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Q02952 (AKA12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A-kinase anchor protein 12

Short name=AKAP-12
Alternative name(s):
A-kinase anchor protein 250 kDa
Short name=AKAP 250
Gravin
Myasthenia gravis autoantigen
Gene names
Name:AKAP12
Synonyms:AKAP250
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1782 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).

Subunit structure

Binds to dimeric RII-alpha regulatory subunit of PKC.

Subcellular location

Cytoplasmcell cortex Probable. Cytoplasmcytoskeleton Probable. Note: May be part of the cortical cytoskeleton.

Tissue specificity

Expressed in endothelial cells, cultured fibroblasts and osteosarcoma, but not in platelets, leukocytes, monocytic cell lines or peripherical blood cells.

Induction

Activated by lysophosphatidylcholine (lysoPC).

Domain

Polybasic regions located between residues 266 and 557 are involved in binding PKC.

Miscellaneous

Antibodies against the C-terminal of gravin can be produced by patients with myasthenia gravis (MG).

Sequence similarities

Contains 3 AKAP domains.

Sequence caution

The sequence BAE06085.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGFRP005332EBI-2562430,EBI-297353

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q02952-1)

Also known as: Alpha;

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: Q02952-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.
     99-106: EEEVIVTE → MLGTITIT
Isoform 3 (identifier: Q02952-3)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-105: Missing.
     106-106: E → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 17821781A-kinase anchor protein 12
PRO_0000064519

Regions

Domain604 – 63431AKAP 1
Domain753 – 78331AKAP 2
Domain798 – 82831AKAP 3
Region266 – 557292Involved in PKC-binding Probable
Region1541 – 155414RII-binding Probable
Compositional bias98 – 1014Poly-Glu

Amino acid modifications

Modified residue751Phosphoserine Ref.15
Modified residue961Phosphoserine Ref.15
Modified residue2191Phosphoserine Ref.9
Modified residue3711Phosphoserine Ref.15
Modified residue3741Phosphotyrosine By similarity
Modified residue3811Phosphoserine Ref.15
Modified residue4831Phosphoserine Ref.15
Modified residue5051Phosphoserine Ref.10
Modified residue5571Phosphoserine Ref.15
Modified residue5981Phosphoserine Ref.15
Modified residue6121Phosphoserine Ref.15
Modified residue6271Phosphoserine Ref.15
Modified residue6451Phosphoserine Ref.15
Modified residue6961Phosphoserine By similarity
Modified residue6971Phosphoserine By similarity
Modified residue6981Phosphoserine By similarity
Modified residue13311Phosphoserine Ref.15
Modified residue13951Phosphoserine Ref.12
Modified residue15871Phosphoserine Ref.15
Lipidation21N-myristoyl glycine Ref.13

Natural variations

Alternative sequence1 – 105105Missing in isoform 3.
VSP_028133
Alternative sequence1 – 9898Missing in isoform 2.
VSP_004110
Alternative sequence99 – 1068EEEVIVTE → MLGTITIT in isoform 2.
VSP_004111
Alternative sequence1061E → M in isoform 3.
VSP_028134
Natural variant1171K → E. Ref.1 Ref.3 Ref.6
Corresponds to variant rs10872670 [ dbSNP | Ensembl ].
VAR_035115
Natural variant2161K → Q. Ref.1 Ref.3 Ref.4 Ref.6
Corresponds to variant rs3734799 [ dbSNP | Ensembl ].
VAR_035116
Natural variant2401E → K in a colorectal cancer sample; somatic mutation. Ref.16
VAR_035780
Natural variant9201E → G. Ref.4
Corresponds to variant rs13212161 [ dbSNP | Ensembl ].
VAR_035117
Natural variant9871A → S. Ref.1
Corresponds to variant rs1042069 [ dbSNP | Ensembl ].
VAR_056731
Natural variant10961V → I.
Corresponds to variant rs3734797 [ dbSNP | Ensembl ].
VAR_035118
Natural variant12961R → L.
Corresponds to variant rs9478198 [ dbSNP | Ensembl ].
VAR_035119
Natural variant13551E → K. Ref.4
Corresponds to variant rs12201388 [ dbSNP | Ensembl ].
VAR_035120
Natural variant16001E → D. Ref.3
Corresponds to variant rs3823310 [ dbSNP | Ensembl ].
VAR_035121
Natural variant16891E → D.
Corresponds to variant rs3734795 [ dbSNP | Ensembl ].
VAR_035122

Experimental info

Sequence conflict142 – 1454TPEI → NRN in AAC51366. Ref.1
Sequence conflict4231T → I in BAE06085. Ref.3
Sequence conflict4491E → G in AAC51366. Ref.1
Sequence conflict6951G → R in AAC51366. Ref.1
Sequence conflict8681S → G in AAC51366. Ref.1
Sequence conflict9461E → G in CAH18338. Ref.4
Sequence conflict11821A → T in CAH18338. Ref.4
Sequence conflict15311E → EE in CAH18338. Ref.4
Sequence conflict15311E → EE in BAE06085. Ref.3
Sequence conflict15311E → EE in AAB58938. Ref.6
Sequence conflict15311E → EE in AAA35931. Ref.7
Sequence conflict15821V → M in CAH18338. Ref.4
Sequence conflict15821V → M in AAA35931. Ref.7
Sequence conflict16021Q → L in BAA19927. Ref.2

Sequences

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

Last modified January 11, 2011. Version 4.
Checksum: DB9DBA4647E6DDD5

FASTA1,782191,482
        10         20         30         40         50         60 
MGAGSSTEQR SPEQPPEGSS TPAEPEPSGG GPSAEAAPDT TADPAIAASD PATKLLQKNG 

        70         80         90        100        110        120 
QLSTINGVAE QDELSLQEGD LNGQKGALNG QGALNSQEEE EVIVTEVGQR DSEDVSKRDS 

       130        140        150        160        170        180 
DKEMATKSAV VHDITDDGQE ETPEIIEQIP SSESNLEELT QPTESQANDI GFKKVFKFVG 

       190        200        210        220        230        240 
FKFTVKKDKT EKPDTVQLLT VKKDEGEGAA GAGDHKDPSL GAGEAASKES EPKQSTEKPE 

       250        260        270        280        290        300 
ETLKREQSHA EISPPAESGQ AVEECKEEGE EKQEKEPSKS AESPTSPVTS ETGSTFKKFF 

       310        320        330        340        350        360 
TQGWAGWRKK TSFRKPKEDE VEASEKKKEQ EPEKVDTEED GKAEVASEKL TASEQAHPQE 

       370        380        390        400        410        420 
PAESAHEPRL SAEYEKVELP SEEQVSGSQG PSEEKPAPLA TEVFDEKIEV HQEEVVAEVH 

       430        440        450        460        470        480 
VSTVEERTEE QKTEVEETAG SVPAEELVEM DAEPQEAEPA KELVKLKETC VSGEDPTQGA 

       490        500        510        520        530        540 
DLSPDEKVLS KPPEGVVSEV EMLSSQERMK VQGSPLKKLF TSTGLKKLSG KKQKGKRGGG 

       550        560        570        580        590        600 
DEESGEHTQV PADSPDSQEE QKGESSASSP EEPEEITCLE KGLAEVQQDG EAEEGATSDG 

       610        620        630        640        650        660 
EKKREGVTPW ASFKKMVTPK KRVRRPSESD KEDELDKVKS ATLSSTESTA SEMQEEMKGS 

       670        680        690        700        710        720 
VEEPKPEEPK RKVDTSVSWE ALICVGSSKK RARRGSSSDE EGGPKAMGGD HQKADEAGKD 

       730        740        750        760        770        780 
KETGTDGILA GSQEHDPGQG SSSPEQAGSP TEGEGVSTWE SFKRLVTPRK KSKSKLEEKS 

       790        800        810        820        830        840 
EDSIAGSGVE HSTPDTEPGK EESWVSIKKF IPGRRKKRPD GKQEQAPVED AGPTGANEDD 

       850        860        870        880        890        900 
SDVPAVVPLS EYDAVEREKM EAQQAQKSAE QPEQKAATEV SKELSESQVH MMAAAVADGT 

       910        920        930        940        950        960 
RAATIIEERS PSWISASVTE PLEQVEAEAA LLTEEVLERE VIAEEEPPTV TEPLPENREA 

       970        980        990       1000       1010       1020 
RGDTVVSEAE LTPEAVTAAE TAGPLGAEEG TEASAAEETT EMVSAVSQLT DSPDTTEEAT 

      1030       1040       1050       1060       1070       1080 
PVQEVEGGVP DIEEQERRTQ EVLQAVAEKV KEESQLPGTG GPEDVLQPVQ RAEAERPEEQ 

      1090       1100       1110       1120       1130       1140 
AEASGLKKET DVVLKVDAQE AKTEPFTQGK VVGQTTPESF EKAPQVTESI ESSELVTTCQ 

      1150       1160       1170       1180       1190       1200 
AETLAGVKSQ EMVMEQAIPP DSVETPTDSE TDGSTPVADF DAPGTTQKDE IVEIHEENEV 

      1210       1220       1230       1240       1250       1260 
ASGTQSGGTE AEAVPAQKER PPAPSSFVFQ EETKEQSKME DTLEHTDKEV SVETVSILSK 

      1270       1280       1290       1300       1310       1320 
TEGTQEADQY ADEKTKDVPF FEGLEGSIDT GITVSREKVT EVALKGEGTE EAECKKDDAL 

      1330       1340       1350       1360       1370       1380 
ELQSHAKSPP SPVEREMVVQ VEREKTEAEP THVNEEKLEH ETAVTVSEEV SKQLLQTVNV 

      1390       1400       1410       1420       1430       1440 
PIIDGAKEVS SLEGSPPPCL GQEEAVCTKI QVQSSEASFT LTAAAEEEKV LGETANILET 

      1450       1460       1470       1480       1490       1500 
GETLEPAGAH LVLEEKSSEK NEDFAAHPGE DAVPTGPDCQ AKSTPVIVSA TTKKGLSSDL 

      1510       1520       1530       1540       1550       1560 
EGEKTTSLKW KSDEVDEQVA CQEVKVSVAI EDLEPENGIL ELETKSSKLV QNIIQTAVDQ 

      1570       1580       1590       1600       1610       1620 
FVRTEETATE MLTSELQTQA HVIKADSQDA GQETEKEGEE PQASAQDETP ITSAKEESES 

      1630       1640       1650       1660       1670       1680 
TAVGQAHSDI SKDMSEASEK TMTVEVEGST VNDQQLEEVV LPSEEEGGGA GTKSVPEDDG 

      1690       1700       1710       1720       1730       1740 
HALLAERIEK SLVEPKEDEK GDDVDDPENQ NSALADTDAS GGLTKESPDT NGPKQKEKED 

      1750       1760       1770       1780 
AQEVELQEGK VHSESDKAIT PQAQEELQKQ ERESAKSELT ES 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 384AEDA06CC83D93
Show »

FASTA1,684181,690
Isoform 3 (Gamma) [UniParc].

Checksum: 8533672E99E8A1D6
Show »

FASTA1,677180,990

References

« Hide 'large scale' references
[1]"Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein."
Nauert J.B., Klauck T.M., Langeberg L.K., Scott J.D.
Curr. Biol. 7:52-62(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLU-117; GLN-216 AND SER-987.
Tissue: Heart.
[2]"Changes of gene expression by lysophosphatidylcholine in vascular endothelial cells: 12 up-regulated distinct genes including 5 cell growth-related, 3 thrombosis-related, and 4 others."
Sato N., Kokame K., Shimokado K., Kato H., Miyata T.
J. Biochem. 123:1119-1126(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Umbilical vein endothelial cell.
[3]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLU-117; GLN-216 AND ASP-1600.
Tissue: Brain.
[4]"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] (ISOFORM 3), VARIANTS GLN-216; GLY-920 AND LYS-1355.
Tissue: Testis.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Sequence of gravin cDNA isolated from a human umbilical vein endothelial cell library."
Bowditch R.D., Ginsberg M.H.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-1782, VARIANTS GLU-117 AND GLN-216.
Tissue: Umbilical vein endothelial cell.
[7]"Molecular cloning and preliminary characterization of a novel cytoplasmic antigen recognized by myasthenia gravis sera."
Gordon T., Grove B., Loftus J.C., O'Toole T., McMillan R., Lindstrom J., Ginsberg M.H.
J. Clin. Invest. 90:992-999(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1478-1782.
Tissue: Umbilical vein endothelial cell.
[8]"Multiple promoters direct expression of three AKAP12 isoforms with distinct subcellular and tissue distribution profiles."
Streb J.W., Kitchen C.M., Gelman I.H., Miano J.M.
J. Biol. Chem. 279:56014-56023(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[9]"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-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"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].
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[14]"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].
[15]"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-75; SER-96; SER-371; SER-381; SER-483; SER-557; SER-598; SER-612; SER-627; SER-645; SER-1331 AND SER-1587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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. expand/collapse author list , 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] LYS-240.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U81607 mRNA. Translation: AAC51366.1.
AB003476 mRNA. Translation: BAA19927.1.
AB210003 mRNA. Translation: BAE06085.1. Different initiation.
CR749527 mRNA. Translation: CAH18338.1.
AL590413, AL033392, AL356535 Genomic DNA. Translation: CAI13590.1.
AL356535, AL033392, AL590413 Genomic DNA. Translation: CAI16151.1.
AL033392, AL356535, AL590413 Genomic DNA. Translation: CAI20467.1.
AL590413, AL033392 Genomic DNA. Translation: CAI13591.1.
AL033392, AL590413 Genomic DNA. Translation: CAI20468.1.
AF001504 mRNA. Translation: AAB58938.1.
M96322 mRNA. Translation: AAA35931.1.
PIRA43922.
JW0057.
RefSeqNP_005091.2. NM_005100.3.
NP_653080.1. NM_144497.2.
XP_005267290.1. XM_005267233.1.
XP_005267291.1. XM_005267234.2.
XP_005267292.1. XM_005267235.1.
UniGeneHs.371240.

3D structure databases

ProteinModelPortalQ02952.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114958. 13 interactions.
IntActQ02952. 7 interactions.
MINTMINT-2411728.
STRING9606.ENSP00000253332.

PTM databases

PhosphoSiteQ02952.

Polymorphism databases

DMDM317373554.

Proteomic databases

PaxDbQ02952.
PRIDEQ02952.

Protocols and materials databases

DNASU9590.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253332; ENSP00000253332; ENSG00000131016. [Q02952-1]
ENST00000354675; ENSP00000346702; ENSG00000131016. [Q02952-2]
ENST00000359755; ENSP00000352794; ENSG00000131016. [Q02952-3]
ENST00000402676; ENSP00000384537; ENSG00000131016. [Q02952-1]
GeneID9590.
KEGGhsa:9590.
UCSCuc003qoe.3. human. [Q02952-1]
uc003qof.3. human. [Q02952-2]
uc003qog.3. human. [Q02952-3]

Organism-specific databases

CTD9590.
GeneCardsGC06P151561.
H-InvDBHIX0025002.
HGNCHGNC:370. AKAP12.
HPAHPA006344.
MIM604698. gene.
neXtProtNX_Q02952.
PharmGKBPA24664.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG050472.
InParanoidQ02952.
KOK16528.
OMAIQVQSSE.
OrthoDBEOG7RFTGR.
PhylomeDBQ02952.
TreeFamTF105411.

Enzyme and pathway databases

SignaLinkQ02952.

Gene expression databases

BgeeQ02952.
CleanExHS_AKAP12.
GenevestigatorQ02952.

Family and domain databases

InterProIPR028540. AKAP12.
IPR001573. Pkinase-A_anch_WSK-motif.
IPR018459. RII_binding_1.
[Graphical view]
PANTHERPTHR23209. PTHR23209. 1 hit.
PfamPF10522. RII_binding_1. 1 hit.
PF03832. WSK. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAKAP12. human.
GeneWikiAKAP12.
GenomeRNAi9590.
NextBio35991.
PROQ02952.
SOURCESearch...

Entry information

Entry nameAKA12_HUMAN
AccessionPrimary (citable) accession number: Q02952
Secondary accession number(s): O00310 expand/collapse secondary AC list , O00498, Q4LE68, Q5SZ80, Q5TGN1, Q68D82, Q99970
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 129 of the entry and version 4 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 6

Human chromosome 6: entries, gene names and cross-references to MIM