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Q9UKE5

- TNIK_HUMAN

UniProt

Q9UKE5 - TNIK_HUMAN

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Protein

TRAF2 and NCK-interacting protein kinase

Gene
TNIK, KIAA0551
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATP By similarityBy similarity
Active sitei153 – 1531Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. receptor signaling protein serine/threonine kinase activity Source: RefGenome
  5. small GTPase regulator activity Source: InterPro

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. activation of JNKK activity Source: UniProtKB
  3. cytoskeleton organization Source: UniProtKB
  4. intracellular signal transduction Source: UniProtKB
  5. protein autophosphorylation Source: UniProtKB
  6. protein phosphorylation Source: UniProtKB
  7. regulation of dendrite morphogenesis Source: UniProtKB
  8. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Neurogenesis, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
SignaLinkiQ9UKE5.

Names & Taxonomyi

Protein namesi
Recommended name:
TRAF2 and NCK-interacting protein kinase (EC:2.7.11.1)
Gene namesi
Name:TNIK
Synonyms:KIAA0551
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:30765. TNIK.

Subcellular locationi

Nucleus. Cytoplasm. Recycling endosome. Cytoplasmcytoskeleton
Note: Associated with recycling endosomes and the cytoskeletal fraction upon RAP2A overexpression.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProtKB
  5. recycling endosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541K → A: Kinase dead. Loss of autophosphorylation and loss of function in cytoskeleton regulation. 2 Publications
Mutagenesisi152 – 1532RD → AA: Loss of autophosphorylation.
Mutagenesisi171 – 1722DF → AA: Loss of autophosphorylation.

Organism-specific databases

PharmGKBiPA134893180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13601360TRAF2 and NCK-interacting protein kinasePRO_0000086761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei326 – 3261Phosphoserine1 Publication
Modified residuei560 – 5601Phosphoserine1 Publication
Modified residuei640 – 6401Phosphoserine4 Publications
Modified residuei678 – 6781Phosphoserine1 Publication
Modified residuei680 – 6801Phosphoserine1 Publication
Modified residuei688 – 6881Phosphoserine3 Publications
Modified residuei707 – 7071Phosphoserine1 Publication
Modified residuei720 – 7201Phosphoserine2 Publications
Modified residuei766 – 7661Phosphoserine1 Publication
Modified residuei769 – 7691Phosphoserine5 Publications

Post-translational modificationi

Autophosphorylated. Autophosphorylation is activated by RAP2A and induces association to the cytoskeletal fraction.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UKE5.
PaxDbiQ9UKE5.
PRIDEiQ9UKE5.

PTM databases

PhosphoSiteiQ9UKE5.

Miscellaneous databases

PMAP-CutDBQ9UKE5.

Expressioni

Tissue specificityi

Expressed ubiquitously. Highest levels observed in heart, brain and skeletal muscle. Expressed in normal colonic epithelia and colorectal cancer tissues.2 Publications

Gene expression databases

ArrayExpressiQ9UKE5.
BgeeiQ9UKE5.
GenevestigatoriQ9UKE5.

Organism-specific databases

HPAiHPA012128.
HPA012297.

Interactioni

Subunit structurei

Interacts (via the CNH domain) with RAP2A (GTP-bound form preferentially); the interaction is direct and required for the activation of TNIK by RAP2A. Interacts with NEDD4; recruits RAP2A to NEDD4. Interacts with TRAF2 and NCK. Interacts with TCF7L2/TCF4 and CTNNB1; the interaction is direct. Interacts with TANC1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352223EBI-1051794,EBI-491549
Tanc1Q6F6B32EBI-1051794,EBI-2133582From a different organism.
TCF7L2Q9NQB03EBI-1051794,EBI-924724

Protein-protein interaction databases

BioGridi116682. 37 interactions.
DIPiDIP-37562N.
IntActiQ9UKE5. 21 interactions.
MINTiMINT-7242209.

Structurei

Secondary structure

1
1360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni22 – 243
Beta strandi25 – 3410
Beta strandi37 – 448
Turni45 – 473
Beta strandi50 – 578
Helixi64 – 7613
Beta strandi85 – 917
Beta strandi100 – 1067
Helixi113 – 1197
Helixi121 – 1233
Helixi127 – 14620
Beta strandi158 – 1614
Beta strandi167 – 1693
Turni173 – 1753
Helixi192 – 1943
Helixi197 – 2004
Helixi214 – 22815
Turni232 – 2354
Helixi238 – 24710
Helixi260 – 26910
Helixi274 – 2763
Helixi280 – 2845
Helixi287 – 2904
Helixi295 – 31117

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X7FX-ray2.80A/B/C/D/E1-325[»]
ProteinModelPortaliQ9UKE5.
SMRiQ9UKE5. Positions 13-313.

Miscellaneous databases

EvolutionaryTraceiQ9UKE5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 289265Protein kinaseAdd
BLAST
Domaini1047 – 1334288CNHAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 1047758Mediates interaction with NEDD4Add
BLAST

Sequence similaritiesi

Contains 1 CNH domain.

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG036506.
InParanoidiQ9UKE5.
KOiK08840.
OMAiTEQYNVG.
OrthoDBiEOG73803V.
PhylomeDBiQ9UKE5.
TreeFamiTF105138.

Family and domain databases

InterProiIPR001180. Citron.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00036. CNH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50219. CNH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UKE5-1) [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

MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL     50
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ 100
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI 150
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI 200
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA 250
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI 300
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL 350
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE 400
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYIRRQ 450
LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL EEQRQAERLQ RQLKQERDYL 500
VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEVEER SRLNRQSSPA 550
MPHKVANRIS DPNLPPRSES FSISGVQPAR TPPMLRPVDP QIPHLVAVKS 600
QGPALTASQS VHEQPTKGLS GFQEALNVTS HRVEMPRQNS DPTSENPPLP 650
TRIEKFDRSS WLRQEEDIPP KVPQRTTSIS PALARKNSPG NGSALGPRLG 700
SQPIRASNPD LRRTEPILES PLQRTSSGSS SSSSTPSSQP SSQGGSQPGS 750
QAGSSERTRV RANSKSEGSP VLPHEPAKVK PEESRDITRP SRPASYKKAI 800
DEDLTALAKE LRELRIEETN RPMKKVTDYS SSSEESESSE EEEEDGESET 850
HDGTVAVSDI PRLIPTGAPG SNEQYNVGMV GTHGLETSHA DSFSGSISRE 900
GTLMIRETSG EKKRSGHSDS NGFAGHINLP DLVQQSHSPA GTPTEGLGRV 950
STHSQEMDSG TEYGMGSSTK ASFTPFVDPR VYQTSPTDED EEDEESSAAA 1000
LFTSELLRQE QAKLNEARKI SVVNVNPTNI RPHSDTPEIR KYKKRFNSEI 1050
LCAALWGVNL LVGTENGLML LDRSGQGKVY NLINRRRFQQ MDVLEGLNVL 1100
VTISGKKNKL RVYYLSWLRN RILHNDPEVE KKQGWITVGD LEGCIHYKVV 1150
KYERIKFLVI ALKNAVEIYA WAPKPYHKFM AFKSFADLQH KPLLVDLTVE 1200
EGQRLKVIFG SHTGFHVIDV DSGNSYDIYI PSHIQGNITP HAIVILPKTD 1250
GMEMLVCYED EGVYVNTYGR ITKDVVLQWG EMPTSVAYIH SNQIMGWGEK 1300
AIEIRSVETG HLDGVFMHKR AQRLKFLCER NDKVFFASVR SGGSSQVFFM 1350
TLNRNSMMNW 1360
Length:1,360
Mass (Da):154,943
Last modified:May 1, 2000 - v1
Checksum:i3590BC2905A72C3D
GO
Isoform 2 (identifier: Q9UKE5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     445-473: Missing.

Show »
Length:1,331
Mass (Da):151,300
Checksum:i85378CBC98631411
GO
Isoform 3 (identifier: Q9UKE5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     537-591: Missing.

Show »
Length:1,305
Mass (Da):148,829
Checksum:i209230BB15712DFC
GO
Isoform 4 (identifier: Q9UKE5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     795-802: Missing.

Show »
Length:1,352
Mass (Da):154,008
Checksum:iF4708A71FF26C54F
GO
Isoform 5 (identifier: Q9UKE5-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     445-473: Missing.
     537-591: Missing.

Show »
Length:1,276
Mass (Da):145,186
Checksum:i9B85E462E4FAE9F0
GO
Isoform 6 (identifier: Q9UKE5-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     445-473: Missing.
     795-802: Missing.

Show »
Length:1,323
Mass (Da):150,365
Checksum:i93B2E73EF75034B9
GO
Isoform 7 (identifier: Q9UKE5-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     537-591: Missing.
     795-802: Missing.

Show »
Length:1,297
Mass (Da):147,894
Checksum:iEED944B571948D3F
GO
Isoform 8 (identifier: Q9UKE5-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     445-473: Missing.
     537-591: Missing.
     795-802: Missing.

Show »
Length:1,268
Mass (Da):144,251
Checksum:i55AD5F59B7A08A2A
GO

Sequence cautioni

The sequence BAA25477.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti778 – 7781K → E.1 Publication
Corresponds to variant rs55778284 [ dbSNP | Ensembl ].
VAR_041231
Natural varianti910 – 9101G → E.1 Publication
Corresponds to variant rs35090763 [ dbSNP | Ensembl ].
VAR_041232
Natural varianti999 – 9991A → T.1 Publication
Corresponds to variant rs17857452 [ dbSNP | Ensembl ].
VAR_041233

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei445 – 47329Missing in isoform 2, isoform 5, isoform 6 and isoform 8. 1 PublicationVSP_004889Add
BLAST
Alternative sequencei537 – 59155Missing in isoform 3, isoform 5, isoform 7 and isoform 8. 1 PublicationVSP_004890Add
BLAST
Alternative sequencei795 – 8028Missing in isoform 4, isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_004891

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF172264 mRNA. Translation: AAF03782.1.
AF172268 mRNA. Translation: AAF03786.1.
AF172267 mRNA. Translation: AAF03785.1.
AF172266 mRNA. Translation: AAF03784.1.
AF172265 mRNA. Translation: AAF03783.1.
AF172270 mRNA. Translation: AAF03788.1.
AF172271 mRNA. Translation: AAF03789.1.
AF172269 mRNA. Translation: AAF03787.1.
AB011123 mRNA. Translation: BAA25477.2. Different initiation.
AK291056 mRNA. Translation: BAF83745.1.
AC026315 Genomic DNA. No translation available.
AC078793 Genomic DNA. No translation available.
AC092919 Genomic DNA. No translation available.
AC137517 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78484.1.
CH471052 Genomic DNA. Translation: EAW78489.1.
CH471052 Genomic DNA. Translation: EAW78492.1.
CH471052 Genomic DNA. Translation: EAW78493.1.
BC019081 mRNA. Translation: AAH19081.2.
BC150256 mRNA. Translation: AAI50257.1.
CCDSiCCDS46956.1. [Q9UKE5-1]
CCDS54673.1. [Q9UKE5-8]
CCDS54674.1. [Q9UKE5-5]
CCDS54675.1. [Q9UKE5-6]
CCDS54676.1. [Q9UKE5-2]
CCDS54677.1. [Q9UKE5-7]
CCDS54678.1. [Q9UKE5-3]
CCDS54679.1. [Q9UKE5-4]
RefSeqiNP_001155032.1. NM_001161560.1. [Q9UKE5-4]
NP_001155033.1. NM_001161561.1. [Q9UKE5-2]
NP_001155034.1. NM_001161562.1. [Q9UKE5-6]
NP_001155035.1. NM_001161563.1. [Q9UKE5-3]
NP_001155036.1. NM_001161564.1. [Q9UKE5-7]
NP_001155037.1. NM_001161565.1. [Q9UKE5-5]
NP_001155038.1. NM_001161566.1. [Q9UKE5-8]
NP_055843.1. NM_015028.2. [Q9UKE5-1]
UniGeneiHs.34024.

Genome annotation databases

EnsembliENST00000284483; ENSP00000284483; ENSG00000154310. [Q9UKE5-4]
ENST00000341852; ENSP00000345352; ENSG00000154310. [Q9UKE5-5]
ENST00000357327; ENSP00000349880; ENSG00000154310. [Q9UKE5-2]
ENST00000436636; ENSP00000399511; ENSG00000154310. [Q9UKE5-1]
ENST00000460047; ENSP00000418916; ENSG00000154310. [Q9UKE5-7]
ENST00000470834; ENSP00000419990; ENSG00000154310. [Q9UKE5-6]
ENST00000475336; ENSP00000418156; ENSG00000154310. [Q9UKE5-8]
ENST00000488470; ENSP00000418378; ENSG00000154310. [Q9UKE5-3]
GeneIDi23043.
KEGGihsa:23043.
UCSCiuc003fhh.2. human. [Q9UKE5-1]
uc003fhi.2. human. [Q9UKE5-3]
uc003fhj.2. human. [Q9UKE5-2]
uc003fhk.2. human. [Q9UKE5-4]
uc003fhl.2. human. [Q9UKE5-5]
uc003fhm.2. human. [Q9UKE5-7]
uc003fhn.2. human. [Q9UKE5-6]
uc003fho.2. human. [Q9UKE5-8]

Polymorphism databases

DMDMi29840818.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF172264 mRNA. Translation: AAF03782.1 .
AF172268 mRNA. Translation: AAF03786.1 .
AF172267 mRNA. Translation: AAF03785.1 .
AF172266 mRNA. Translation: AAF03784.1 .
AF172265 mRNA. Translation: AAF03783.1 .
AF172270 mRNA. Translation: AAF03788.1 .
AF172271 mRNA. Translation: AAF03789.1 .
AF172269 mRNA. Translation: AAF03787.1 .
AB011123 mRNA. Translation: BAA25477.2 . Different initiation.
AK291056 mRNA. Translation: BAF83745.1 .
AC026315 Genomic DNA. No translation available.
AC078793 Genomic DNA. No translation available.
AC092919 Genomic DNA. No translation available.
AC137517 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78484.1 .
CH471052 Genomic DNA. Translation: EAW78489.1 .
CH471052 Genomic DNA. Translation: EAW78492.1 .
CH471052 Genomic DNA. Translation: EAW78493.1 .
BC019081 mRNA. Translation: AAH19081.2 .
BC150256 mRNA. Translation: AAI50257.1 .
CCDSi CCDS46956.1. [Q9UKE5-1 ]
CCDS54673.1. [Q9UKE5-8 ]
CCDS54674.1. [Q9UKE5-5 ]
CCDS54675.1. [Q9UKE5-6 ]
CCDS54676.1. [Q9UKE5-2 ]
CCDS54677.1. [Q9UKE5-7 ]
CCDS54678.1. [Q9UKE5-3 ]
CCDS54679.1. [Q9UKE5-4 ]
RefSeqi NP_001155032.1. NM_001161560.1. [Q9UKE5-4 ]
NP_001155033.1. NM_001161561.1. [Q9UKE5-2 ]
NP_001155034.1. NM_001161562.1. [Q9UKE5-6 ]
NP_001155035.1. NM_001161563.1. [Q9UKE5-3 ]
NP_001155036.1. NM_001161564.1. [Q9UKE5-7 ]
NP_001155037.1. NM_001161565.1. [Q9UKE5-5 ]
NP_001155038.1. NM_001161566.1. [Q9UKE5-8 ]
NP_055843.1. NM_015028.2. [Q9UKE5-1 ]
UniGenei Hs.34024.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2X7F X-ray 2.80 A/B/C/D/E 1-325 [» ]
ProteinModelPortali Q9UKE5.
SMRi Q9UKE5. Positions 13-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116682. 37 interactions.
DIPi DIP-37562N.
IntActi Q9UKE5. 21 interactions.
MINTi MINT-7242209.

Chemistry

BindingDBi Q9UKE5.
ChEMBLi CHEMBL4527.
GuidetoPHARMACOLOGYi 2244.

PTM databases

PhosphoSitei Q9UKE5.

Polymorphism databases

DMDMi 29840818.

Proteomic databases

MaxQBi Q9UKE5.
PaxDbi Q9UKE5.
PRIDEi Q9UKE5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284483 ; ENSP00000284483 ; ENSG00000154310 . [Q9UKE5-4 ]
ENST00000341852 ; ENSP00000345352 ; ENSG00000154310 . [Q9UKE5-5 ]
ENST00000357327 ; ENSP00000349880 ; ENSG00000154310 . [Q9UKE5-2 ]
ENST00000436636 ; ENSP00000399511 ; ENSG00000154310 . [Q9UKE5-1 ]
ENST00000460047 ; ENSP00000418916 ; ENSG00000154310 . [Q9UKE5-7 ]
ENST00000470834 ; ENSP00000419990 ; ENSG00000154310 . [Q9UKE5-6 ]
ENST00000475336 ; ENSP00000418156 ; ENSG00000154310 . [Q9UKE5-8 ]
ENST00000488470 ; ENSP00000418378 ; ENSG00000154310 . [Q9UKE5-3 ]
GeneIDi 23043.
KEGGi hsa:23043.
UCSCi uc003fhh.2. human. [Q9UKE5-1 ]
uc003fhi.2. human. [Q9UKE5-3 ]
uc003fhj.2. human. [Q9UKE5-2 ]
uc003fhk.2. human. [Q9UKE5-4 ]
uc003fhl.2. human. [Q9UKE5-5 ]
uc003fhm.2. human. [Q9UKE5-7 ]
uc003fhn.2. human. [Q9UKE5-6 ]
uc003fho.2. human. [Q9UKE5-8 ]

Organism-specific databases

CTDi 23043.
GeneCardsi GC03M170779.
HGNCi HGNC:30765. TNIK.
HPAi HPA012128.
HPA012297.
MIMi 610005. gene.
neXtProti NX_Q9UKE5.
PharmGKBi PA134893180.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG036506.
InParanoidi Q9UKE5.
KOi K08840.
OMAi TEQYNVG.
OrthoDBi EOG73803V.
PhylomeDBi Q9UKE5.
TreeFami TF105138.

Enzyme and pathway databases

Reactomei REACT_169436. Oxidative Stress Induced Senescence.
SignaLinki Q9UKE5.

Miscellaneous databases

EvolutionaryTracei Q9UKE5.
GeneWikii TNIK.
GenomeRNAii 23043.
NextBioi 44076.
PMAP-CutDB Q9UKE5.
PROi Q9UKE5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UKE5.
Bgeei Q9UKE5.
Genevestigatori Q9UKE5.

Family and domain databases

InterProi IPR001180. Citron.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00036. CNH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50219. CNH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton."
    Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.
    J. Biol. Chem. 274:30729-30737(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF2 AND NCK, AUTOPHOSPHORYLATION.
  2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "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] (ISOFORM 5).
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 1).
    Tissue: Placenta.
  8. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton."
    Taira K., Umikawa M., Takei K., Myagmar B.-E., Shinzato M., Machida N., Uezato H., Nonaka S., Kariya K.
    J. Biol. Chem. 279:49488-49496(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAP2A, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54.
  10. Cited for: INTERACTION WITH TANC1.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. "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-640; SER-688; SER-720 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678 AND SER-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. "The kinase TNIK is an essential activator of Wnt target genes."
    Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
    EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54; 152-ARG-ASP-153 AND 171-ASP-PHE-172, INTERACTION WITH TCF7L2 AND CTNNB1, TISSUE SPECIFICITY, FUNCTION.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560; SER-640; SER-688; SER-707; SER-720; SER-766 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: FUNCTION, INTERACTION WITH NEDD4 AND RAP2A.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: FUNCTION.
  21. "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-326; SER-640; SER-688 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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] GLU-778; GLU-910 AND THR-999.

Entry informationi

Entry nameiTNIK_HUMAN
AccessioniPrimary (citable) accession number: Q9UKE5
Secondary accession number(s): A7E2A3
, A8K4U1, D3DNQ6, O60298, Q8WUY7, Q9UKD8, Q9UKD9, Q9UKE0, Q9UKE1, Q9UKE2, Q9UKE3, Q9UKE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 139 of the entry and version 1 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. 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

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