Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01380
Entry Name
UniProt Accession
Theoretical PI
4.84
Molecular Weight
97341.59
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
A-kinase anchor protein 1, mitochondrial
Protein Synonyms/Alias
A-kinase anchor protein 149 kDa; AKAP 149; Dual specificity A-kinase-anchoring protein 1; D-AKAP-1; Protein kinase A-anchoring protein 1; PRKA1; Spermatid A-kinase anchor protein 84; S-AKAP84;
Gene Name
AKAP1
Gene Synonyms/Alias
AKAP149; PRKA1;
Created Date
30-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
584
Canonical
SMDSVDSCCSLKKTE
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.
Sequence Annotation
Domain: 607 671 KH.
Domain: 758 817 Tudor.
Region: 344 357 PKA-RII subunit binding domain.
Modified residue: 70 70 Phosphothreonine.
Modified residue: 105 105 Phosphoserine.
Modified residue: 107 107 Phosphoserine.
Modified residue: 169 169 Phosphoserine.
Modified residue: 429 429 Phosphoserine.
Modified residue: 447 447 Phosphothreonine.
Modified residue: 533 533 Phosphothreonine.
Protein Length
903 AA.
Protein Sequence
(Canonical)
MAIQFRSLFP LALPGMLALL GWWWFFSRKK GHVSSHDEQQ VEAGAVQLRA DPAIKEPLPV  60
EDVCPKVVST PPSVTEPPEK ELSTVSKLPA EPPALLQTHP PCRRSESSGI LPNTTDMRLR  120
PGTRRDDSTK LELALTGGEA KSIPLECPLS SPKGVLFSSK SAEVCKQDSP FSRVPRKVQP  180
GYPVVPAEKR SSGERARETG GAEGTGDAVL GEKVLEEALL SREHVLELEN SKGPSLASLE  240
GEEDKGKSSS SQVVGPVQEE EYVAEKLPSR FIESAHTELA KDDAAPAPPV ADAKAQDRGV  300
EGELGNEESL DRNEEGLDRN EEGLDRNEES LDRNEEGLDR NEEIKRAAFQ IISQVISEAT  360
EQVLATTVGK VAGRVCQASQ LQGQKEESCV PVHQKTVLGP DTAEPATAEA AVAPPDAGLP  420
LPGLPAEGSP PPKTYVSCLK SLLSSPTKDS KPNISAHHIS LASCLALTTP SEELPDRAGI  480
LVEDATCVTC MSDSSQSVPL VASPGHCSDS FSTSGLEDSC TETSSSPRDK AITPPLPEST  540
VPFSNGVLKG ELSDLGAEDG WTMDAEADHS GGSDRNSMDS VDSCCSLKKT ESFQNAQAGS  600
NPKKVDLIIW EIEVPKHLVG RLIGKQGRYV SFLKQTSGAK IYISTLPYTQ SVQICHIEGS  660
QHHVDKALNL IGKKFKELNL TNIYAPPLPS LALPSLPMTS WLMLPDGITV EVIVVNQVNA  720
GHLFVQQHTH PTFHALRSLD QQMYLCYSQP GIPTLPTPVE ITVICAAPGA DGAWWRAQVV  780
ASYEETNEVE IRYVDYGGYK RVKVDVLRQI RSDFVTLPFQ GAEVLLDSVM PLSDDDQFSP  840
EADAAMSEMT GNTALLAQVT SYSPTGLPLI QLWSVVGDEV VLINRSLVER GLAQWVDSYY  900
TSL                                                                903
FASTA
(Canonical)
>LipidDB-9606-01380|Q92667
MAIQFRSLFPLALPGMLALLGWWWFFSRKKGHVSSHDEQQVEAGAVQLRADPAIKEPLPV
EDVCPKVVSTPPSVTEPPEKELSTVSKLPAEPPALLQTHPPCRRSESSGILPNTTDMRLR
PGTRRDDSTKLELALTGGEAKSIPLECPLSSPKGVLFSSKSAEVCKQDSPFSRVPRKVQP
GYPVVPAEKRSSGERARETGGAEGTGDAVLGEKVLEEALLSREHVLELENSKGPSLASLE
GEEDKGKSSSSQVVGPVQEEEYVAEKLPSRFIESAHTELAKDDAAPAPPVADAKAQDRGV
EGELGNEESLDRNEEGLDRNEEGLDRNEESLDRNEEGLDRNEEIKRAAFQIISQVISEAT
EQVLATTVGKVAGRVCQASQLQGQKEESCVPVHQKTVLGPDTAEPATAEAAVAPPDAGLP
LPGLPAEGSPPPKTYVSCLKSLLSSPTKDSKPNISAHHISLASCLALTTPSEELPDRAGI
LVEDATCVTCMSDSSQSVPLVASPGHCSDSFSTSGLEDSCTETSSSPRDKAITPPLPEST
VPFSNGVLKGELSDLGAEDGWTMDAEADHSGGSDRNSMDSVDSCCSLKKTESFQNAQAGS
NPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGS
QHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNA
GHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVV
ASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMPLSDDDQFSP
EADAAMSEMTGNTALLAQVTSYSPTGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYY
TSL
Gene Ontology
GO:0005829; C:cytosol; TAS:Reactome
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-KW
GO:0005739; C:mitochondrion; IDA:HPA
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0003723; F:RNA binding; TAS:ProtInc
GO:0007596; P:blood coagulation; TAS:Reactome
Interpro
InterPro; IPR004087; KH_dom
InterPro; IPR004088; KH_dom_type_1
InterPro; IPR002999; Tudor
Pfam
Pfam; PF00013; KH_1;
Pfam; PF00567; TUDOR;
SMART
SMART; SM00322; KH;
SMART; SM00333; TUDOR;
PROSITE
PROSITE; PS50084; KH_TYPE_1;
PROSITE; PS50304; TUDOR;
PRINTS