neXtProt	NX_Q92667.
PharmGKB	PA24661.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG306785.
HOGENOM	HOG000013170.
HOVERGEN	HBG057436.
InParanoid	Q92667.
KO	K16518.
OrthoDB	EOG40GCR6.
PhylomeDB	Q92667.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q92667.
Bgee	Q92667.
CleanEx	HS_AKAP1.
Genevestigator	Q92667.
GermOnline	ENSG00000121057. Homo sapiens.
Family and domain databases
InterPro	IPR004087. KH_dom. IPR004088. KH_dom_type_1. IPR002999. Tudor. [Graphical view]
Pfam	PF00013. KH_1. 1 hit. PF00567. TUDOR. 1 hit. [Graphical view]
SMART	SM00322. KH. 1 hit. SM00333. TUDOR. 1 hit. [Graphical view]
PROSITE	PS50084. KH_TYPE_1. 1 hit. PS50304. TUDOR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q92667.
ChEMBL	CHEMBL3678.
ChiTaRS	AKAP1. human.
GenomeRNAi	8165.
NextBio	30837.
PMAP-CutDB	Q92667.
SOURCE	Search...

Entry information

Entry name

AKAP1_HUMAN

Accession

Primary (citable) accession number: Q92667
Secondary accession number(s): A8K8Q1 , D3DTZ0, Q13320, Q9BW14

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 131 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.