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Protein

A-kinase anchor protein 7 isoform gamma

Gene

AKAP7

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

Functioni

Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291AMPBy similarity
Binding sitei129 – 1291CMPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi219 – 2213AMPBy similarity
Nucleotide bindingi219 – 2213CMPBy similarity

GO - Molecular functioni

  • nucleotide binding Source: UniProtKB-KW
  • protein kinase A binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 7 isoform gamma
Short name:
AKAP-7 isoform gamma
Alternative name(s):
A-kinase anchor protein 18 kDa
Short name:
AKAP 18
Protein kinase A-anchoring protein 7 isoform gamma
Short name:
PRKA7 isoform gamma
Gene namesi
Name:AKAP7
Synonyms:AKAP18
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:377. AKAP7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24671.

Polymorphism and mutation databases

BioMutaiCNTNAP2.
DMDMi357528766.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348A-kinase anchor protein 7 isoform gammaPRO_0000064523Add
BLAST

Proteomic databases

EPDiQ9P0M2.
MaxQBiQ9P0M2.
PaxDbiQ9P0M2.
PeptideAtlasiQ9P0M2.
PRIDEiQ9P0M2.

PTM databases

iPTMnetiQ9P0M2.
PhosphoSiteiQ9P0M2.

Expressioni

Tissue specificityi

Expressed in brain, heart, lung, pancreas and placenta.1 Publication

Gene expression databases

BgeeiQ9P0M2.
CleanExiHS_AKAP7.
ExpressionAtlasiQ9P0M2. baseline and differential.
GenevisibleiQ9P0M2. HS.

Organism-specific databases

HPAiHPA027172.
HPA028327.

Interactioni

Subunit structurei

Binds cAMP-dependent protein kinase (PKA). Interacts with PRKCA; only the cytoplasmic form is capable of interacting with PRKCA.1 Publication

GO - Molecular functioni

  • protein kinase A binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114851. 17 interactions.
IntActiQ9P0M2. 3 interactions.
STRINGi9606.ENSP00000405252.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZP3X-ray2.63M/N/O/P/Q/R287-326[»]
ProteinModelPortaliQ9P0M2.
SMRiQ9P0M2. Positions 83-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni294 – 34855PKA-RII-alpha subunit binding domainBy similarityAdd
BLAST
Regioni295 – 31925RI-alpha-bindingBy similarityAdd
BLAST
Regioni296 – 30914RII-bindingAdd
BLAST

Phylogenomic databases

eggNOGiKOG2814. Eukaryota.
ENOG4111FMP. LUCA.
GeneTreeiENSGT00390000012756.
HOGENOMiHOG000294077.
HOVERGENiHBG050475.
InParanoidiQ9P0M2.
OMAiIGEKNGG.
TreeFamiTF105406.

Family and domain databases

Gene3Di3.90.1140.10. 1 hit.
InterProiIPR019511. AKAP7_RI-RII-bd_dom.
IPR019510. Kinase-A_anchor_nucl_local_sig.
IPR009097. RNA_ligase/cNuc_Pdiesterase.
[Graphical view]
PfamiPF10469. AKAP7_NLS. 1 hit.
PF10470. AKAP7_RIRII_bdg. 1 hit.
[Graphical view]
SUPFAMiSSF55144. SSF55144. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform Gamma (identifier: Q9P0M2-1) [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
MERPEAGGIN SNECENVSRK KKMSEEFEAN TMDSLVDMPF ATVDIQDDCG
60 70 80 90 100
ITDEPQINLK RSQENEWVKS DQVKKRKKKR KDYQPNYFLS IPITNKEIIK
110 120 130 140 150
GIKILQNAII QQDERLAKAM VSDGSFHITL LVMQLLNEDE VNIGIDALLE
160 170 180 190 200
LKPFIEELLQ GKHLTLPFQG IGTFGNQVGF VKLAEGDHVN SLLEIAETAN
210 220 230 240 250
RTFQEKGILV GESRSFKPHL TFMKLSKSPW LRKNGVKKID PDLYEKFISH
260 270 280 290 300
RFGEEILYRI DLCSMLKKKQ SNGYYHCESS IVIGEKNGGE PDDAELVRLS
310 320 330 340
KRLVENAVLK AVQQYLEETQ NKNKPGEGSS VKTEAADQNG NDNENNRK
Length:348
Mass (Da):39,518
Last modified:November 16, 2011 - v2
Checksum:i642221A7CA8730CA
GO
Isoform Alpha (identifier: O43687-2) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry O43687.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:81
Mass (Da):8,969
GO
Isoform Beta (identifier: O43687-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry O43687.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:104
Mass (Da):11,465
GO

Sequence cautioni

The sequence AAF28106.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAI19003.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI19788.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI21509.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261E → K.
Corresponds to variant rs7771473 [ dbSNP | Ensembl ].
VAR_024246
Natural varianti215 – 2151S → N.
Corresponds to variant rs1190788 [ dbSNP | Ensembl ].
VAR_024247

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK300587 mRNA. Translation: BAG62285.1.
AL137063, AL136110, AL137222 Genomic DNA. Translation: CAI19003.1. Sequence problems.
AL137222, AL136110, AL137063 Genomic DNA. Translation: CAI19788.1. Sequence problems.
AL136110, AL137063, AL137222 Genomic DNA. Translation: CAI21509.1. Sequence problems.
AF152929 mRNA. Translation: AAF28106.1. Different initiation.
CCDSiCCDS5142.2. [Q9P0M2-1]
RefSeqiNP_057461.2. NM_016377.3. [Q9P0M2-1]
UniGeneiHs.486483.
Hs.732515.

Genome annotation databases

EnsembliENST00000431975; ENSP00000405252; ENSG00000118507. [Q9P0M2-1]
GeneIDi9465.
UCSCiuc003qck.5. human. [Q9P0M2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK300587 mRNA. Translation: BAG62285.1.
AL137063, AL136110, AL137222 Genomic DNA. Translation: CAI19003.1. Sequence problems.
AL137222, AL136110, AL137063 Genomic DNA. Translation: CAI19788.1. Sequence problems.
AL136110, AL137063, AL137222 Genomic DNA. Translation: CAI21509.1. Sequence problems.
AF152929 mRNA. Translation: AAF28106.1. Different initiation.
CCDSiCCDS5142.2. [Q9P0M2-1]
RefSeqiNP_057461.2. NM_016377.3. [Q9P0M2-1]
UniGeneiHs.486483.
Hs.732515.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZP3X-ray2.63M/N/O/P/Q/R287-326[»]
ProteinModelPortaliQ9P0M2.
SMRiQ9P0M2. Positions 83-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114851. 17 interactions.
IntActiQ9P0M2. 3 interactions.
STRINGi9606.ENSP00000405252.

PTM databases

iPTMnetiQ9P0M2.
PhosphoSiteiQ9P0M2.

Polymorphism and mutation databases

BioMutaiCNTNAP2.
DMDMi357528766.

Proteomic databases

EPDiQ9P0M2.
MaxQBiQ9P0M2.
PaxDbiQ9P0M2.
PeptideAtlasiQ9P0M2.
PRIDEiQ9P0M2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000431975; ENSP00000405252; ENSG00000118507. [Q9P0M2-1]
GeneIDi9465.
UCSCiuc003qck.5. human. [Q9P0M2-1]

Organism-specific databases

CTDi9465.
GeneCardsiAKAP7.
H-InvDBHIX0032781.
HGNCiHGNC:377. AKAP7.
HPAiHPA027172.
HPA028327.
MIMi604693. gene.
neXtProtiNX_Q9P0M2.
PharmGKBiPA24671.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2814. Eukaryota.
ENOG4111FMP. LUCA.
GeneTreeiENSGT00390000012756.
HOGENOMiHOG000294077.
HOVERGENiHBG050475.
InParanoidiQ9P0M2.
OMAiIGEKNGG.
TreeFamiTF105406.

Miscellaneous databases

ChiTaRSiAKAP7. human.
GenomeRNAii9465.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0M2.
CleanExiHS_AKAP7.
ExpressionAtlasiQ9P0M2. baseline and differential.
GenevisibleiQ9P0M2. HS.

Family and domain databases

Gene3Di3.90.1140.10. 1 hit.
InterProiIPR019511. AKAP7_RI-RII-bd_dom.
IPR019510. Kinase-A_anchor_nucl_local_sig.
IPR009097. RNA_ligase/cNuc_Pdiesterase.
[Graphical view]
PfamiPF10469. AKAP7_NLS. 1 hit.
PF10470. AKAP7_RIRII_bdg. 1 hit.
[Graphical view]
SUPFAMiSSF55144. SSF55144. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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.
    , 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].
  3. "Alternative splicing regulates the subcellular localization of A-kinase anchoring protein 18 isoforms."
    Trotter K.W., Fraser I.D.C., Scott G.K., Stutts M.J., Scott J.D., Milgram S.L.
    J. Cell Biol. 147:1481-1492(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-348, FUNCTION, RII-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Lung.
  4. "The A-kinase anchoring protein 15 regulates feedback inhibition of the epithelial Na+ channel."
    Bengrine A., Li J., Awayda M.S.
    FASEB J. 21:1189-1201(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKCA.

Entry informationi

Entry nameiAKA7G_HUMAN
AccessioniPrimary (citable) accession number: Q9P0M2
Secondary accession number(s): B4DUC3, Q9HCZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 16, 2011
Last modified: July 6, 2016
This is version 119 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.