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Reviewed, UniProtKB/Swiss-Prot Q99683 (M3K5_HUMAN)

Last modified February 9, 2010. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mitogen-activated protein kinase kinase kinase 5
    EC=2.7.11.25
Alternative name(s):
    MAPK/ERK kinase kinase 5
      Short name=MEK kinase 5
      Short name=MEKK 5
    Apoptosis signal-regulating kinase 1
      Short name=ASK-1
Gene names
Name: MAP3K5
Synonyms: ASK1, MAPKKK5, MEKK5
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1374 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of a protein kinase signal transduction cascade. Phosphorylates and activates MAP2K4 and MAP2K6, which in turn activate the JNK and p38 MAP kinases, respectively. Overexpression induces apoptotic cell death. Ref.1 Ref.2 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Contains an N-terminal autoinhibitory domain. Activated by phosphorylation at Thr-838, inhibited by phosphorylation at Ser-966 and Ser-1033. Binds to, and stabilizes MAP3K6 and is activated by MAP3K6 by phosphorylation on Thr-838. Ref.8 Ref.11 Ref.13

Subunit structure

Homodimer when inactive. Binds both upstream activators and downstream substrates in multimolecular complexes. Associates with and inhibited by HIV-1 Nef. Interacts with DAB2IP and PPM1L. Interacts with ARRB2. Ref.8 Ref.11 Ref.13 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.14 Ref.18

Tissue specificity

Abundantly expressed in heart and pancreas.

Induction

By TNF-alpha. Inhibited by HIV-1 Nef. Ref.8 Ref.11 Ref.13

Post-translational modification

Dephosphorylated and activated by PGAM5. Ref.8 Ref.11 Ref.13 Ref.18 Ref.15 Ref.16

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13741374Mitogen-activated protein kinase kinase kinase 5
PRO_0000086249

Regions

Domain680 – 938259Protein kinase
Nucleotide binding686 – 6949ATP By similarity

Sites

Active site8031Proton acceptor By similarity
Binding site7091ATP

Amino acid modifications

Modified residue8361Phosphothreonine
Modified residue8381Phosphothreonine Ref.8 Ref.13
Modified residue9581Phosphoserine
Modified residue9661Phosphoserine Ref.11
Modified residue9761Phosphothreonine
Modified residue9771Phosphoserine
Modified residue9781Phosphoserine
Modified residue9791Phosphoserine
Modified residue9841Phosphoserine
Modified residue9861Phosphoserine
Modified residue9891Phosphothreonine
Modified residue10291Phosphoserine Ref.15 Ref.16
Modified residue10331Phosphoserine Ref.11 Ref.15 Ref.16

Natural variations

Natural variant10061G → R: dbSNP rs45626535. Ref.19
VAR_040693
Natural variant12141I → T: dbSNP rs56379668. Ref.19
VAR_040694
Natural variant12501I → V: dbSNP rs35551087. Ref.19
VAR_040695
Natural variant13141T → I: dbSNP rs45599539. Ref.19
VAR_040696
Natural variant13151D → N: dbSNP rs41288957. Ref.19
VAR_040697

Experimental info

Mutagenesis7091K → M: Loss of kinase activity. Inhibits activation of JNK and apoptosis mediated by TNFRSF6 and DAXX. Ref.13 Ref.5
Mutagenesis7091K → R: Loss of kinase activity. Abolishes DAXX-mediated apoptosis. Ref.13 Ref.5
Mutagenesis9661S → A: Enhanced induction of apoptosis, increased kinase activity, and loss of YWHAG binding. Ref.11
Mutagenesis10331S → A: Enhanced induction of apoptosis and increased kinase activity. Ref.11

Secondary structure

............................ 1374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99683-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 265BDC65968AF985

FASTA1,374154,537
        10         20         30         40         50         60 
MSTEADEGIT FSVPPFAPSG FCTIPEGGIC RRGGAAAVGE GEEHQLPPPP PGSFWNVESA 

        70         80         90        100        110        120 
AAPGIGCPAA TSSSSATRGR GSSVGGGSRR TTVAYVINEA SQGQLVVAES EALQSLREAC 

       130        140        150        160        170        180 
ETVGATLETL HFGKLDFGET TVLDRFYNAD IAVVEMSDAF RQPSLFYHLG VRESFSMANN 

       190        200        210        220        230        240 
IILYCDTNSD SLQSLKEIIC QKNTMCTGNY TFVPYMITPH NKVYCCDSSF MKGLTELMQP 

       250        260        270        280        290        300 
NFELLLGPIC LPLVDRFIQL LKVAQASSSQ YFRESILNDI RKARNLYTGK ELAAELARIR 

       310        320        330        340        350        360 
QRVDNIEVLT ADIVINLLLS YRDIQDYDSI VKLVETLEKL PTFDLASHHH VKFHYAFALN 

       370        380        390        400        410        420 
RRNLPGDRAK ALDIMIPMVQ SEGQVASDMY CLVGRIYKDM FLDSNFTDTE SRDHGASWFK 

       430        440        450        460        470        480 
KAFESEPTLQ SGINYAVLLL AAGHQFESSF ELRKVGVKLS SLLGKKGNLE KLQSYWEVGF 

       490        500        510        520        530        540 
FLGASVLAND HMRVIQASEK LFKLKTPAWY LKSIVETILI YKHFVKLTTE QPVAKQELVD 

       550        560        570        580        590        600 
FWMDFLVEAT KTDVTVVRFP VLILEPTKIY QPSYLSINNE VEEKTISIWH VLPDDKKGIH 

       610        620        630        640        650        660 
EWNFSASSVR GVSISKFEER CCFLYVLHNS DDFQIYFCTE LHCKKFFEMV NTITEEKGRS 

       670        680        690        700        710        720 
TEEGDCESDL LEYDYEYDEN GDRVVLGKGT YGIVYAGRDL SNQVRIAIKE IPERDSRYSQ 

       730        740        750        760        770        780 
PLHEEIALHK HLKHKNIVQY LGSFSENGFI KIFMEQVPGG SLSALLRSKW GPLKDNEQTI 

       790        800        810        820        830        840 
GFYTKQILEG LKYLHDNQIV HRDIKGDNVL INTYSGVLKI SDFGTSKRLA GINPCTETFT 

       850        860        870        880        890        900 
GTLQYMAPEI IDKGPRGYGK AADIWSLGCT IIEMATGKPP FYELGEPQAA MFKVGMFKVH 

       910        920        930        940        950        960 
PEIPESMSAE AKAFILKCFE PDPDKRACAN DLLVDEFLKV SSKKKKTQPK LSALSAGSNE 

       970        980        990       1000       1010       1020 
YLRSISLPVP VLVEDTSSSS EYGSVSPDTE LKVDPFSFKT RAKSCGERDV KGIRTLFLGI 

      1030       1040       1050       1060       1070       1080 
PDENFEDHSA PPSPEEKDSG FFMLRKDSER RATLHRILTE DQDKIVRNLM ESLAQGAEEP 

      1090       1100       1110       1120       1130       1140 
KLKWEHITTL IASLREFVRS TDRKIIATTL SKLKLELDFD SHGISQVQVV LFGFQDAVNK 

      1150       1160       1170       1180       1190       1200 
VLRNHNIKPH WMFALDSIIR KAVQTAITIL VPELRPHFSL ASESDTADQE DLDVEDDHEE 

      1210       1220       1230       1240       1250       1260 
QPSNQTVRRP QAVIEDAVAT SGVSTLSSTV SHDSQSAHRS LNVQLGRMKI ETNRLLEELV 

      1270       1280       1290       1300       1310       1320 
RKEKELQALL HRAIEEKDQE IKHLKLKSQP IEIPELPVFH LNSSGTNTED SELTDWLRVN 

      1330       1340       1350       1360       1370 
GADEDTISRF LAEDYTLLDV LYYVTRDDLK CLRLRGGMLC TLWKAIIDFR NKQT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase."
Wang X.S., Diener K., Jannuzzi D., Trollinger D., Tan T.-H., Lichenstein H., Zukowski M., Yao Z.
J. Biol. Chem. 271:31607-31611(1996) [PubMed: 8940179] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways."
Ichijo H., Nishida E., Irie K., ten Dijke P., Saitoh M., Moriguchi T., Takagi M., Matsumoto K., Miyazono K., Gotoh Y.
Science 275:90-94(1997) [PubMed: 8974401] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Lung.
[5]"Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx."
Chang H.Y., Nishitoh H., Yang X., Ichijo H., Baltimore D.
Science 281:1860-1863(1998) [PubMed: 9743501] [Abstract]
Cited for: INTERACTION WITH DAXX, MUTAGENESIS OF LYS-709.
[6]"Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3."
McDonald P.H., Chow C.W., Miller W.E., Laporte S.A., Field M.E., Lin F.-T., Davis R.J., Lefkowitz R.J.
Science 290:1574-1577(2000) [PubMed: 11090355] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[7]"HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell."
Geleziunas R., Xu W., Takeda K., Ichijo H., Greene W.C.
Nature 410:834-838(2001) [PubMed: 11298454] [Abstract]
Cited for: INTERACTION WITH HIV-1 NEF, INHIBITION BY HIV-1 NEF.
[8]"Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer."
Tobiume K., Saitoh M., Ichijo H.
J. Cell. Physiol. 191:95-104(2002) [PubMed: 11920685] [Abstract]
Cited for: FUNCTION, HOMODIMERIZATION, ENZYME REGULATION, PHOSPHORYLATION AT THR-838.
[9]"AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3."
Zhang R., He X., Liu W., Lu M., Hsieh J.-T., Min W.
J. Clin. Invest. 111:1933-1943(2003) [PubMed: 12813029] [Abstract]
Cited for: INTERACTION WITH DAB2IP.
[10]"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
J. Biol. Chem. 279:44955-44965(2004) [PubMed: 15310755] [Abstract]
Cited for: INTERACTION WITH DAB2IP.
[11]"Negative control of apoptosis signal-regulating kinase 1 through phosphorylation of Ser-1034."
Fujii K., Goldman E.H., Park H.R., Zhang L., Chen J., Fu H.
Oncogene 23:5099-5104(2004) [PubMed: 15094778] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-966 AND SER-1033, MUTAGENESIS OF SER-966 AND SER-1033, INTERACTION WITH YWHAG.
[12]"Regulation of apoptosis signal-regulating kinase 1 by protein phosphatase 2Cepsilon."
Saito J., Toriumi S., Awano K., Ichijo H., Sasaki K., Kobayashi T., Tamura S.
Biochem. J. 405:591-596(2007) [PubMed: 17456047] [Abstract]
Cited for: INTERACTION WITH PPM1L.
[13]"Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-activated protein kinase kinase kinase in a heteromeric complex with ASK1."
Takeda K., Shimozono R., Noguchi T., Umeda T., Morimoto Y., Naguro I., Tobiume K., Saitoh M., Matsuzawa A., Ichijo H.
J. Biol. Chem. 282:7522-7531(2007) [PubMed: 17210579] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH MAP3K5, PHOSPHORYLATION AT THR-838, MUTAGENESIS OF LYS-709.
[14]"The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus."
Guo C., Whitmarsh A.J.
J. Biol. Chem. 283:15903-15911(2008) [PubMed: 18408005] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[15]"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: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, MASS SPECTROMETRY.
Tissue: Platelet.
[16]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, MASS SPECTROMETRY.
[17]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836; THR-838; SER-958; THR-976; SER-977; SER-978; SER-979; SER-984; SER-986; THR-989 AND SER-1033, MASS SPECTROMETRY.
[18]"Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1."
Takeda K., Komuro Y., Hayakawa T., Oguchi H., Ishida Y., Murakami S., Noguchi T., Kinoshita H., Sekine Y., Iemura S., Natsume T., Ichijo H.
Proc. Natl. Acad. Sci. U.S.A. 106:12301-12305(2009) [PubMed: 19590015] [Abstract]
Cited for: INTERACTION WITH PGAM5, PHOSPHORYLATION.
[19]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-1006; THR-1214; VAL-1250; ILE-1314 AND ASN-1315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U67156 mRNA. Translation: AAC50894.1.
D84476 mRNA. Translation: BAA12684.2.
AL024508, AL121933 Genomic DNA. Translation: CAI20176.1.
AL121933, AL024508 Genomic DNA. Translation: CAI15470.1.
BC054503 mRNA. Translation: AAH54503.1.
BC088829 mRNA. Translation: AAH88829.1.
IPIIPI00412433.
RefSeqNP_005914.1.
UniGeneHs.186486

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLQX-ray2.30A/B659-951[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29516N.
IntActQ99683. 19 interactions.
STRINGQ99683.

Proteomic databases

PRIDEQ99683.

Genome annotation databases

EnsemblENST00000359015; ENSP00000351908; ENSG00000197442; Homo sapiens. [Genome view]
GeneID4217.
KEGGhsa:4217.
UCSCuc003qhc.1. human.

Organism-specific databases

CTD4217.
GeneCardsGC06M136919.
H-InvDBHIX0025089.
HIX0028382.
HGNCHGNC:6857. MAP3K5.
HPACAB007824.
MIM602448. gene.
PharmGKBPA30601.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ99683.
InParanoidQ99683.
OMAESMSAEA.
OrthoDBEOG9909VQ.
PhylomeDBQ99683.

Enzyme and pathway databases

BRENDA2.7.11.25. 247.
2.7.12.2. 247.
Pathway_Interaction_DBpi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
mtor_4pathway. mTOR signaling pathway.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
tnfpathway. TNF receptor signaling pathway.

Gene expression databases

ArrayExpressQ99683.
BgeeQ99683.
CleanExHS_MAP3K5.
GenevestigatorQ99683.
GermOnlineENSG00000197442. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR010993. SAM_homology.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio16633.
SOURCESearch...

Entry information

Entry nameM3K5_HUMAN
AccessionPrimary (citable) accession number: Q99683
Secondary accession number(s): Q5THN3, Q99461
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: February 9, 2010
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents