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Protein

A-kinase anchor protein 2

Gene

AKAP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (By similarity).By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 2
Short name:
AKAP-2
Alternative name(s):
AKAP-KL
Protein kinase A-anchoring protein 2
Short name:
PRKA2
Gene namesi
Name:AKAP2
Synonyms:KIAA0920, PRKA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:372. AKAP2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162398639.

Polymorphism and mutation databases

BioMutaiAKAP2.
DMDMi254763433.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859A-kinase anchor protein 2PRO_0000064524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei91 – 911PhosphoserineCombined sources
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei152 – 1521PhosphoserineCombined sources
Modified residuei336 – 3361PhosphoserineBy similarity
Modified residuei393 – 3931PhosphoserineCombined sources
Modified residuei461 – 4611PhosphoserineCombined sources
Modified residuei465 – 4651PhosphoserineBy similarity
Modified residuei473 – 4731PhosphoserineBy similarity
Modified residuei517 – 5171PhosphoserineCombined sources
Modified residuei526 – 5261PhosphothreonineCombined sources
Modified residuei631 – 6311PhosphoserineCombined sources
Modified residuei720 – 7201PhosphoserineCombined sources
Modified residuei748 – 7481PhosphoserineCombined sources
Modified residuei778 – 7781PhosphoserineCombined sources
Modified residuei785 – 7851PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y2D5.
MaxQBiQ9Y2D5.
PaxDbiQ9Y2D5.
PRIDEiQ9Y2D5.

PTM databases

iPTMnetiQ9Y2D5.
PhosphoSiteiQ9Y2D5.
SwissPalmiQ9Y2D5.

Expressioni

Gene expression databases

BgeeiQ9Y2D5.
CleanExiHS_AKAP2.
ExpressionAtlasiQ9Y2D5. baseline and differential.
GenevisibleiQ9Y2D5. HS.

Organism-specific databases

HPAiHPA058905.

Interactioni

Protein-protein interaction databases

BioGridi116386. 37 interactions.
138657. 5 interactions.
IntActiQ9Y2D5. 33 interactions.
STRINGi9606.ENSP00000451476.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2D5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni566 – 57914PKA-RII subunit binding domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili213 – 29078Sequence analysisAdd
BLAST
Coiled coili710 – 74839Sequence analysisAdd
BLAST

Domaini

The 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.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG9A. Eukaryota.
ENOG410ZMFZ. LUCA.
GeneTreeiENSGT00530000063206.
HOVERGENiHBG050477.
InParanoidiQ9Y2D5.
KOiK16519.
OMAiVRPSEEM.
OrthoDBiEOG7PS1DX.
PhylomeDBiQ9Y2D5.
TreeFamiTF105402.

Family and domain databases

InterProiIPR029304. AKAP2_C.
[Graphical view]
PfamiPF15304. AKAP2_C. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2D5-3) [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
MEIEVSVAEC KSVPGITSTP HPMDHPSAFY SPPHNGLLTD HHESLDNDVA
60 70 80 90 100
REIRYLDEVL EANCCDSAVD GTYNGTSSPE PGAVVLVGGL SPPVHEATQP
110 120 130 140 150
EPTERTASRQ APPHIELSNS SPDPMAEAER TNGHSPSQPR DALGDSLQVP
160 170 180 190 200
VSPSSTTSSR CSSRDGEFTL TTLKKEAKFE LRAFHEDKKP SKLFEDDEHE
210 220 230 240 250
KEQYCIRKVR PSEEMLELEK ERRELIRSQA VKKNPGIAAK WWNPPQEKTI
260 270 280 290 300
EEQLDEEHLE SHKKYKERKE RRAQQEQLLL QKQLQQQQQQ PPSQLCTAPA
310 320 330 340 350
SSHERASMID KAKEDIVTEQ IDFSAARKQF QLMENSRQAV AKGQSTPRLF
360 370 380 390 400
SIKPFYRPLG SVNSDKPLTN PRPPSVGGPP EDSGASAAKG QKSPGALETP
410 420 430 440 450
SAAGSQGNTA SQGKEGPYSE PSKRGPLSKL WAEDGEFTSA RAVLTVVKDD
460 470 480 490 500
DHGILDQFSR SVNVSLTQEE LDSGLDELSV RSQDTTVLET LSNDFSMDNI
510 520 530 540 550
SDSGASNETT NALQENSLAD FSLPQTPQTD NPSEGRGEGV SKSFSDHGFY
560 570 580 590 600
SPSSTLGDSP LVDDPLEYQA GLLVQNAIQQ AIAEQVDKAV SKTSRDGAEQ
610 620 630 640 650
QGPEATVEEA EAAAFGSEKP QSMFEPPQVS SPVQEKRDVL PKILPAEDRA
660 670 680 690 700
LRERGPPQPL PAVQPSGPIN MEETRPEGSY FSKYSEAAEL RSTASLLATQ
710 720 730 740 750
ESDVMVGPFK LRSRKQRTLS MIEEEIRAAQ EREEELKRQR QVLQSTQSPR
760 770 780 790 800
TKNAPSLPSR TCYKTAPGKI EKVKPPPSPT TEGPSLQPDL APEEAAGTQR
810 820 830 840 850
PKNLMQTLME DYETHKSKRR ERMDDSSVLE ATRVNRRKSA LALRWEAGIY

ANQEEEDNE
Length:859
Mass (Da):94,661
Last modified:July 28, 2009 - v3
Checksum:i6DCE563596DFBA4B
GO
Isoform 2 (identifier: Q9Y2D5-4) [UniParc]FASTAAdd to basket

Also known as: PALM2-AKAP2

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAEAELHKER...SSLSPDHKNM
     827-827: S → SYTSKLLSCKVTSE

Note: Based on a naturally occurring readthrough transcript which produces a PALM2-AKAP2 fusion protein.
Show »
Length:1,103
Mass (Da):122,071
Checksum:iB501182135112FE5
GO
Isoform 3 (identifier: Q9Y2D5-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRWPQPGAAA...SSLSPDHKNM

Show »
Length:948
Mass (Da):104,107
Checksum:i9DBF30D86F05F61F
GO
Isoform 4 (identifier: Q9Y2D5-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAEAELHKER...SSLSPDHKNM

Note: Based on a naturally occurring readthrough transcript which produces a PALM2-AKAP2 fusion protein.
Show »
Length:1,090
Mass (Da):120,630
Checksum:i51F5C843CC9C1A4C
GO
Isoform 5 (identifier: Q9Y2D5-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRWPQPGAAA...SSLSPDHKNM
     827-827: S → SYTSKLLSCKVTSE

Show »
Length:961
Mass (Da):105,548
Checksum:iD2BF4A482F710D91
GO

Sequence cautioni

The sequence BAA76764.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821K → Q in BAG51862 (PubMed:14702039).Curated
Sequence conflicti282 – 2821K → Q in BAG62154 (PubMed:14702039).Curated
Sequence conflicti282 – 2821K → Q in AAI46864 (PubMed:15489334).Curated
Sequence conflicti282 – 2821K → Q in AAI71800 (PubMed:15489334).Curated
Sequence conflicti647 – 6471E → G in CAB53707 (PubMed:17974005).Curated
Sequence conflicti651 – 6511L → P in BAG51862 (PubMed:14702039).Curated
Sequence conflicti719 – 7191L → S in BAG51862 (PubMed:14702039).Curated
Isoform 3 (identifier: Q9Y2D5-5)
Sequence conflicti20 – 201P → L in AAI46864 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti561 – 5611L → S.2 Publications
Corresponds to variant rs914358 [ dbSNP | Ensembl ].
VAR_024248

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAEAELHKERLQAIAEKRKR QTEIEGKRQQLDEQILLLQH SKSKVLREKWLLQGIPAGTA EEEEARRRQSEEDEFRVKQL EDNIQRLEQEIQTLESEESQ ISAKEQIILEKLKETEKSFK DFQKGFSSTDGDAVNYISSQ LPDLPILCSRTAEPSPGQDG TSRAAGVGWENVLLKEGESA SNATETSGPDMTIKKPPQLS EDDIWLKSEGDNYSATLLEP AASSLSPDHKNM in isoform 2 and isoform 4. 3 PublicationsVSP_037769
Alternative sequencei1 – 11M → MRWPQPGAAARLPPESPGPP ESPGPPEREAAAARRWTGAE PQDCAPGSGRPEKPPQLSED DIWLKSEGDNYSATLLEPAA SSLSPDHKNM in isoform 3 and isoform 5. 2 PublicationsVSP_037770
Alternative sequencei827 – 8271S → SYTSKLLSCKVTSE in isoform 2 and isoform 5. 3 PublicationsVSP_037771

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ303079 mRNA. Translation: CAC38839.1.
AB023137 mRNA. Translation: BAA76764.2. Different initiation.
AK057098 mRNA. Translation: BAG51862.1.
AK300427 mRNA. Translation: BAG62154.1.
AL627225
, AL158823, AL158829, AL353598, AL353806 Genomic DNA. Translation: CAI10811.1.
AL353806
, AL158823, AL158829, AL353598, AL627225 Genomic DNA. Translation: CAI12434.1.
AL158829
, AL158823, AL353598, AL353806, AL627225 Genomic DNA. Translation: CAI13896.1.
AL158823
, AL158829, AL353598, AL353806, AL627225 Genomic DNA. Translation: CAI39560.1.
AL353598
, AL158823, AL158829, AL353806, AL627225 Genomic DNA. Translation: CAI40816.1.
CH471105 Genomic DNA. Translation: EAW59057.1.
BC140818 mRNA. Translation: AAI40819.1.
BC146863 mRNA. Translation: AAI46864.1.
BC171800 mRNA. Translation: AAI71800.1.
AL110268 mRNA. Translation: CAB53707.1.
CCDSiCCDS43861.1. [Q9Y2D5-5]
CCDS48003.1. [Q9Y2D5-3]
CCDS56581.1. [Q9Y2D5-7]
PIRiT14787.
RefSeqiNP_001004065.2. NM_001004065.4. [Q9Y2D5-5]
NP_001130034.1. NM_001136562.2. [Q9Y2D5-3]
NP_001185585.1. NM_001198656.1. [Q9Y2D5-7]
NP_009134.1. NM_007203.4. [Q9Y2D5-4]
NP_671492.1. NM_147150.2. [Q9Y2D5-6]
UniGeneiHs.591908.

Genome annotation databases

EnsembliENST00000259318; ENSP00000259318; ENSG00000241978. [Q9Y2D5-3]
ENST00000374525; ENSP00000363649; ENSG00000241978. [Q9Y2D5-5]
ENST00000434623; ENSP00000404782; ENSG00000241978. [Q9Y2D5-7]
GeneIDi11217.
445815.
KEGGihsa:11217.
hsa:445815.
UCSCiuc004bem.4. human. [Q9Y2D5-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ303079 mRNA. Translation: CAC38839.1.
AB023137 mRNA. Translation: BAA76764.2. Different initiation.
AK057098 mRNA. Translation: BAG51862.1.
AK300427 mRNA. Translation: BAG62154.1.
AL627225
, AL158823, AL158829, AL353598, AL353806 Genomic DNA. Translation: CAI10811.1.
AL353806
, AL158823, AL158829, AL353598, AL627225 Genomic DNA. Translation: CAI12434.1.
AL158829
, AL158823, AL353598, AL353806, AL627225 Genomic DNA. Translation: CAI13896.1.
AL158823
, AL158829, AL353598, AL353806, AL627225 Genomic DNA. Translation: CAI39560.1.
AL353598
, AL158823, AL158829, AL353806, AL627225 Genomic DNA. Translation: CAI40816.1.
CH471105 Genomic DNA. Translation: EAW59057.1.
BC140818 mRNA. Translation: AAI40819.1.
BC146863 mRNA. Translation: AAI46864.1.
BC171800 mRNA. Translation: AAI71800.1.
AL110268 mRNA. Translation: CAB53707.1.
CCDSiCCDS43861.1. [Q9Y2D5-5]
CCDS48003.1. [Q9Y2D5-3]
CCDS56581.1. [Q9Y2D5-7]
PIRiT14787.
RefSeqiNP_001004065.2. NM_001004065.4. [Q9Y2D5-5]
NP_001130034.1. NM_001136562.2. [Q9Y2D5-3]
NP_001185585.1. NM_001198656.1. [Q9Y2D5-7]
NP_009134.1. NM_007203.4. [Q9Y2D5-4]
NP_671492.1. NM_147150.2. [Q9Y2D5-6]
UniGeneiHs.591908.

3D structure databases

ProteinModelPortaliQ9Y2D5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116386. 37 interactions.
138657. 5 interactions.
IntActiQ9Y2D5. 33 interactions.
STRINGi9606.ENSP00000451476.

PTM databases

iPTMnetiQ9Y2D5.
PhosphoSiteiQ9Y2D5.
SwissPalmiQ9Y2D5.

Polymorphism and mutation databases

BioMutaiAKAP2.
DMDMi254763433.

Proteomic databases

EPDiQ9Y2D5.
MaxQBiQ9Y2D5.
PaxDbiQ9Y2D5.
PRIDEiQ9Y2D5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259318; ENSP00000259318; ENSG00000241978. [Q9Y2D5-3]
ENST00000374525; ENSP00000363649; ENSG00000241978. [Q9Y2D5-5]
ENST00000434623; ENSP00000404782; ENSG00000241978. [Q9Y2D5-7]
GeneIDi11217.
445815.
KEGGihsa:11217.
hsa:445815.
UCSCiuc004bem.4. human. [Q9Y2D5-3]

Organism-specific databases

CTDi11217.
445815.
GeneCardsiAKAP2.
HGNCiHGNC:372. AKAP2.
HPAiHPA058905.
MIMi604582. gene.
neXtProtiNX_Q9Y2D5.
PharmGKBiPA162398639.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG9A. Eukaryota.
ENOG410ZMFZ. LUCA.
GeneTreeiENSGT00530000063206.
HOVERGENiHBG050477.
InParanoidiQ9Y2D5.
KOiK16519.
OMAiVRPSEEM.
OrthoDBiEOG7PS1DX.
PhylomeDBiQ9Y2D5.
TreeFamiTF105402.

Miscellaneous databases

ChiTaRSiAKAP2. human.
GeneWikiiAKAP2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2D5.
CleanExiHS_AKAP2.
ExpressionAtlasiQ9Y2D5. baseline and differential.
GenevisibleiQ9Y2D5. HS.

Family and domain databases

InterProiIPR029304. AKAP2_C.
[Graphical view]
PfamiPF15304. AKAP2_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Homo sapiens AKAP-2 complete cDNA sequence."
    Schuetze N., Reichel S., Ruecker N., Lechner A., Eulert J., Jakob F.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Prediction of the coding sequences of unidentified human genes. XIII. 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., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  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.
    , 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] (ISOFORMS 1 AND 3), VARIANT SER-561.
    Tissue: Placenta and Small intestine.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 3; 4 AND 5), VARIANT SER-561.
    Tissue: Brain.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-859 (ISOFORMS 1/3/4).
    Tissue: Brain.
  8. "The paralemmin protein family: identification of paralemmin-2, an isoform differentially spliced to AKAP2/AKAP-KL, and of palmdelphin, a more distant cytosolic relative."
    Hu B., Copeland N.G., Gilbert D.J., Jenkins N.A., Kilimann M.W.
    Biochem. Biophys. Res. Commun. 285:1369-1376(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 3).
    Tissue: Muscle.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-152; SER-393; SER-631; SER-720 AND SER-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  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-152; SER-393; SER-461 AND SER-720, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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 SER-152; SER-393 AND SER-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-152; SER-393 AND SER-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-152; SER-393; SER-517; THR-526; SER-631; SER-778 AND SER-785, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAKAP2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2D5
Secondary accession number(s): B1ALX9
, B2RTU4, B3KQ00, B4DTZ2, B7ZW07, B9EJB5, Q9UG26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 28, 2009
Last modified: June 8, 2016
This is version 134 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 9
    Human chromosome 9: 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

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.