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Q8N4C8 (MINK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Misshapen-like kinase 1

EC=2.7.11.1
Alternative name(s):
GCK family kinase MiNK
MAPK/ERK kinase kinase kinase 6
Short name=MEK kinase kinase 6
Short name=MEKKK 6
Misshapen/NIK-related kinase
Mitogen-activated protein kinase kinase kinase kinase 6
Gene names
Name:MINK1
Synonyms:B55, MAP4K6, MINK, YSK2, ZC3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1332 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine kinase which acts as a negative regulator of Ras-related Rap2-mediated signal transduction to control neuronal structure and AMPA receptor trafficking. Required for normal synaptic density, dendrite complexity, as well as surface AMPA receptor expression in hippocampal neurons. Can activate the JNK and MAPK14/p38 pathways and mediates stimulation of the stress-activated protein kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway. Phosphorylates: TANC1 upon stimulation by RAP2A, MBP and SMAD1. Has an essential function in negative selection of thymocytes, perhaps by coupling NCK1 to activation of JNK1. Ref.2 Ref.7 Ref.9 Ref.18

Isoform 4 can activate the JNK pathway. Involved in the regulation of actin cytoskeleton reorganization, cell-matrix adhesion, cell-cell adhesion and cell migration. Ref.2 Ref.7 Ref.9 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q9JM52

Cofactor

Magnesium By similarity. UniProtKB Q9JM52

Subunit structure

Interacts with TANC1 By similarity. Interacts with RAP2A. Isoform 4 interacts with NCK1. Ref.2 Ref.9

Subcellular location

Cytoplasm. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell projectionaxon By similarity. Cell projectiondendrite By similarity Ref.2 Ref.9.

Isoform 4: Golgi apparatus Ref.2 Ref.9.

Tissue specificity

Expressed in the brain, isoform 2 is more abundant than isoform 1. Isoform 3 is ubiquitously expressed. Isoform 1 is most abundant in the skeletal muscle. Isoform 4 is ubiquitously expressed with relative high levels in brain, skeletal muscle, pancreas and testis. Ref.1 Ref.2

Induction

Activated after Ras induction via a mechanism involving reactive oxygen species. Ref.7

Post-translational modification

Autophosphorylated. Ref.2

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 CNH domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Golgi apparatus
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Traceable author statement Ref.1. Source: ProtInc

actin cytoskeleton reorganization

Inferred from mutant phenotype Ref.2. Source: UniProtKB

dendrite morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

multicellular organismal development

Inferred from sequence or structural similarity. Source: UniProtKB

negative thymic T cell selection

Inferred from electronic annotation. Source: Ensembl

positive regulation of JNK cascade

Inferred from mutant phenotype Ref.2. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.2. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell migration

Inferred from mutant phenotype Ref.2. Source: UniProtKB

regulation of cell-cell adhesion

Inferred from mutant phenotype Ref.2. Source: UniProtKB

regulation of cell-matrix adhesion

Inferred from mutant phenotype Ref.2. Source: UniProtKB

response to stress

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic transmission

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.2. Source: UniProtKB

axon

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.9Ref.18. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

small GTPase regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 Ref.1 (identifier: Q8N4C8-1)

Also known as: MINK-alpha;

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.
Isoform 1 Ref.1 (identifier: Q8N4C8-2)

Also known as: MiNK-1; MINK-delta;

The sequence of this isoform differs from the canonical sequence as follows:
     696-732: Missing.
Isoform 2 Ref.1 (identifier: Q8N4C8-3)

Also known as: MiNK-2; MINK-gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     696-732: Missing.
     800-800: A → ASYKRAIGE
Isoform 4 (identifier: Q8N4C8-4)

Also known as: MINK-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     581-600: Missing.
Isoform 5 (identifier: Q8N4C8-5)

Also known as: MINK-eta;

The sequence of this isoform differs from the canonical sequence as follows:
     581-600: Missing.
     696-732: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13321332Misshapen-like kinase 1
PRO_0000086329

Regions

Domain25 – 289265Protein kinase
Domain1019 – 1306288CNH
Nucleotide binding31 – 399ATP By similarity UniProtKB O00506
Region866 – 1332467Mediates interaction with RAP2A
Compositional bias359 – 495137Gln-rich
Compositional bias542 – 729188Pro-rich

Sites

Active site1531Proton acceptor By similarity UniProtKB O00506
Binding site541ATP By similarity UniProtKB O00506

Amino acid modifications

Modified residue6411Phosphoserine Ref.12
Modified residue7631Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.19
Modified residue7771Phosphoserine Ref.13
Modified residue7781Phosphoserine Ref.13 Ref.15
Modified residue7821Phosphoserine Ref.12 Ref.13

Natural variations

Alternative sequence581 – 60020Missing in isoform 4 and isoform 5.
VSP_041871
Alternative sequence696 – 73237Missing in isoform 1, isoform 2 and isoform 5. Ref.1
VSP_007059
Alternative sequence8001A → ASYKRAIGE in isoform 2. Ref.1
VSP_007060
Natural variant5141A → T. Ref.20
Corresponds to variant rs56131206 [ dbSNP | Ensembl ].
VAR_040799
Natural variant7711V → A. Ref.2 Ref.6
Corresponds to variant rs11556634 [ dbSNP | Ensembl ].
VAR_046058
Natural variant7751P → L. Ref.2 Ref.6 Ref.12 Ref.13 Ref.14 Ref.15 Ref.21
Corresponds to variant rs11556635 [ dbSNP | Ensembl ].
VAR_046059
Natural variant8631V → I. Ref.20
Corresponds to variant rs2302319 [ dbSNP | Ensembl ].
VAR_046060
Natural variant10101E → V in a gastric adenocarcinoma sample; somatic mutation. Ref.20
VAR_046061
Natural variant12001I → V. Ref.20
VAR_040800

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (MINK-alpha) [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 3E3B182CDDB3659C

FASTA1,332149,822
        10         20         30         40         50         60 
MGDPAPARSL DDIDLSALRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE 

        70         80         90        100        110        120 
DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKSPPGNDDQ LWLVMEFCGA GSVTDLVKNT 

       130        140        150        160        170        180 
KGNALKEDCI AYICREILRG LAHLHAHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR 

       190        200        210        220        230        240 
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDIWSLG ITAIEMAEGA PPLCDMHPMR 

       250        260        270        280        290        300 
ALFLIPRNPP PRLKSKKWSK KFIDFIDTCL IKTYLSRPPT EQLLKFPFIR DQPTERQVRI 

       310        320        330        340        350        360 
QLKDHIDRSR KKRGEKEETE YEYSGSEEED DSHGEEGEPS SIMNVPGEST LRREFLRLQQ 

       370        380        390        400        410        420 
ENKSNSEALK QQQQLQQQQQ RDPEAHIKHL LHQRQRRIEE QKEERRRVEE QQRREREQRK 

       430        440        450        460        470        480 
LQEKEQQRRL EDMQALRREE ERRQAEREQE YKRKQLEEQR QSERLQRQLQ QEHAYLKSLQ 

       490        500        510        520        530        540 
QQQQQQQLQK QQQQQLLPGD RKPLYHYGRG MNPADKPAWA REVEERTRMN KQQNSPLAKS 

       550        560        570        580        590        600 
KPGSTGPEPP IPQASPGPPG PLSQTPPMQR PVEPQEGPHK SLVAHRVPLK PYAAPVPRSQ 

       610        620        630        640        650        660 
SLQDQPTRNL AAFPASHDPD PAIPAPTATP SARGAVIRQN SDPTSEGPGP SPNPPAWVRP 

       670        680        690        700        710        720 
DNEAPPKVPQ RTSSIATALN TSGAGGSRPA QAVRARPRSN SAWQIYLQRR AERGTPKPPG 

       730        740        750        760        770        780 
PPAQPPGPPN ASSNPDLRRS DPGWERSDSV LPASHGHLPQ AGSLERNRVG VSSKPDSSPV 

       790        800        810        820        830        840 
LSPGNKAKPD DHRSRPGRPA DFVLLKERTL DEAPRPPKKA MDYSSSSEEV ESSEDDEEEG 

       850        860        870        880        890        900 
EGGPAEGSRD TPGGRSDGDT DSVSTMVVHD VEEITGTQPP YGGGTMVVQR TPEEERNLLH 

       910        920        930        940        950        960 
ADSNGYTNLP DVVQPSHSPT ENSKGQSPPS KDGSGDYQSR GLVKAPGKSS FTMFVDLGIY 

       970        980        990       1000       1010       1020 
QPGGSGDSIP ITALVGGEGT RLDQLQYDVR KGSVVNVNPT NTRAHSETPE IRKYKKRFNS 

      1030       1040       1050       1060       1070       1080 
EILCAALWGV NLLVGTENGL MLLDRSGQGK VYGLIGRRRF QQMDVLEGLN LLITISGKRN 

      1090       1100       1110       1120       1130       1140 
KLRVYYLSWL RNKILHNDPE VEKKQGWTTV GDMEGCGHYR VVKYERIKFL VIALKSSVEV 

      1150       1160       1170       1180       1190       1200 
YAWAPKPYHK FMAFKSFADL PHRPLLVDLT VEEGQRLKVI YGSSAGFHAV DVDSGNSYDI 

      1210       1220       1230       1240       1250       1260 
YIPVHIQSQI TPHAIIFLPN TDGMEMLLCY EDEGVYVNTY GRIIKDVVLQ WGEMPTSVAY 

      1270       1280       1290       1300       1310       1320 
ICSNQIMGWG EKAIEIRSVE TGHLDGVFMH KRAQRLKFLC ERNDKVFFAS VRSGGSSQVY 

      1330 
FMTLNRNCIM NW 

« Hide

Isoform 1 (MiNK-1) (MINK-delta) [UniParc].

Checksum: 029AD8C2806C90EE
Show »

FASTA1,295145,806
Isoform 2 (MiNK-2) (MINK-gamma) [UniParc].

Checksum: FD65470BFC6981B2
Show »

FASTA1,303146,711
Isoform 4 (MINK-beta) [UniParc].

Checksum: B8D157A582DA5D18
Show »

FASTA1,312147,653
Isoform 5 (MINK-eta) [UniParc].

Checksum: 4E992F63A486A95A
Show »

FASTA1,275143,637

References

« Hide 'large scale' references
[1]"Molecular cloning of MINK, a novel member of mammalian GCK family kinases, which is up-regulated during postnatal mouse cerebral development."
Dan I., Watanabe N.M., Kobayashi T., Yamashita-Suzuki K., Fukagaya Y., Kajikawa E., Kimura W.K., Nakashima T.M., Matsumoto K., Ninomiya-Tsuji J., Kusumi A.
FEBS Lett. 469:19-23(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[2]"Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta."
Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y., Daniel-Issakani S., Payan D.G., Xu X.
J. Biol. Chem. 279:54387-54397(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCK1, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AUTOPHOSPHORYLATION, VARIANTS ALA-771 AND LEU-775.
[3]Erratum
Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y., Daniel-Issakani S., Payan D.G., Xu X.
J. Biol. Chem. 280:5128-5128(2005)
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 3), VARIANTS ALA-771 AND LEU-775.
Tissue: Lymph.
[7]"Involvement of MINK, a Ste20 family kinase, in Ras oncogene-induced growth arrest in human ovarian surface epithelial cells."
Nicke B., Bastien J., Khanna S.J., Warne P.H., Cowling V., Cook S.J., Peters G., Delpuech O., Schulze A., Berns K., Mullenders J., Beijersbergen R.L., Bernards R., Ganesan T.S., Downward J., Hancock D.C.
Mol. Cell 20:673-685(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[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-763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1."
Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K., Bayarjargal M., Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T., Kariya K.
Biochem. Biophys. Res. Commun. 377:573-578(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAP2A, SUBCELLULAR LOCATION.
[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-763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, 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-641; SER-763 AND SER-782, VARIANT [LARGE SCALE ANALYSIS] LEU-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763; SER-777; SER-778 AND SER-782, VARIANT [LARGE SCALE ANALYSIS] LEU-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, VARIANT [LARGE SCALE ANALYSIS] LEU-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-778, VARIANT [LARGE SCALE ANALYSIS] LEU-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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-763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Smad inhibition by the Ste20 kinase Misshapen."
Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M., Kariya K., Mao J., Ip Y.T., Xu L.
Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"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-763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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. expand/collapse author list , 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] THR-514; ILE-863; VAL-1010 AND VAL-1200.
[21]"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: VARIANT [LARGE SCALE ANALYSIS] LEU-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB041926 mRNA. Translation: BAA94838.1.
AB035698 mRNA. Translation: BAA90753.1.
AY775058 mRNA. Translation: AAV41830.1.
AC233723 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90401.1.
CH471108 Genomic DNA. Translation: EAW90403.1.
CH471108 Genomic DNA. Translation: EAW90399.1.
CH471108 Genomic DNA. Translation: EAW90400.1.
CH471108 Genomic DNA. Translation: EAW90402.1.
BC034673 mRNA. Translation: AAH34673.1.
CCDSCCDS45588.1. [Q8N4C8-1]
CCDS45589.1. [Q8N4C8-3]
CCDS45590.1. [Q8N4C8-4]
RefSeqNP_001020108.1. NM_001024937.3. [Q8N4C8-4]
NP_056531.1. NM_015716.4. [Q8N4C8-2]
NP_722549.2. NM_153827.4. [Q8N4C8-1]
NP_733763.1. NM_170663.4. [Q8N4C8-3]
UniGeneHs.443417.

3D structure databases

ProteinModelPortalQ8N4C8.
SMRQ8N4C8. Positions 13-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119075. 5 interactions.
IntActQ8N4C8. 2 interactions.
STRING9606.ENSP00000347427.

Chemistry

ChEMBLCHEMBL5518.
GuidetoPHARMACOLOGY2103.

PTM databases

PhosphoSiteQ8N4C8.

Polymorphism databases

DMDM296437370.

Proteomic databases

MaxQBQ8N4C8.
PaxDbQ8N4C8.
PRIDEQ8N4C8.

Protocols and materials databases

DNASU50488.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347992; ENSP00000269296; ENSG00000141503. [Q8N4C8-3]
ENST00000355280; ENSP00000347427; ENSG00000141503. [Q8N4C8-1]
ENST00000453408; ENSP00000406487; ENSG00000141503. [Q8N4C8-4]
GeneID50488.
KEGGhsa:50488.
UCSCuc010vsk.2. human. [Q8N4C8-3]
uc010vsl.2. human. [Q8N4C8-1]
uc010vsm.2. human. [Q8N4C8-4]
uc010vsn.2. human. [Q8N4C8-2]

Organism-specific databases

CTD50488.
GeneCardsGC17P004736.
H-InvDBHIX0013452.
HGNCHGNC:17565. MINK1.
HPAHPA056296.
MIM609426. gene.
neXtProtNX_Q8N4C8.
PharmGKBPA134910641.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000290708.
HOVERGENHBG036506.
InParanoidQ8N4C8.
KOK04413.
OMAGTQTPYG.
OrthoDBEOG73803V.
PhylomeDBQ8N4C8.
TreeFamTF105138.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkQ8N4C8.

Gene expression databases

ArrayExpressQ8N4C8.
BgeeQ8N4C8.
CleanExHS_MINK1.
GenevestigatorQ8N4C8.

Family and domain databases

InterProIPR001180. 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]
PfamPF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00036. CNH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50219. CNH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMINK1. human.
GeneWikiMINK1.
GenomeRNAi50488.
NextBio53052.
PROQ8N4C8.
SOURCESearch...

Entry information

Entry nameMINK1_HUMAN
AccessionPrimary (citable) accession number: Q8N4C8
Secondary accession number(s): D3DTK3 expand/collapse secondary AC list , D3DTK4, Q5U8Z0, Q9P1X1, Q9P2R8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM