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Q99996

- AKAP9_HUMAN

UniProt

Q99996 - AKAP9_HUMAN

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Protein

A-kinase anchor protein 9

Gene

AKAP9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Binds to type II regulatory subunits of protein kinase A. Scaffolding protein that assembles several protein kinases and phosphatases on the centrosome and Golgi apparatus. May be required to maintain the integrity of the Golgi apparatus. Isoform 4 is associated with the N-methyl-D-aspartate receptor and is specifically found in the neuromuscular junction (NMJ) as well as in neuronal synapses, suggesting a role in the organization of postsynaptic specializations.1 Publication

GO - Molecular functioni

  1. ion channel binding Source: BHF-UCL
  2. protein complex scaffold Source: BHF-UCL
  3. receptor binding Source: ProtInc

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: Reactome
  2. mitotic cell cycle Source: Reactome
  3. Sertoli cell development Source: Ensembl
  4. signal transduction Source: ProtInc
  5. spermatogenesis Source: Ensembl
  6. synaptic transmission Source: Reactome
  7. transport Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
SignaLinkiQ99996.

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 9
Short name:
AKAP-9
Alternative name(s):
A-kinase anchor protein 350 kDa
Short name:
AKAP 350
Short name:
hgAKAP 350
A-kinase anchor protein 450 kDa
Short name:
AKAP 450
AKAP 120-like protein
Centrosome- and Golgi-localized PKN-associated protein
Short name:
CG-NAP
Protein hyperion
Protein kinase A-anchoring protein 9
Short name:
PRKA9
Protein yotiao
Gene namesi
Name:AKAP9
Synonyms:AKAP350, AKAP450, KIAA0803
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:379. AKAP9.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. ciliary basal body Source: Ensembl
  3. cytoskeleton Source: ProtInc
  4. cytosol Source: Reactome
  5. Golgi apparatus Source: UniProtKB
  6. intracellular membrane-bounded organelle Source: HPA
  7. pericentriolar material Source: Ensembl
  8. voltage-gated potassium channel complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

Pathology & Biotechi

Involvement in diseasei

Long QT syndrome 11 (LQT11) [MIM:611820]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1582 – 15821S → L in LQT11. 1 Publication
VAR_043489

Keywords - Diseasei

Disease mutation, Long QT syndrome

Organism-specific databases

MIMi611820. phenotype.
Orphaneti101016. Romano-Ward syndrome.
PharmGKBiPA24673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 39113911A-kinase anchor protein 9PRO_0000064534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei3846 – 38461Phosphoserine1 Publication
Modified residuei3869 – 38691Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99996.
PaxDbiQ99996.
PRIDEiQ99996.

PTM databases

PhosphoSiteiQ99996.

Expressioni

Tissue specificityi

Widely expressed. Isoform 4 is highly expressed in skeletal muscle and in pancreas.

Gene expression databases

BgeeiQ99996.
ExpressionAtlasiQ99996. baseline and differential.
GenevestigatoriQ99996.

Organism-specific databases

HPAiCAB012909.
HPA008548.
HPA026109.

Interactioni

Subunit structurei

Interacts with the regulatory region of protein kinase N (PKN), protein phosphatase 2A (PP2A), protein phosphatase 1 (PP1) and the immature non-phosphorylated form of PKC epsilon. Interacts with CIP4 and FNBP1. Interacts with chloride intracellular channel proteins CLIC1, CLIC4 and CLIC5. CSNK1D binding promotes its centrosomal subcellular location.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA2Q083793EBI-1048311,EBI-618309
KDM1AO603412EBI-1048311,EBI-710124

Protein-protein interaction databases

BioGridi115445. 40 interactions.
DIPiDIP-29942N.
IntActiQ99996. 23 interactions.
MINTiMINT-1174958.

Structurei

3D structure databases

ProteinModelPortaliQ99996.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2554 – 256714PKA-RII subunit binding domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili164 – 914751Sequence AnalysisAdd
BLAST
Coiled coili944 – 102279Sequence AnalysisAdd
BLAST
Coiled coili1100 – 118586Sequence AnalysisAdd
BLAST
Coiled coili1253 – 128028Sequence AnalysisAdd
BLAST
Coiled coili1336 – 139257Sequence AnalysisAdd
BLAST
Coiled coili1434 – 145926Sequence AnalysisAdd
BLAST
Coiled coili1585 – 165975Sequence AnalysisAdd
BLAST
Coiled coili1857 – 2455599Sequence AnalysisAdd
BLAST
Coiled coili2544 – 256118Sequence AnalysisAdd
BLAST
Coiled coili2603 – 2776174Sequence AnalysisAdd
BLAST
Coiled coili3065 – 309228Sequence AnalysisAdd
BLAST
Coiled coili3124 – 3470347Sequence AnalysisAdd
BLAST
Coiled coili3587 – 3689103Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi203 – 29290Gln-richAdd
BLAST
Compositional biasi321 – 1010690Glu-richAdd
BLAST
Compositional biasi1846 – 2772927Glu-richAdd
BLAST
Compositional biasi3726 – 37305Poly-Leu

Domaini

RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000110871.
HOVERGENiHBG050481.
InParanoidiQ99996.
KOiK16551.
OMAiKMRKFLD.
OrthoDBiEOG7VMP46.
PhylomeDBiQ99996.
TreeFamiTF105408.

Family and domain databases

InterProiIPR028745. AKAP9.
IPR019528. PACT_domain.
[Graphical view]
PANTHERiPTHR18932:SF10. PTHR18932:SF10. 1 hit.
PfamiPF10495. PACT_coil_coil. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99996-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEDEERQKKL EAGKAKIEEL SLAFLVRQLA QFRQRKAQSD GQSPSKKQKK
60 70 80 90 100
KRKTSSSKHD VSAHHDLNID QSQCNEMYIN SSQRVESTVI PESTIMRTLH
110 120 130 140 150
SGEITSHEQG FSVELESEIS TTADDCSSEV NGCSFVMRTG KPTNLLREEE
160 170 180 190 200
FGVDDSYSEQ GAQDSPTHLE MMESELAGKQ HEIEELNREL EEMRVTYGTE
210 220 230 240 250
GLQQLQEFEA AIKQRDGIIT QLTANLQQAR REKDETMREF LELTEQSQKL
260 270 280 290 300
QIQFQQLQAS ETLRNSTHSS TAADLLQAKQ QILTHQQQLE EQDHLLEDYQ
310 320 330 340 350
KKKEDFTMQI SFLQEKIKVY EMEQDKKVEN SNKEEIQEKE TIIEELNTKI
360 370 380 390 400
IEEEKKTLEL KDKLTTADKL LGELQEQIVQ KNQEIKNMKL ELTNSKQKER
410 420 430 440 450
QSSEEIKQLM GTVEELQKRN HKDSQFETDI VQRMEQETQR KLEQLRAELD
460 470 480 490 500
EMYGQQIVQM KQELIRQHMA QMEEMKTRHK GEMENALRSY SNITVNEDQI
510 520 530 540 550
KLMNVAINEL NIKLQDTNSQ KEKLKEELGL ILEEKCALQR QLEDLVEELS
560 570 580 590 600
FSREQIQRAR QTIAEQESKL NEAHKSLSTV EDLKAEIVSA SESRKELELK
610 620 630 640 650
HEAEVTNYKI KLEMLEKEKN AVLDRMAESQ EAELERLRTQ LLFSHEEELS
660 670 680 690 700
KLKEDLEIEH RINIEKLKDN LGIHYKQQID GLQNEMSQKI ETMQFEKDNL
710 720 730 740 750
ITKQNQLILE ISKLKDLQQS LVNSKSEEMT LQINELQKEI EILRQEEKEK
760 770 780 790 800
GTLEQEVQEL QLKTELLEKQ MKEKENDLQE KFAQLEAENS ILKDEKKTLE
810 820 830 840 850
DMLKIHTPVS QEERLIFLDS IKSKSKDSVW EKEIEILIEE NEDLKQQCIQ
860 870 880 890 900
LNEEIEKQRN TFSFAEKNFE VNYQELQEEY ACLLKVKDDL EDSKNKQELE
910 920 930 940 950
YKSKLKALNE ELHLQRINPT TVKMKSSVFD EDKTFVAETL EMGEVVEKDT
960 970 980 990 1000
TELMEKLEVT KREKLELSQR LSDLSEQLKQ KHGEISFLNE EVKSLKQEKE
1010 1020 1030 1040 1050
QVSLRCRELE IIINHNRAEN VQSCDTQVSS LLDGVVTMTS RGAEGSVSKV
1060 1070 1080 1090 1100
NKSFGEESKI MVEDKVSFEN MTVGEESKQE QLILDHLPSV TKESSLRATQ
1110 1120 1130 1140 1150
PSENDKLQKE LNVLKSEQND LRLQMEAQRI CLSLVYSTHV DQVREYMENE
1160 1170 1180 1190 1200
KDKALCSLKE ELIFAQEEKI KELQKIHQLE LQTMKTQETG DEGKPLHLLI
1210 1220 1230 1240 1250
GKLQKAVSEE CSYFLQTLCS VLGEYYTPAL KCEVNAEDKE NSGDYISENE
1260 1270 1280 1290 1300
DPELQDYRYE VQDFQENMHT LLNKVTEEYN KLLVLQTRLS KIWGQQTDGM
1310 1320 1330 1340 1350
KLEFGEENLP KEETEFLSIH SQMTNLEDID VNHKSKLSSL QDLEKTKLEE
1360 1370 1380 1390 1400
QVQELESLIS SLQQQLKETE QNYEAEIHCL QKRLQAVSES TVPPSLPVDS
1410 1420 1430 1440 1450
VVITESDAQR TMYPGSCVKK NIDGTIEFSG EFGVKEETNI VKLLEKQYQE
1460 1470 1480 1490 1500
QLEEEVAKVI VSMSIAFAQQ TELSRISGGK ENTASSKQAH AVCQQEQHYF
1510 1520 1530 1540 1550
NEMKLSQDQI GFQTFETVDV KFKEEFKPLS KELGEHGKEI LLSNSDPHDI
1560 1570 1580 1590 1600
PESKDCVLTI SEEMFSKDKT FIVRQSIHDE ISVSSMDASR QLMLNEEQLE
1610 1620 1630 1640 1650
DMRQELVRQY QEHQQATELL RQAHMRQMER QREDQEQLQE EIKRLNRQLA
1660 1670 1680 1690 1700
QRSSIDNENL VSERERVLLE ELEALKQLSL AGREKLCCEL RNSSTQTQNG
1710 1720 1730 1740 1750
NENQGEVEEQ TFKEKELDRK PEDVPPEILS NERYALQKAN NRLLKILLEV
1760 1770 1780 1790 1800
VKTTAAVEET IGRHVLGILD RSSKSQSSAS LIWRSEAEAS VKSCVHEEHT
1810 1820 1830 1840 1850
RVTDESIPSY SGSDMPRNDI NMWSKVTEEG TELSQRLVRS GFAGTEIDPE
1860 1870 1880 1890 1900
NEELMLNISS RLQAAVEKLL EAISETSSQL EHAKVTQTEL MRESFRQKQE
1910 1920 1930 1940 1950
ATESLKCQEE LRERLHEESR AREQLAVELS KAEGVIDGYA DEKTLFERQI
1960 1970 1980 1990 2000
QEKTDIIDRL EQELLCASNR LQELEAEQQQ IQEERELLSR QKEAMKAEAG
2010 2020 2030 2040 2050
PVEQQLLQET EKLMKEKLEV QCQAEKVRDD LQKQVKALEI DVEEQVSRFI
2060 2070 2080 2090 2100
ELEQEKNTEL MDLRQQNQAL EKQLEKMRKF LDEQAIDREH ERDVFQQEIQ
2110 2120 2130 2140 2150
KLEQQLKVVP RFQPISEHQT REVEQLANHL KEKTDKCSEL LLSKEQLQRD
2160 2170 2180 2190 2200
IQERNEEIEK LEFRVRELEQ ALLVSADTFQ KVEDRKHFGA VEAKPELSLE
2210 2220 2230 2240 2250
VQLQAERDAI DRKEKEITNL EEQLEQFREE LENKNEEVQQ LHMQLEIQKK
2260 2270 2280 2290 2300
ESTTRLQELE QENKLFKDDM EKLGLAIKES DAMSTQDQHV LFGKFAQIIQ
2310 2320 2330 2340 2350
EKEVEIDQLN EQVTKLQQQL KITTDNKVIE EKNELIRDLE TQIECLMSDQ
2360 2370 2380 2390 2400
ECVKRNREEE IEQLNEVIEK LQQELANIGQ KTSMNAHSLS EEADSLKHQL
2410 2420 2430 2440 2450
DVVIAEKLAL EQQVETANEE MTFMKNVLKE TNFKMNQLTQ ELFSLKRERE
2460 2470 2480 2490 2500
SVEKIQSIPE NSVNVAIDHL SKDKPELEVV LTEDALKSLE NQTYFKSFEE
2510 2520 2530 2540 2550
NGKGSIINLE TRLLQLESTV SAKDLELTQC YKQIKDMQEQ GQFETEMLQK
2560 2570 2580 2590 2600
KIVNLQKIVE EKVAAALVSQ IQLEAVQEYA KFCQDNQTIS SEPERTNIQN
2610 2620 2630 2640 2650
LNQLREDELG SDISALTLRI SELESQVVEM HTSLILEKEQ VEIAEKNVLE
2660 2670 2680 2690 2700
KEKKLLELQK LLEGNEKKQR EKEKKRSPQD VEVLKTTTEL FHSNEESGFF
2710 2720 2730 2740 2750
NELEALRAES VATKAELASY KEKAEKLQEE LLVKETNMTS LQKDLSQVRD
2760 2770 2780 2790 2800
HLAEAKEKLS ILEKEDETEV QESKKACMFE PLPIKLSKSI ASQTDGTLKI
2810 2820 2830 2840 2850
SSSNQTPQIL VKNAGIQINL QSECSSEEVT EIISQFTEKI EKMQELHAAE
2860 2870 2880 2890 2900
ILDMESRHIS ETETLKREHY VAVQLLKEEC GTLKAVIQCL RSKEVFGFYN
2910 2920 2930 2940 2950
MCFSTLCDSG SDWGQGIYLT HSQGFDIASE GRGEESESAT DSFPKKIKGL
2960 2970 2980 2990 3000
LRAVHNEGMQ VLSLTESPYS DGEDHSIQQV SEPWLEERKA YINTISSLKD
3010 3020 3030 3040 3050
LITKMQLQRE AEVYDSSQSH ESFSDWRGEL LLALQQVFLE ERSVLLAAFR
3060 3070 3080 3090 3100
TELTALGTTD AVGLLNCLEQ RIQEQGVEYQ AAMECLQKAD RRSLLSEIQA
3110 3120 3130 3140 3150
LHAQMNGRKI TLKREQESEK PSQELLEYNI QQKQSQMLEM QVELSSMKDR
3160 3170 3180 3190 3200
ATELQEQLSS EKMVVAELKS ELAQTKLELE TTLKAQHKHL KELEAFRLEV
3210 3220 3230 3240 3250
KDKTDEVHLL NDTLASEQKK SRELQWALEK EKAKLGRSEE RDKEELEDLK
3260 3270 3280 3290 3300
FSLESQKQRN LQLNLLLEQQ KQLLNESQQK IESQRMLYDA QLSEEQGRNL
3310 3320 3330 3340 3350
ELQVLLESEK VRIREMSSTL DRERELHAQL QSSDGTGQSR PPLPSEDLLK
3360 3370 3380 3390 3400
ELQKQLEEKH SRIVELLNET EKYKLDSLQT RQQMEKDRQV HRKTLQTEQE
3410 3420 3430 3440 3450
ANTEGQKKMH ELQSKVEDLQ RQLEEKRQQV YKLDLEGQRL QGIMQEFQKQ
3460 3470 3480 3490 3500
ELEREEKRES RRILYQNLNE PTTWSLTSDR TRNWVLQQKI EGETKESNYA
3510 3520 3530 3540 3550
KLIEMNGGGT GCNHELEMIR QKLQCVASKL QVLPQKASER LQFETADDED
3560 3570 3580 3590 3600
FIWVQENIDE IILQLQKLTG QQGEEPSLVS PSTSCGSLTE RLLRQNAELT
3610 3620 3630 3640 3650
GHISQLTEEK NDLRNMVMKL EEQIRWYRQT GAGRDNSSRF SLNGGANIEA
3660 3670 3680 3690 3700
IIASEKEVWN REKLTLQKSL KRAEAEVYKL KAELRNDSLL QTLSPDSEHV
3710 3720 3730 3740 3750
TLKRIYGKYL RAESFRKALI YQKKYLLLLL GGFQECEDAT LALLARMGGQ
3760 3770 3780 3790 3800
PAFTDLEVIT NRPKGFTRFR SAVRVSIAIS RMKFLVRRWH RVTGSVSINI
3810 3820 3830 3840 3850
NRDGFGLNQG AEKTDSFYHS SGGLELYGEP RHTTYRSRSD LDYIRSPLPF
3860 3870 3880 3890 3900
QNRYPGTPAD FNPGSLACSQ LQNYDPDRAL TDYITRLEAL QRRLGTIQSG
3910
STTQFHAGMR R
Length:3,911
Mass (Da):453,667
Last modified:August 1, 1999 - v3
Checksum:i3FB1CB1C819B47AA
GO
Isoform 2 (identifier: Q99996-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     17-28: Missing.
     2895-2907: VFGFYNMCFSTLC → GSSIPELAHSDAYQTREICSS

Show »
Length:3,907
Mass (Da):452,987
Checksum:i81761B4341430CDF
GO
Isoform 3 (identifier: Q99996-3) [UniParc]FASTAAdd to Basket

Also known as: CG-NAP

The sequence of this isoform differs from the canonical sequence as follows:
     17-28: Missing.
     2175-2182: Missing.
     2895-2907: VFGFYNMCFSTLC → GSSIPELAHSDAYQTREICSS

Show »
Length:3,899
Mass (Da):452,110
Checksum:iF90C9F18B32FD314
GO
Isoform 4 (identifier: Q99996-4) [UniParc]FASTAAdd to Basket

Also known as: Yotiao

The sequence of this isoform differs from the canonical sequence as follows:
     1637-1643: QLQEEIK → LAQVRVL
     1644-3911: Missing.

Show »
Length:1,643
Mass (Da):191,308
Checksum:iC41FBD5551FB644E
GO
Isoform 5 (identifier: Q99996-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2895-2948: Missing.

Show »
Length:3,857
Mass (Da):447,753
Checksum:i6DEB35CA282A0FDD
GO
Isoform 6 (identifier: Q99996-6) [UniParc]FASTAAdd to Basket

Also known as: AKAP350

The sequence of this isoform differs from the canonical sequence as follows:
     2175-2183: SADTFQKVE → Q
     2895-2907: VFGFYNMCFSTLC → GSSIPELAHSDAYQTREICSS
     3901-3911: STTQFHAGMRR → ALSLTTSWQHHSARPTAPLFFEILSHSLG

Show »
Length:3,929
Mass (Da):455,423
Checksum:iEE569AD99523AE2F
GO

Sequence cautioni

The sequence AAB86384.1 differs from that shown. Reason: Frameshift at position 1637. Curated
The sequence AAC60380.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761E → Q in BAA78718. (PubMed:10358086)Curated
Sequence conflicti554 – 5541E → G in BAA78718. (PubMed:10358086)Curated
Sequence conflicti638 – 6381R → S in BAA78718. (PubMed:10358086)Curated
Sequence conflicti663 – 6631N → S in BAA78718. (PubMed:10358086)Curated
Sequence conflicti913 – 9131H → N in BAA78718. (PubMed:10358086)Curated
Sequence conflicti956 – 9561K → N in BAA78718. (PubMed:10358086)Curated
Sequence conflicti980 – 9823QKH → PKP in AAB86384. (PubMed:9482789)Curated
Sequence conflicti980 – 9823QKH → PKP in CAB40713. (PubMed:10202149)Curated
Sequence conflicti997 – 9971Q → P in AAB86384. (PubMed:9482789)Curated
Sequence conflicti997 – 9971Q → P in CAB40713. (PubMed:10202149)Curated
Sequence conflicti1001 – 10011Q → P in AAB86384. (PubMed:9482789)Curated
Sequence conflicti1001 – 10011Q → P in CAB40713. (PubMed:10202149)Curated
Sequence conflicti1020 – 10201N → D in BAA78718. (PubMed:10358086)Curated
Sequence conflicti1028 – 10281V → E in BAA78718. (PubMed:10358086)Curated
Sequence conflicti1626 – 16261R → P in AAB86384. (PubMed:9482789)Curated
Sequence conflicti1626 – 16261R → P in CAB40713. (PubMed:10202149)Curated
Sequence conflicti1703 – 17031N → T in BAA78718. (PubMed:10358086)Curated
Sequence conflicti1707 – 17071V → G in BAA78718. (PubMed:10358086)Curated
Sequence conflicti1802 – 18032Missing in AAD22767. (PubMed:9915845)Curated
Sequence conflicti1843 – 18431A → P in BAA78718. (PubMed:10358086)Curated
Sequence conflicti1956 – 19561I → V in BAA78718. (PubMed:10358086)Curated
Sequence conflicti2027 – 20271V → D in AAD22767. (PubMed:9915845)Curated
Sequence conflicti2157 – 21582EI → HE in AAD39719. (PubMed:9915845)Curated
Sequence conflicti2169 – 21691E → V in BAA78718. (PubMed:10358086)Curated
Sequence conflicti2514 – 25141L → R in BAA78718. (PubMed:10358086)Curated
Sequence conflicti2851 – 28511I → N in BAA34523. (PubMed:9872452)Curated
Sequence conflicti2957 – 29571E → D in BAA78718. (PubMed:10358086)Curated
Sequence conflicti3087 – 30871Q → H in BAA78718. (PubMed:10358086)Curated
Sequence conflicti3218 – 32181Q → H in BAA78718. (PubMed:10358086)Curated
Sequence conflicti3307 – 33093ESE → QSQ in BAA78718. (PubMed:10358086)Curated
Sequence conflicti3751 – 37511P → A in BAA78718. (PubMed:10358086)Curated
Sequence conflicti3833 – 38331T → S in BAA78718. (PubMed:10358086)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti475 – 4751M → I.1 Publication
Corresponds to variant rs6964587 [ dbSNP | Ensembl ].
VAR_024249
Natural varianti1347 – 13471K → KQ.1 Publication
VAR_010926
Natural varianti1582 – 15821S → L in LQT11. 1 Publication
VAR_043489
Natural varianti2421 – 24211M → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035785
Natural varianti2496 – 24961K → R.
Corresponds to variant rs35759833 [ dbSNP | Ensembl ].
VAR_043490
Natural varianti2804 – 28041N → S.
Corresponds to variant rs6960867 [ dbSNP | Ensembl ].
VAR_030162
Natural varianti2983 – 29831P → S.3 Publications
Corresponds to variant rs1063242 [ dbSNP | Ensembl ].
VAR_030163
Natural varianti3301 – 33011E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035786
Natural varianti3448 – 34481Q → R.
Corresponds to variant rs34956633 [ dbSNP | Ensembl ].
VAR_043491
Natural varianti3618 – 36181M → V.
Corresponds to variant rs34327395 [ dbSNP | Ensembl ].
VAR_043492

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei17 – 2812Missing in isoform 2 and isoform 3. 3 PublicationsVSP_004102Add
BLAST
Alternative sequencei1637 – 16437QLQEEIK → LAQVRVL in isoform 4. 1 PublicationVSP_004103
Alternative sequencei1644 – 39112268Missing in isoform 4. 1 PublicationVSP_004104Add
BLAST
Alternative sequencei2175 – 21839SADTFQKVE → Q in isoform 6. 1 PublicationVSP_004106
Alternative sequencei2175 – 21828Missing in isoform 3. 1 PublicationVSP_004105
Alternative sequencei2895 – 294854Missing in isoform 5. CuratedVSP_004108Add
BLAST
Alternative sequencei2895 – 290713VFGFY…FSTLC → GSSIPELAHSDAYQTREICS S in isoform 2, isoform 3 and isoform 6. 3 PublicationsVSP_004107Add
BLAST
Alternative sequencei3901 – 391111STTQFHAGMRR → ALSLTTSWQHHSARPTAPLF FEILSHSLG in isoform 6. 1 PublicationVSP_004109Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131693 mRNA. Translation: CAB40713.1.
AB019691 mRNA. Translation: BAA78718.1.
AJ010770 Genomic DNA. Translation: CAA09361.1.
AF026245 mRNA. Translation: AAB86384.1. Frameshift.
AC004013 Genomic DNA. Translation: AAB96867.2.
AC000066 Genomic DNA. Translation: AAC60380.1. Sequence problems.
AC000120 Genomic DNA. Translation: AAS07419.1.
CH236949 Genomic DNA. Translation: EAL24155.1.
CH236949 Genomic DNA. Translation: EAL24156.1.
CH236949 Genomic DNA. Translation: EAL24157.1.
AF083037 mRNA. Translation: AAD22767.1.
AF091711 mRNA. Translation: AAD39719.1.
AB018346 mRNA. Translation: BAA34523.1.
CCDSiCCDS5622.1. [Q99996-2]
PIRiT08880.
RefSeqiNP_005742.4. NM_005751.4. [Q99996-2]
NP_671714.1. NM_147185.2. [Q99996-3]
UniGeneiHs.651221.

Genome annotation databases

EnsembliENST00000356239; ENSP00000348573; ENSG00000127914. [Q99996-2]
GeneIDi10142.
KEGGihsa:10142.
UCSCiuc003ulf.3. human. [Q99996-3]
uc003ulg.3. human. [Q99996-2]

Polymorphism databases

DMDMi14194461.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131693 mRNA. Translation: CAB40713.1 .
AB019691 mRNA. Translation: BAA78718.1 .
AJ010770 Genomic DNA. Translation: CAA09361.1 .
AF026245 mRNA. Translation: AAB86384.1 . Frameshift.
AC004013 Genomic DNA. Translation: AAB96867.2 .
AC000066 Genomic DNA. Translation: AAC60380.1 . Sequence problems.
AC000120 Genomic DNA. Translation: AAS07419.1 .
CH236949 Genomic DNA. Translation: EAL24155.1 .
CH236949 Genomic DNA. Translation: EAL24156.1 .
CH236949 Genomic DNA. Translation: EAL24157.1 .
AF083037 mRNA. Translation: AAD22767.1 .
AF091711 mRNA. Translation: AAD39719.1 .
AB018346 mRNA. Translation: BAA34523.1 .
CCDSi CCDS5622.1. [Q99996-2 ]
PIRi T08880.
RefSeqi NP_005742.4. NM_005751.4. [Q99996-2 ]
NP_671714.1. NM_147185.2. [Q99996-3 ]
UniGenei Hs.651221.

3D structure databases

ProteinModelPortali Q99996.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115445. 40 interactions.
DIPi DIP-29942N.
IntActi Q99996. 23 interactions.
MINTi MINT-1174958.

PTM databases

PhosphoSitei Q99996.

Polymorphism databases

DMDMi 14194461.

Proteomic databases

MaxQBi Q99996.
PaxDbi Q99996.
PRIDEi Q99996.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356239 ; ENSP00000348573 ; ENSG00000127914 . [Q99996-2 ]
GeneIDi 10142.
KEGGi hsa:10142.
UCSCi uc003ulf.3. human. [Q99996-3 ]
uc003ulg.3. human. [Q99996-2 ]

Organism-specific databases

CTDi 10142.
GeneCardsi GC07P091570.
GeneReviewsi AKAP9.
HGNCi HGNC:379. AKAP9.
HPAi CAB012909.
HPA008548.
HPA026109.
MIMi 604001. gene.
611820. phenotype.
neXtProti NX_Q99996.
Orphaneti 101016. Romano-Ward syndrome.
PharmGKBi PA24673.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000110871.
HOVERGENi HBG050481.
InParanoidi Q99996.
KOi K16551.
OMAi KMRKFLD.
OrthoDBi EOG7VMP46.
PhylomeDBi Q99996.
TreeFami TF105408.

Enzyme and pathway databases

Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
SignaLinki Q99996.

Miscellaneous databases

ChiTaRSi AKAP9. human.
GeneWikii AKAP9.
GenomeRNAii 10142.
NextBioi 38371.
PROi Q99996.
SOURCEi Search...

Gene expression databases

Bgeei Q99996.
ExpressionAtlasi Q99996. baseline and differential.
Genevestigatori Q99996.

Family and domain databases

InterProi IPR028745. AKAP9.
IPR019528. PACT_domain.
[Graphical view ]
PANTHERi PTHR18932:SF10. PTHR18932:SF10. 1 hit.
Pfami PF10495. PACT_coil_coil. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1."
    Lin J.W., Wyszynski M., Madhavan R., Sealock R., Kim J.U., Sheng M.
    J. Neurosci. 18:2017-2027(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Brain.
  2. "Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450."
    Witczak O., Skaalhegg B.S., Keryer G., Bornens M., Tasken K., Jahnsen T., Oerstavik S.
    EMBO J. 18:1858-1868(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLN-1347 INS.
  3. "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus."
    Takahashi M., Shibata H., Shimakawa M., Miyamoto M., Mukai H., Ono Y.
    J. Biol. Chem. 274:17267-17274(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS ILE-475 AND SER-2983.
    Tissue: Brain.
  4. "Cloning of Hyperion."
    Kemmner W.A., Deiss S., Schwarz U.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "AKAP350, a multiply spliced protein kinase A-anchoring protein associated with centrosomes."
    Schmidt P.H., Dransfield D.T., Claudio J.O., Hawley R.G., Trotter K.W., Milgram S.L., Goldenring J.R.
    J. Biol. Chem. 274:3055-3066(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 323-3911 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 2157-3911 (ISOFORM 6), VARIANT SER-2983.
    Tissue: Gastric parietal cell and Lung.
  8. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2212-3911 (ISOFORMS 2/3), VARIANT SER-2983.
    Tissue: Brain.
  9. "AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member."
    Shanks R.A., Larocca M.C., Berryman M., Edwards J.C., Urushidani T., Navarre J., Goldenring J.R.
    J. Biol. Chem. 277:40973-40980(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLIC1; CLIC4 AND CLIC5.
  10. "Centrosomal anchoring of the protein kinase CK1delta mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450."
    Sillibourne J.E., Milne D.M., Takahashi M., Ono Y., Meek D.W.
    J. Mol. Biol. 322:785-797(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSNK1D, SUBCELLULAR LOCATION.
  11. "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus."
    Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., Goldenring J.R.
    Mol. Biol. Cell 15:2771-2781(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CIP4 AND FNBP1, SUBCELLULAR LOCATION.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "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-165 AND SER-3846, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-2421 AND GLN-3301.
  16. Cited for: VARIANT LQT11 LEU-1582.

Entry informationi

Entry nameiAKAP9_HUMAN
AccessioniPrimary (citable) accession number: Q99996
Secondary accession number(s): A4D1F0
, A4D1F2, A4D1F4, O14869, O43355, O94895, Q75N20, Q9UQH3, Q9UQQ4, Q9Y6B8, Q9Y6Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: August 1, 1999
Last modified: October 29, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3