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P13861

- KAP2_HUMAN

UniProt

P13861 - KAP2_HUMAN

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Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

PRKAR2A

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

Functioni

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei208 – 2081cAMP 1
Binding sitei217 – 2171cAMP 1
Binding sitei338 – 3381cAMP 2
Binding sitei347 – 3471cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi139 – 260122cAMP 1Add
BLAST
Nucleotide bindingi261 – 404144cAMP 2Add
BLAST

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
  3. cAMP-dependent protein kinase regulator activity Source: UniProtKB
  4. protein kinase A catalytic subunit binding Source: BHF-UCL
  5. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. activation of phospholipase C activity Source: Reactome
  2. activation of protein kinase A activity Source: Reactome
  3. blood coagulation Source: Reactome
  4. cellular response to glucagon stimulus Source: Reactome
  5. energy reserve metabolic process Source: Reactome
  6. epidermal growth factor receptor signaling pathway Source: Reactome
  7. fibroblast growth factor receptor signaling pathway Source: Reactome
  8. innate immune response Source: Reactome
  9. intracellular signal transduction Source: ProtInc
  10. negative regulation of cAMP-dependent protein kinase activity Source: BHF-UCL
  11. neurotrophin TRK receptor signaling pathway Source: Reactome
  12. regulation of insulin secretion Source: Reactome
  13. signal transduction Source: Reactome
  14. small molecule metabolic process Source: Reactome
  15. transmembrane transport Source: Reactome
  16. water transport Source: Reactome
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15334. DARPP-32 events.
REACT_15530. PKA activation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_1946. PKA activation in glucagon signalling.
REACT_24023. Regulation of water balance by renal Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP13861.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene namesi
Name:PRKAR2A
Synonyms:PKR2, PRKAR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9391. PRKAR2A.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane 1 Publication
Note: Colocalizes with PJA2 in the cytoplasm and the cell membrane.

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: BHF-UCL
  2. cAMP-dependent protein kinase complex Source: InterPro
  3. centrosome Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProtKB
  7. focal adhesion Source: UniProtKB
  8. membrane Source: UniProtKB
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33757.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 404403cAMP-dependent protein kinase type II-alpha regulatory subunitPRO_0000205385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei54 – 541Phosphothreonine2 Publications
Modified residuei58 – 581Phosphoserine2 Publications
Modified residuei78 – 781Phosphoserine4 Publications
Modified residuei80 – 801Phosphoserine4 Publications
Modified residuei99 – 991Phosphoserine; by PKA4 Publications
Modified residuei215 – 2151Phosphothreonine; by PDPK1By similarity

Post-translational modificationi

Phosphorylated by the activated catalytic chain.6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13861.
PaxDbiP13861.
PRIDEiP13861.

2D gel databases

OGPiP13861.

PTM databases

PhosphoSiteiP13861.

Expressioni

Tissue specificityi

Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Gene expression databases

BgeeiP13861.
CleanExiHS_PRKAR2A.
ExpressionAtlasiP13861. baseline and differential.
GenevestigatoriP13861.

Organism-specific databases

HPAiCAB005023.

Interactioni

Subunit structurei

The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with AKAP4 and CBFA2T3. Interacts with the phosphorylated form of PJA2. Interacts with MYRIP. This interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P03259-25EBI-2556122,EBI-7225021From a different organism.
AKAP1Q926673EBI-2556122,EBI-2119593
AKAP3O759692EBI-2556122,EBI-9033101

Protein-protein interaction databases

BioGridi111562. 39 interactions.
DIPiDIP-552N.
IntActiP13861. 19 interactions.
MINTiMINT-5000495.
STRINGi9606.ENSP00000265563.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2415
Helixi29 – 4315

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IZXX-ray1.30A/B4-44[»]
2KYGNMR-A/B1-45[»]
ProteinModelPortaliP13861.
SMRiP13861. Positions 4-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13861.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 138137Dimerization and phosphorylationAdd
BLAST

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP13861.
KOiK04739.
OMAiLEMSERM.
PhylomeDBiP13861.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. cAMP/cGMP_kin.
IPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P13861-1) [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
MSHIQIPPGL TELLQGYTVE VLRQQPPDLV EFAVEYFTRL REARAPASVL
60 70 80 90 100
PAATPRQSLG HPPPEPGPDR VADAKGDSES EEDEDLEVPV PSRFNRRVSV
110 120 130 140 150
CAETYNPDEE EEDTDPRVIH PKTDEQRCRL QEACKDILLF KNLDQEQLSQ
160 170 180 190 200
VLDAMFERIV KADEHVIDQG DDGDNFYVIE RGTYDILVTK DNQTRSVGQY
210 220 230 240 250
DNRGSFGELA LMYNTPRAAT IVATSEGSLW GLDRVTFRRI IVKNNAKKRK
260 270 280 290 300
MFESFIESVP LLKSLEVSER MKIVDVIGEK IYKDGERIIT QGEKADSFYI
310 320 330 340 350
IESGEVSILI RSRTKSNKDG GNQEVEIARC HKGQYFGELA LVTNKPRAAS
360 370 380 390 400
AYAVGDVKCL VMDVQAFERL LGPCMDIMKR NISHYEEQLV KMFGSSVDLG

NLGQ
Length:404
Mass (Da):45,518
Last modified:January 23, 2007 - v2
Checksum:iC7D6E8E476E1DB65
GO
Isoform 2 (identifier: P13861-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     292-313: Missing.

Show »
Length:382
Mass (Da):43,067
Checksum:i87D6AC1A5CE9E300
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei292 – 31322Missing in isoform 2. 2 PublicationsVSP_056821Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14968 mRNA. Translation: CAA33094.1.
BT007225 mRNA. Translation: AAP35889.1.
AC141002 Genomic DNA. No translation available.
AC144546 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64926.1.
CH471055 Genomic DNA. Translation: EAW64927.1.
BC002763 mRNA. Translation: AAH02763.1.
X99455 Genomic DNA. Translation: CAA67817.1.
CCDSiCCDS2778.1.
PIRiS03885. OKHU2R.
RefSeqiNP_004148.1. NM_004157.2.
XP_005265370.1. XM_005265313.1.
UniGeneiHs.631923.

Genome annotation databases

EnsembliENST00000265563; ENSP00000265563; ENSG00000114302.
ENST00000454963; ENSP00000394041; ENSG00000114302.
GeneIDi5576.
KEGGihsa:5576.
UCSCiuc003cux.1. human.

Polymorphism databases

DMDMi125198.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14968 mRNA. Translation: CAA33094.1 .
BT007225 mRNA. Translation: AAP35889.1 .
AC141002 Genomic DNA. No translation available.
AC144546 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64926.1 .
CH471055 Genomic DNA. Translation: EAW64927.1 .
BC002763 mRNA. Translation: AAH02763.1 .
X99455 Genomic DNA. Translation: CAA67817.1 .
CCDSi CCDS2778.1.
PIRi S03885. OKHU2R.
RefSeqi NP_004148.1. NM_004157.2.
XP_005265370.1. XM_005265313.1.
UniGenei Hs.631923.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IZX X-ray 1.30 A/B 4-44 [» ]
2KYG NMR - A/B 1-45 [» ]
ProteinModelPortali P13861.
SMRi P13861. Positions 4-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111562. 39 interactions.
DIPi DIP-552N.
IntActi P13861. 19 interactions.
MINTi MINT-5000495.
STRINGi 9606.ENSP00000265563.

Chemistry

BindingDBi P13861.

PTM databases

PhosphoSitei P13861.

Polymorphism databases

DMDMi 125198.

2D gel databases

OGPi P13861.

Proteomic databases

MaxQBi P13861.
PaxDbi P13861.
PRIDEi P13861.

Protocols and materials databases

DNASUi 5576.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265563 ; ENSP00000265563 ; ENSG00000114302 .
ENST00000454963 ; ENSP00000394041 ; ENSG00000114302 .
GeneIDi 5576.
KEGGi hsa:5576.
UCSCi uc003cux.1. human.

Organism-specific databases

CTDi 5576.
GeneCardsi GC03M048782.
HGNCi HGNC:9391. PRKAR2A.
HPAi CAB005023.
MIMi 176910. gene.
neXtProti NX_P13861.
PharmGKBi PA33757.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0664.
GeneTreei ENSGT00530000062947.
HOGENOMi HOG000196668.
HOVERGENi HBG002025.
InParanoidi P13861.
KOi K04739.
OMAi LEMSERM.
PhylomeDBi P13861.
TreeFami TF314920.

Enzyme and pathway databases

Reactomei REACT_15334. DARPP-32 events.
REACT_15530. PKA activation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_1946. PKA activation in glucagon signalling.
REACT_24023. Regulation of water balance by renal Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinki P13861.

Miscellaneous databases

ChiTaRSi PRKAR2A. human.
EvolutionaryTracei P13861.
GeneWikii PRKAR2A.
GenomeRNAii 5576.
NextBioi 21620.
PROi P13861.
SOURCEi Search...

Gene expression databases

Bgeei P13861.
CleanExi HS_PRKAR2A.
ExpressionAtlasi P13861. baseline and differential.
Genevestigatori P13861.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR002373. cAMP/cGMP_kin.
IPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view ]
Pfami PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view ]
PIRSFi PIRSF000548. PK_regulatory. 1 hit.
PRINTSi PR00103. CAMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view ]
SUPFAMi SSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human testis cDNA for the regulatory subunit RII alpha of cAMP-dependent protein kinase encodes an alternate amino-terminal region."
    Oyen O., Myklebust F., Scott J.D., Hansson V., Jahnsen T.
    FEBS Lett. 246:57-64(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Placenta.
  6. "Molecular cloning, upstream sequence and promoter studies of the human gene for the regulatory subunit RII alpha of cAMP-dependent protein kinase."
    Foss K.B., Solberg R., Simard J., Myklebust F., Hansson V., Jahnsen T., Tasken K.
    Biochim. Biophys. Acta 1350:98-108(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87.
  7. "Identification and characterization of myeloid translocation gene 16b as a novel a kinase anchoring protein in T lymphocytes."
    Schillace R.V., Andrews S.F., Liberty G.A., Davey M.P., Carr D.W.
    J. Immunol. 168:1590-1599(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBFA2T3.
  8. "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-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  10. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  11. Cited for: INTERACTION WITH MYRIP.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78; SER-80 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-78; SER-80 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "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-48; THR-54; SER-58; SER-78 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PJA2.
  22. "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-78 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKAP2_HUMAN
AccessioniPrimary (citable) accession number: P13861
Secondary accession number(s): Q16823, Q9BUB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 155 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3