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O95819 (M4K4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase kinase kinase kinase 4

EC=2.7.11.1
Alternative name(s):
HPK/GCK-like kinase HGK
MAPK/ERK kinase kinase kinase 4
Short name=MEK kinase kinase 4
Short name=MEKKK 4
Nck-interacting kinase
Gene names
Name:MAP4K4
Synonyms:HGK, KIAA0687, NIK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1239 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine kinase that may play a role in the response to environmental stress and cytokines such as TNF-alpha. Appears to act upstream of the JUN N-terminal pathway. Phosphorylates SMAD1 on Thr-322. Ref.1 Ref.15

Catalytic activity

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

Cofactor

Magnesium. Ref.1

Subunit structure

Interacts with the SH3 domain of the adapter proteins Nck By similarity. Interacts (via its CNH regulatory domain) with ATL1 (via the N-terminal region). Interacts with RAP2A (GTP-bound form preferentially). Ref.6 Ref.7 UniProtKB P97820

Subcellular location

Cytoplasm Ref.7.

Tissue specificity

Appears to be ubiquitous. Expressed in all tissue types examined. Isoform 5 appears to be more abundant in the brain. Isoform 4 is predominant in the liver, skeletal muscle and placenta. Ref.1

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GBP3Q9H0R54EBI-2511133,EBI-2798916

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: O95819-1)

Also known as: Tumor-associated;

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 2 Ref.1 (identifier: O95819-2)

The sequence of this isoform differs from the canonical sequence as follows:
     495-525: Missing.
     740-740: A → AGEV
Isoform 3 Ref.1 (identifier: O95819-3)

The sequence of this isoform differs from the canonical sequence as follows:
     623-623: V → VQWSHLASLK...SDSDEVPPRV
     740-740: A → AGEV
Isoform 4 Ref.1 (identifier: O95819-4)

Also known as: HGK-S;

The sequence of this isoform differs from the canonical sequence as follows:
     495-525: Missing.
     569-622: Missing.
     740-740: A → AGEV
     1112-1112: H → HVRKNPHSM
Isoform 5 Ref.1 (identifier: O95819-5)

Also known as: HGK-L;

The sequence of this isoform differs from the canonical sequence as follows:
     495-525: Missing.
     569-622: Missing.
     623-623: V → VQWSHLASLK...SDSDEVPPRV
     740-740: A → AGEV
     1112-1112: H → HVRKNPHSM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 12391238Mitogen-activated protein kinase kinase kinase kinase 4
PRO_0000086280

Regions

Domain25 – 289265Protein kinase
Domain926 – 1213288CNH
Nucleotide binding31 – 399ATP By similarity UniProtKB O00506
Region858 – 1212355Mediates interaction with RAP2A

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.17
Modified residue51Phosphoserine Ref.11
Modified residue6291Phosphoserine Ref.10 Ref.16
Modified residue6311Phosphoserine Ref.10 Ref.16
Modified residue6391Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.16
Modified residue6441Phosphoserine Ref.9 Ref.11
Modified residue7121Phosphoserine Ref.9
Modified residue8001Phosphoserine Ref.12
Modified residue8051Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Modified residue9001Phosphoserine Ref.11

Natural variations

Alternative sequence495 – 52531Missing in isoform 2, isoform 4 and isoform 5. Ref.1
VSP_007054
Alternative sequence569 – 62254Missing in isoform 4 and isoform 5. Ref.1
VSP_007055
Alternative sequence6231V → VQWSHLASLKNNVSPVSRSH SFSDPSPKFAHHHLRSQDPC PPSRSEVLSQSSDSKSEAPD PTQKAWSRSDSDEVPPRV in isoform 3 and isoform 5. Ref.1
VSP_007056
Alternative sequence7401A → AGEV in isoform 2, isoform 3, isoform 4 and isoform 5. Ref.1
VSP_007057
Alternative sequence11121H → HVRKNPHSM in isoform 4 and isoform 5. Ref.1
VSP_007058
Natural variant7121S → T. Ref.18
VAR_040746
Isoform 3:
Natural variant6821D → V.

Experimental info

Sequence conflict6581S → SS Ref.3
Sequence conflict6581S → SS Ref.4
Sequence conflict8391Q → R in AAO32626. Ref.2

Secondary structure

................................................ 1239
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Tumor-associated) [UniParc].

Last modified March 28, 2003. Version 2.
Checksum: 8FBBE2F9ABEEC757

FASTA1,239142,101
        10         20         30         40         50         60 
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE 

        70         80         90        100        110        120 
DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT 

       130        140        150        160        170        180 
KGNTLKEDWI AYISREILRG LAHLHIHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR 

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

       250        260        270        280        290        300 
ALFLIPRNPP PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI 

       310        320        330        340        350        360 
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES TLRRDFLRLQ 

       370        380        390        400        410        420 
QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE QQKEQRRRLE EQQRREREAR 

       430        440        450        460        470        480 
RQQEREQRRR EQEEKRRLEE LERRRKEEEE RRRAEEEKRR VEREQEYIRR QLEEEQRHLE 

       490        500        510        520        530        540 
VLQQQLLQEQ AMLLECRWRE MEEHRQAERL QRQLQQEQAY LLSLQHDHRR PHPQHSQQPP 

       550        560        570        580        590        600 
PPQQERSKPS FHAPEPKAHY EPADRAREVE DRFRKTNHSS PEAQSKQTGR VLEPPVPSRS 

       610        620        630        640        650        660 
ESFSNGNSES VHPALQRPAE PQVPVRTTSR SPVLSRRDSP LQGSGQQNSQ AGQRNSTSIE 

       670        680        690        700        710        720 
PRLLWERVEK LVPRPGSGSS SGSSNSGSQP GSHPGSQSGS GERFRVRSSS KSEGSPSQRL 

       730        740        750        760        770        780 
ENAVKKPEDK KEVFRPLKPA DLTALAKELR AVEDVRPPHK VTDYSSSSEE SGTTDEEDDD 

       790        800        810        820        830        840 
VEQEGADEST SGPEDTRAAS SLNLSNGETE SVKTMIVHDD VESEPAMTPS KEGTLIVRQT 

       850        860        870        880        890        900 
QSASSTLQKH KSSSSFTPFI DPRLLQISPS SGTTVTSVVG FSCDGMRPEA IRQDPTRKGS 

       910        920        930        940        950        960 
VVNVNPTNTR PQSDTPEIRK YKKRFNSEIL CAALWGVNLL VGTESGLMLL DRSGQGKVYP 

       970        980        990       1000       1010       1020 
LINRRRFQQM DVLEGLNVLV TISGKKDKLR VYYLSWLRNK ILHNDPEVEK KQGWTTVGDL 

      1030       1040       1050       1060       1070       1080 
EGCVHYKVVK YERIKFLVIA LKSSVEVYAW APKPYHKFMA FKSFGELVHK PLLVDLTVEE 

      1090       1100       1110       1120       1130       1140 
GQRLKVIYGS CAGFHAVDVD SGSVYDIYLP THIQCSIKPH AIIILPNTDG MELLVCYEDE 

      1150       1160       1170       1180       1190       1200 
GVYVNTYGRI TKDVVLQWGE MPTSVAYIRS NQTMGWGEKA IEIRSVETGH LDGVFMHKRA 

      1210       1220       1230 
QRLKFLCERN DKVFFASVRS GGSSQVYFMT LGRTSLLSW 

« Hide

Isoform 2 [UniParc].

Checksum: FD4A41765D9719F7
Show »

FASTA1,211138,418
Isoform 3 [UniParc].

Checksum: 6DCBFA9AB27A8AD9
Show »

FASTA1,319150,913
Isoform 4 (HGK-S) [UniParc].

Checksum: 03D9E1A3D7F9415D
Show »

FASTA1,165133,401
Isoform 5 (HGK-L) [UniParc].

Checksum: AF0219B2CA816B5B
Show »

FASTA1,242141,929

References

« Hide 'large scale' references
[1]"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
Tissue: Macrophage.
[2]"The STE20 kinase HGK is broadly expressed in human tumor cells and can modulate cellular transformation, invasion, and adhesion."
Wright J.H., Wang X., Manning G., LaMere B.J., Le P., Zhu S., Khatry D., Flanagan P.M., Buckley S.D., Whyte D.B., Howlett A.R., Bischoff J.R., Lipson K.E., Jallal B.
Mol. Cell. Biol. 23:2068-2082(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Glioblastoma.
[3]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1239 (ISOFORM 2).
Tissue: Brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-1239 (ISOFORM 3).
Tissue: Testis.
[5]"Isolation, expression profile and chromosome assignment of a novel serine/threonine kinase gene."
Saito T., Seki N., Hori T.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 700-1239.
Tissue: Brain.
[6]"A novel GTP-binding protein hGBP3 interacts with NIK/HGK."
Luan Z., Zhang Y., Liu A., Man Y., Cheng L., Hu G.
FEBS Lett. 530:233-238(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATL1.
[7]"Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase."
Machida N., Umikawa M., Takei K., Sakima N., Myagmar B.E., Taira K., Uezato H., Ogawa Y., Kariya K.
J. Biol. Chem. 279:15711-15714(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAP2A, SUBCELLULAR LOCATION.
[8]"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-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-639; SER-644; SER-712 AND SER-805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-629; SER-631; SER-639 AND SER-805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-639; SER-644; SER-805 AND SER-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"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-800 AND SER-805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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.
[16]"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-629; SER-631 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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: VARIANT [LARGE SCALE ANALYSIS] THR-712, VARIANT [LARGE SCALE ANALYSIS] VAL-682 (ISOFORM 3).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF096300 mRNA. Translation: AAD16137.1.
AY212247 mRNA. Translation: AAO32626.1.
AB014587 mRNA. Translation: BAA31662.1.
AL137755 mRNA. Translation: CAB70907.2.
AB013385 mRNA. Translation: BAA33714.1.
CCDSCCDS56130.1. [O95819-1]
PIRT46481.
RefSeqNP_001229488.1. NM_001242559.1. [O95819-1]
NP_004825.3. NM_004834.4. [O95819-4]
NP_663720.1. NM_145687.3.
UniGeneHs.701013.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4OBOX-ray2.10A/B2-328[»]
4OBPX-ray2.27A/B2-328[»]
4OBQX-ray2.19A/B2-328[»]
ProteinModelPortalO95819.
SMRO95819. Positions 13-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114838. 22 interactions.
IntActO95819. 17 interactions.
MINTMINT-1172114.
STRING9606.ENSP00000313644.

Chemistry

BindingDBO95819.
ChEMBLCHEMBL6166.
GuidetoPHARMACOLOGY2088.

PTM databases

PhosphoSiteO95819.

Proteomic databases

MaxQBO95819.
PaxDbO95819.
PRIDEO95819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347699; ENSP00000314363; ENSG00000071054. [O95819-1]
GeneID9448.
KEGGhsa:9448.
UCSCuc002tbc.3. human. [O95819-3]
uc002tbd.3. human. [O95819-2]
uc002tbg.3. human. [O95819-1]
uc002tbh.3. human. [O95819-4]

Organism-specific databases

CTD9448.
GeneCardsGC02P102313.
HGNCHGNC:6866. MAP4K4.
HPAHPA008476.
MIM604666. gene.
neXtProtNX_O95819.
PharmGKBPA30612.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000290708.
HOVERGENHBG036506.
KOK04407.
PhylomeDBO95819.
TreeFamTF105138.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkO95819.

Gene expression databases

ArrayExpressO95819.
BgeeO95819.
CleanExHS_MAP4K4.
GenevestigatorO95819.

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

ChiTaRSMAP4K4. human.
GeneWikiMAP4K4.
GenomeRNAi9448.
NextBio35392.
PROO95819.
SOURCESearch...

Entry information

Entry nameM4K4_HUMAN
AccessionPrimary (citable) accession number: O95819
Secondary accession number(s): O75172, Q9NST7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: July 9, 2014
This is version 143 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 2

Human chromosome 2: entries, gene names and cross-references to MIM