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O14976

- GAK_HUMAN

UniProt

O14976 - GAK_HUMAN

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Protein

Cyclin-G-associated kinase

Gene

GAK

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

Functioni

Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei173 – 1731Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: ProtInc

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell development Source: Ensembl
  3. clathrin coat disassembly Source: Ensembl
  4. clathrin-mediated endocytosis Source: Ensembl
  5. endoplasmic reticulum organization Source: Ensembl
  6. epidermal cell differentiation Source: Ensembl
  7. establishment of skin barrier Source: Ensembl
  8. forebrain morphogenesis Source: Ensembl
  9. Golgi organization Source: Ensembl
  10. intrahepatic bile duct development Source: Ensembl
  11. positive regulation of neural precursor cell proliferation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinkiO14976.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-G-associated kinase (EC:2.7.11.1)
Gene namesi
Name:GAK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4113. GAK.

Subcellular locationi

Cytoplasmperinuclear region 1 Publication. Golgi apparatustrans-Golgi network 1 Publication. Cell junctionfocal adhesion 1 Publication
Note: Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. Golgi apparatus Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Golgi apparatus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28528.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 13111310Cyclin-G-associated kinasePRO_0000085958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei16 – 161Phosphoserine2 Publications
Modified residuei456 – 4561Phosphoserine1 Publication
Modified residuei770 – 7701Phosphoserine1 Publication
Modified residuei826 – 8261Phosphoserine4 Publications
Modified residuei829 – 8291Phosphoserine5 Publications
Modified residuei834 – 8341Phosphoserine3 Publications
Modified residuei939 – 9391Phosphoserine1 Publication
Modified residuei1096 – 10961Phosphoserine1 Publication
Modified residuei1176 – 11761Phosphoserine1 Publication
Modified residuei1185 – 11851Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO14976.
PaxDbiO14976.
PRIDEiO14976.

PTM databases

PhosphoSiteiO14976.

Expressioni

Tissue specificityi

Ubiquitous. Highest in testis.

Gene expression databases

BgeeiO14976.
CleanExiHS_GAK.
ExpressionAtlasiO14976. baseline and differential.
GenevestigatoriO14976.

Organism-specific databases

HPAiHPA027405.
HPA027459.
HPA027463.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP13A2Q9NQ112EBI-714707,EBI-6308763
HSPA8P111425EBI-714707,EBI-351896
LRRK2Q5S00710EBI-714707,EBI-5323863

Protein-protein interaction databases

BioGridi108853. 13 interactions.
IntActiO14976. 10 interactions.
MINTiMINT-5000432.
STRINGi9606.ENSP00000314499.

Structurei

Secondary structure

1
1311
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni27 – 304Combined sources
Beta strandi32 – 354Combined sources
Beta strandi38 – 4710Combined sources
Beta strandi50 – 5910Combined sources
Turni60 – 623Combined sources
Beta strandi65 – 7511Combined sources
Helixi76 – 9217Combined sources
Beta strandi101 – 1077Combined sources
Turni109 – 1113Combined sources
Beta strandi115 – 12410Combined sources
Beta strandi127 – 1293Combined sources
Helixi130 – 1389Combined sources
Helixi145 – 16319Combined sources
Beta strandi165 – 1673Combined sources
Helixi176 – 1783Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi187 – 1893Combined sources
Helixi208 – 22114Combined sources
Helixi224 – 2263Combined sources
Helixi229 – 2324Combined sources
Helixi242 – 25817Combined sources
Turni262 – 2654Combined sources
Helixi268 – 2725Combined sources
Helixi286 – 2883Combined sources
Helixi289 – 2957Combined sources
Helixi300 – 3023Combined sources
Helixi306 – 31914Combined sources
Helixi329 – 3324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C57X-ray2.55A/B14-351[»]
4C58X-ray2.16A27-351[»]
4C59X-ray2.80A14-351[»]
4O38X-ray2.10A/B12-347[»]
ProteinModelPortaliO14976.
SMRiO14976. Positions 25-334, 400-746, 1139-1311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 314275Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini399 – 566168Phosphatase tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini572 – 710139C2 tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini1247 – 131165JPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi347 – 3504Poly-Pro

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 C2 tensin-type domain.PROSITE-ProRule annotation
Contains 1 J domain.PROSITE-ProRule annotation
Contains 1 phosphatase tensin-type domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000034235.
HOVERGENiHBG004322.
InParanoidiO14976.
KOiK08855.
OMAiYMCDMMA.
OrthoDBiEOG7WT40V.
PhylomeDBiO14976.
TreeFamiTF105165.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR001623. DnaJ_domain.
IPR011009. Kinase-like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00069. Pkinase. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[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: O14976-1) [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
MSLLQSALDF LAGPGSLGGA SGRDQSDFVG QTVELGELRL RVRRVLAEGG
60 70 80 90 100
FAFVYEAQDV GSGREYALKR LLSNEEEKNR AIIQEVCFMK KLSGHPNIVQ
110 120 130 140 150
FCSAASIGKE ESDTGQAEFL LLTELCKGQL VEFLKKMESR GPLSCDTVLK
160 170 180 190 200
IFYQTCRAVQ HMHRQKPPII HRDLKVENLL LSNQGTIKLC DFGSATTISH
210 220 230 240 250
YPDYSWSAQR RALVEEEITR NTTPMYRTPE IIDLYSNFPI GEKQDIWALG
260 270 280 290 300
CILYLLCFRQ HPFEDGAKLR IVNGKYSIPP HDTQYTVFHS LIRAMLQVNP
310 320 330 340 350
EERLSIAEVV HQLQEIAAAR NVNPKSPITE LLEQNGGYGS ATLSRGPPPP
360 370 380 390 400
VGPAGSGYSG GLALAEYDQP YGGFLDILRG GTERLFTNLK DTSSKVIQSV
410 420 430 440 450
ANYAKGDLDI SYITSRIAVM SFPAEGVESA LKNNIEDVRL FLDSKHPGHY
460 470 480 490 500
AVYNLSPRTY RPSRFHNRVS ECGWAARRAP HLHTLYNICR NMHAWLRQDH
510 520 530 540 550
KNVCVVHCMD GRAASAVAVC SFLCFCRLFS TAEAAVYMFS MKRCPPGIWP
560 570 580 590 600
SHKRYIEYMC DMVAEEPITP HSKPILVRAV VMTPVPLFSK QRSGCRPFCE
610 620 630 640 650
VYVGDERVAS TSQEYDKMRD FKIEDGKAVI PLGVTVQGDV LIVIYHARST
660 670 680 690 700
LGGRLQAKMA SMKMFQIQFH TGFVPRNATT VKFAKYDLDA CDIQEKYPDL
710 720 730 740 750
FQVNLEVEVE PRDRPSREAP PWENSSMRGL NPKILFSSRE EQQDILSKFG
760 770 780 790 800
KPELPRQPGS TAQYDAGAGS PEAEPTDSDS PPSSSADASR FLHTLDWQEE
810 820 830 840 850
KEAETGAENA SSKESESALM EDRDESEVSD EGGSPISSEG QEPRADPEPP
860 870 880 890 900
GLAAGLVQQD LVFEVETPAV LPEPVPQEDG VDLLGLHSEV GAGPAVPPQA
910 920 930 940 950
CKAPSSNTDL LSCLLGPPEA ASQGPPEDLL SEDPLLLASP APPLSVQSTP
960 970 980 990 1000
RGGPPAAADP FGPLLPSSGN NSQPCSNPDL FGEFLNSDSV TVPPSFPSAH
1010 1020 1030 1040 1050
SAPPPSCSAD FLHLGDLPGE PSKMTASSSN PDLLGGWAAW TETAASAVAP
1060 1070 1080 1090 1100
TPATEGPLFS PGGQPAPCGS QASWTKSQNP DPFADLGDLS SGLQGSPAGF
1110 1120 1130 1140 1150
PPGGFIPKTA TTPKGSSSWQ TSRPPAQGAS WPPQAKPPPK ACTQPRPNYA
1160 1170 1180 1190 1200
SNFSVIGARE ERGVRAPSFA QKPKVSENDF EDLLSNQGFS SRSDKKGPKT
1210 1220 1230 1240 1250
IAEMRKQDLA KDTDPLKLKL LDWIEGKERN IRALLSTLHT VLWDGESRWT
1260 1270 1280 1290 1300
PVGMADLVAP EQVKKHYRRA VLAVHPDKAA GQPYEQHAKM IFMELNDAWS
1310
EFENQGSRPL F
Length:1,311
Mass (Da):143,191
Last modified:August 29, 2001 - v2
Checksum:i0ACE45DF57A5F981
GO
Isoform 2 (identifier: O14976-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-127: Missing.

Note: No experimental confirmation available.

Show »
Length:1,232
Mass (Da):134,464
Checksum:i483EE5F6B8416FDB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti607 – 6071R → C in AAH85005. (PubMed:15489334)Curated
Sequence conflicti1113 – 11131P → A in BAA22623. (PubMed:9299234)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441S → L.1 Publication
VAR_040505
Natural varianti580 – 5801V → M.1 Publication
Corresponds to variant rs34255232 [ dbSNP | Ensembl ].
VAR_040506
Natural varianti787 – 7871D → Y.1 Publication
Corresponds to variant rs34585705 [ dbSNP | Ensembl ].
VAR_040507
Natural varianti877 – 8771Q → R.1 Publication
Corresponds to variant rs149842313 [ dbSNP | Ensembl ].
VAR_040508
Natural varianti962 – 9621G → D in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_040509
Natural varianti1051 – 10511T → M.1 Publication
Corresponds to variant rs35227944 [ dbSNP | Ensembl ].
VAR_040510
Natural varianti1120 – 11201Q → H.1 Publication
Corresponds to variant rs55801437 [ dbSNP | Ensembl ].
VAR_040511
Natural varianti1137 – 11371P → L.1 Publication
Corresponds to variant rs56169884 [ dbSNP | Ensembl ].
VAR_040512
Natural varianti1168 – 11681S → N.1 Publication
Corresponds to variant rs56326341 [ dbSNP | Ensembl ].
VAR_040513
Natural varianti1265 – 12651K → R.1 Publication
Corresponds to variant rs2306242 [ dbSNP | Ensembl ].
VAR_040514
Natural varianti1297 – 12971D → N.1 Publication
Corresponds to variant rs1134921 [ dbSNP | Ensembl ].
VAR_040515

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 12779Missing in isoform 2. 1 PublicationVSP_054479Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88435 mRNA. Translation: BAA22623.1.
BC000816 mRNA. Translation: AAH00816.1.
BC008668 mRNA. Translation: AAH08668.1.
BC085005 mRNA. Translation: AAH85005.1.
CCDSiCCDS3340.1. [O14976-1]
RefSeqiNP_001273762.1. NM_001286833.1.
NP_005246.2. NM_005255.2. [O14976-1]
UniGeneiHs.369607.

Genome annotation databases

EnsembliENST00000314167; ENSP00000314499; ENSG00000178950. [O14976-1]
ENST00000511163; ENSP00000421361; ENSG00000178950. [O14976-2]
GeneIDi2580.
KEGGihsa:2580.
UCSCiuc003gbm.4. human. [O14976-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88435 mRNA. Translation: BAA22623.1 .
BC000816 mRNA. Translation: AAH00816.1 .
BC008668 mRNA. Translation: AAH08668.1 .
BC085005 mRNA. Translation: AAH85005.1 .
CCDSi CCDS3340.1. [O14976-1 ]
RefSeqi NP_001273762.1. NM_001286833.1.
NP_005246.2. NM_005255.2. [O14976-1 ]
UniGenei Hs.369607.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4C57 X-ray 2.55 A/B 14-351 [» ]
4C58 X-ray 2.16 A 27-351 [» ]
4C59 X-ray 2.80 A 14-351 [» ]
4O38 X-ray 2.10 A/B 12-347 [» ]
ProteinModelPortali O14976.
SMRi O14976. Positions 25-334, 400-746, 1139-1311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108853. 13 interactions.
IntActi O14976. 10 interactions.
MINTi MINT-5000432.
STRINGi 9606.ENSP00000314499.

Chemistry

BindingDBi O14976.
ChEMBLi CHEMBL4355.
GuidetoPHARMACOLOGYi 2027.

PTM databases

PhosphoSitei O14976.

Proteomic databases

MaxQBi O14976.
PaxDbi O14976.
PRIDEi O14976.

Protocols and materials databases

DNASUi 2580.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314167 ; ENSP00000314499 ; ENSG00000178950 . [O14976-1 ]
ENST00000511163 ; ENSP00000421361 ; ENSG00000178950 . [O14976-2 ]
GeneIDi 2580.
KEGGi hsa:2580.
UCSCi uc003gbm.4. human. [O14976-1 ]

Organism-specific databases

CTDi 2580.
GeneCardsi GC04M000832.
H-InvDB HIX0004007.
HGNCi HGNC:4113. GAK.
HPAi HPA027405.
HPA027459.
HPA027463.
MIMi 602052. gene.
neXtProti NX_O14976.
PharmGKBi PA28528.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119113.
HOGENOMi HOG000034235.
HOVERGENi HBG004322.
InParanoidi O14976.
KOi K08855.
OMAi YMCDMMA.
OrthoDBi EOG7WT40V.
PhylomeDBi O14976.
TreeFami TF105165.

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinki O14976.

Miscellaneous databases

ChiTaRSi GAK. human.
GeneWikii GAK_(protein).
GenomeRNAii 2580.
NextBioi 10201.
PROi O14976.
SOURCEi Search...

Gene expression databases

Bgeei O14976.
CleanExi HS_GAK.
ExpressionAtlasi O14976. baseline and differential.
Genevestigatori O14976.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR000008. C2_dom.
IPR001623. DnaJ_domain.
IPR011009. Kinase-like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
[Graphical view ]
Pfami PF00226. DnaJ. 1 hit.
PF00069. Pkinase. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view ]
SMARTi SM00271. DnaJ. 1 hit.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51182. C2_TENSIN. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, expression, and chromosomal localization of human GAK."
    Kimura S.H., Tsuruga H., Yabuta N., Endo Y., Nojima H.
    Genomics 44:179-187(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Fibroblast.
  2. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 981-1311 (ISOFORM 1).
    Tissue: Ovary and Placenta.
  3. "Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells."
    Greener T., Zhao X., Nojima H., Eisenberg E., Greene L.E.
    J. Biol. Chem. 275:1365-1370(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-456; SER-770; SER-826; SER-829; SER-834 AND SER-1096, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826; SER-829 AND SER-834, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-826; SER-829; SER-834; SER-939; SER-1176 AND SER-1185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "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-826 AND SER-829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of the human cyclin G associated kinase (GAK)."
    Midwest center for structural genomics (MCSG)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-347.
  12. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-144; MET-580; TYR-787; ARG-877; ASP-962; MET-1051; HIS-1120; LEU-1137; ASN-1168; ARG-1265 AND ASN-1297.

Entry informationi

Entry nameiGAK_HUMAN
AccessioniPrimary (citable) accession number: O14976
Secondary accession number(s): Q5U4P5, Q9BVY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: October 29, 2014
This is version 146 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 4
    Human chromosome 4: 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
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3