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Q92667 (AKAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length903 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Potential
Chain30 – 903874A-kinase anchor protein 1, mitochondrial
PRO_0000016659

Regions

Domain607 – 67165KH
Domain758 – 81760Tudor
Region344 – 35714PKA-RII subunit binding domain

Amino acid modifications

Modified residue701Phosphothreonine Ref.10
Modified residue1051Phosphoserine By similarity
Modified residue1071Phosphoserine By similarity
Modified residue1691Phosphoserine Ref.7
Modified residue4291Phosphoserine Ref.9
Modified residue4471Phosphothreonine Ref.12
Modified residue5331Phosphothreonine Ref.9 Ref.10

Natural variations

Alternative sequence572 – 59322GSDRN…KTESF → VAAPPPGKRGTLITRCPGFF EC in isoform 2.
VSP_002845
Alternative sequence594 – 903310Missing in isoform 2.
VSP_002846
Natural variant181A → V.
Corresponds to variant rs17761023 [ dbSNP | Ensembl ].
VAR_049676
Natural variant601V → M.
Corresponds to variant rs2230770 [ dbSNP | Ensembl ].
VAR_024512
Natural variant1021C → Y.
Corresponds to variant rs2230771 [ dbSNP | Ensembl ].
VAR_049677
Natural variant1241R → C.
Corresponds to variant rs17833723 [ dbSNP | Ensembl ].
VAR_049678

Experimental info

Sequence conflict7951D → H in AAH00729. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (AKAP149) [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 0C906FAFFB0DBAF7

FASTA90397,342
        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 

« Hide

Isoform 2 (S-AKAP84) [UniParc].

Checksum: 3F2FC6A1381EFEC1
Show »

FASTA59362,921

References

« Hide '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. 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] [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. 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].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS11594.1. [Q92667-1]
PIRI39173.
RefSeqNP_001229831.1. NM_001242902.1. [Q92667-1]
NP_001229832.1. NM_001242903.1. [Q92667-1]
NP_003479.1. NM_003488.3. [Q92667-1]
XP_005257764.1. XM_005257707.1. [Q92667-1]
XP_005257766.1. XM_005257709.1. [Q92667-1]
XP_006722189.1. XM_006722126.1. [Q92667-1]
XP_006722190.1. XM_006722127.1. [Q92667-1]
UniGeneHs.463506.

3D structure databases

ProteinModelPortalQ92667.
SMRQ92667. Positions 758-867.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113818. 13 interactions.
IntActQ92667. 10 interactions.
MINTMINT-2411938.
STRING9606.ENSP00000337736.

Chemistry

BindingDBQ92667.

PTM databases

PhosphoSiteQ92667.

Polymorphism databases

DMDM8134304.

Proteomic databases

MaxQBQ92667.
PaxDbQ92667.
PRIDEQ92667.

Protocols and materials databases

DNASU8165.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314126; ENSP00000314075; ENSG00000121057. [Q92667-2]
ENST00000337714; ENSP00000337736; ENSG00000121057. [Q92667-1]
ENST00000481416; ENSP00000433212; ENSG00000121057. [Q92667-2]
ENST00000539273; ENSP00000443139; ENSG00000121057. [Q92667-1]
ENST00000571629; ENSP00000459968; ENSG00000121057. [Q92667-1]
ENST00000572557; ENSP00000459895; ENSG00000121057. [Q92667-1]
GeneID8165.
KEGGhsa:8165.
UCSCuc002iux.3. human. [Q92667-1]

Organism-specific databases

CTD8165.
GeneCardsGC17P055162.
HGNCHGNC:367. AKAP1.
HPACAB019286.
HPA008691.
MIM602449. gene.
neXtProtNX_Q92667.
PharmGKBPA24661.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306785.
HOGENOMHOG000013170.
HOVERGENHBG057436.
InParanoidQ92667.
KOK16518.
OMADLIIWEI.
OrthoDBEOG779NXH.
PhylomeDBQ92667.
TreeFamTF105401.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ92667.
BgeeQ92667.
CleanExHS_AKAP1.
GenevestigatorQ92667.

Family and domain databases

Gene3D3.30.1370.10. 1 hit.
InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR002999. Tudor.
[Graphical view]
PfamPF00013. KH_1. 1 hit.
PF00567. TUDOR. 1 hit.
[Graphical view]
SMARTSM00322. KH. 1 hit.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMSSF54791. SSF54791. 1 hit.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50304. TUDOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAKAP1. human.
GeneWikiAKAP1.
GenomeRNAi8165.
NextBio30837.
PMAP-CutDBQ92667.
PROQ92667.
SOURCESearch...

Entry information

Entry nameAKAP1_HUMAN
AccessionPrimary (citable) accession number: Q92667
Secondary accession number(s): A8K8Q1 expand/collapse secondary AC list , D3DTZ0, Q13320, Q9BW14
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM