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Protein

Mitogen-activated protein kinase kinase kinase 5

Gene

MAP3K5

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

Functioni

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1).18 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Activated by various stressors, including oxidative stress, endoplasmic reticulum stress, and calcium overload, as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) and lipopolysaccharide (LPS). Homophilic association of MAP3K5/ASK1 through the C-terminal coiled-coil domains and the heteromeric complex formation of MAP3K5/ASK1 with the reduced form of thioredoxin (TXN), constitutes an inactive form of the kinase (PubMed:17210579, PubMed:9564042). Upon ROS-induced dissociation of TXN from MAP3K5/ASK1, TRAF2 and TRAF6 are reciprocally recruited to MAP3K5/ASK1 and form the active MAP3K5/ASK1 signalosome, in which TRAF2 and TRAF6 appear to facilitate the active configuration of MAP3K5/ASK1 (PubMed:9774977, PubMed:10688666, PubMed:11920685). MAP3K5/ASK1 activity is also regulated through several phosphorylation and dephosphorylation events. Thr-838 is an activating phosphorylation site that is autophosphorylated and phosphorylated by MAP3K6/ASK2 and dephosphorylated by PPP5C (PubMed:11689443). Ser-83 and Ser-1033 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2 (PubMed:11154276, PubMed:12697749, PubMed:15094778). Phosphorylation of Ser-966 induces association of MAP3K5/ASK1 with the 14-3-3 family proteins, which suppresses MAP3K5/ASK1 activity (PubMed:10411906, PubMed:14688258). Calcium/calmodulin-activated protein phosphatase calcineurin (PPP3CA) has been shown to directly dephosphorylate this site (PubMed:14749717). SOCS1 binds to ASK1 by recognizing phosphorylation of Tyr-718 and induces MAP3K5/ASK1 degradation in endothelial cells (PubMed:16407264). Also dephosphorylated and activated by PGAM5. Contains an N-terminal autoinhibitory domain. Once activated targeted for proteosomal degradation by RC3H2-mediated ubiquitination (PubMed:24448648).15 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei709 – 7091ATP
Active sitei803 – 8031Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi686 – 6949ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • MAP kinase kinase kinase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein phosphatase binding Source: BHF-UCL
  • protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

  • activation of JUN kinase activity Source: ProtInc
  • activation of MAPKK activity Source: BHF-UCL
  • apoptotic signaling pathway Source: ProtInc
  • cellular response to hydrogen peroxide Source: BHF-UCL
  • cellular response to reactive nitrogen species Source: Ensembl
  • innate immune response Source: UniProtKB-KW
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
  • JNK cascade Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • p38MAPK cascade Source: Ensembl
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  • positive regulation of JNK cascade Source: ParkinsonsUK-UCL
  • positive regulation of JUN kinase activity Source: ParkinsonsUK-UCL
  • positive regulation of myoblast differentiation Source: Ensembl
  • positive regulation of neuron death Source: ParkinsonsUK-UCL
  • programmed necrotic cell death Source: Ensembl
  • protein phosphorylation Source: ParkinsonsUK-UCL
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • response to ischemia Source: Ensembl
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Host-virus interaction, Immunity, Innate immunity, Stress response

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.2. 2681.
ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
SignaLinkiQ99683.
SIGNORiQ99683.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase 5 (EC:2.7.11.25)
Alternative name(s):
Apoptosis signal-regulating kinase 1
Short name:
ASK-1
MAPK/ERK kinase kinase 5
Short name:
MEK kinase 5
Short name:
MEKK 5
Gene namesi
Name:MAP3K5
Synonyms:ASK1, MAPKKK5, MEKK5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6857. MAP3K5.

Subcellular locationi

  • Cytoplasm
  • Endoplasmic reticulum

  • Note: Interaction with 14-3-3 proteins alters the distribution of MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum region.

GO - Cellular componenti

  • cytosol Source: Reactome
  • IRE1-TRAF2-ASK1 complex Source: ParkinsonsUK-UCL
  • protein kinase complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi709 – 7091K → M: Loss of kinase activity. Inhibits activation of JNK and apoptosis mediated by TNFRSF6 and DAXX. 2 Publications
Mutagenesisi709 – 7091K → R: Loss of kinase activity. Abolishes DAXX-mediated apoptosis. Loss of RC3H2-mediated ubiquitination. 3 Publications
Mutagenesisi966 – 9661S → A: Enhanced induction of apoptosis, increased kinase activity, and loss of YWHAG binding. 2 Publications
Mutagenesisi1033 – 10331S → A: Enhanced induction of apoptosis and increased kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA30601.

Chemistry

ChEMBLiCHEMBL5285.
GuidetoPHARMACOLOGYi2080.

Polymorphism and mutation databases

BioMutaiMAP3K5.
DMDMi6685617.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13741374Mitogen-activated protein kinase kinase kinase 5PRO_0000086249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831Phosphoserine; by PIM1, PKB/AKT1 and PKB/AKT23 Publications
Modified residuei718 – 7181Phosphotyrosine1 Publication
Modified residuei813 – 8131Phosphothreonine; by autocatalysis1 Publication
Modified residuei838 – 8381Phosphothreonine; by autocatalysis, MELK and MAP3K66 Publications
Modified residuei842 – 8421Phosphothreonine; by autocatalysis1 Publication
Modified residuei958 – 9581PhosphoserineCombined sources1 Publication
Modified residuei966 – 9661Phosphoserine3 Publications
Modified residuei1029 – 10291PhosphoserineCombined sources
Modified residuei1033 – 10331PhosphoserineCombined sources2 Publications

Post-translational modificationi

Phosphorylated at Thr-838 through autophosphorylation and by MAP3K6/ASK2 which leads to activation. Thr-838 is dephosphorylated by PPP5C. Ser-83 and Ser-1033 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2. Phosphorylated at Ser-966 which induces association of MAP3K5/ASK1 with the 14-3-3 family proteins and suppresses MAP3K5/ASK1 activity. Calcineurin (CN) dephosphorylates this site. Also dephosphorylated and activated by PGAM5.13 Publications
Ubiquitinated. Tumor necrosis factor (TNF) induces TNFR2-dependent ubiquitination leading to proteasomal degradation.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99683.
MaxQBiQ99683.
PaxDbiQ99683.
PeptideAtlasiQ99683.
PRIDEiQ99683.

PTM databases

iPTMnetiQ99683.
PhosphoSiteiQ99683.

Expressioni

Tissue specificityi

Abundantly expressed in heart and pancreas.

Inductioni

By TNF. Inhibited by HIV-1 Nef.

Gene expression databases

BgeeiENSG00000197442.
CleanExiHS_MAP3K5.
GenevisibleiQ99683. HS.

Organism-specific databases

HPAiCAB007824.

Interactioni

Subunit structurei

Homodimer when inactive. Binds both upstream activators and downstream substrates in multimolecular complexes. Associates with and inhibited by HIV-1 Nef (PubMed:11298454). Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF (PubMed:15310755, PubMed:15701637, PubMed:17210579, PubMed:17389591). This complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Interacts with SOCS1 which recognizes phosphorylation of Tyr-718 and induces MAP3K5/ASK1 degradation in endothelial cells. Interacts with the 14-3-3 family proteins such as YWHAB, YWHAE, YWHAQ, YWHAH, YWHAZ and SFN (PubMed:10411906, PubMed:15023544, PubMed:15094778). Interacts with ARRB2, BIRC2, DAB2IP, IGF1R, MAP3K6/ASK2, PGAM5, PIM1, PPP5C, SOCS1, STUB1, TRAF2, TRAF6 and TXN (PubMed:9564042,PubMed:9774977, PubMed:10688666, PubMed:11090355, PubMed:11689443, PubMed:12556535, PubMed:12813029, PubMed:15310755, PubMed:16038411, PubMed:16129676, PubMed:16407264, PubMed:17220297, PubMed:17724081, PubMed:18408005, PubMed:19590015, PubMed:19749799). Interacts with ERN1 in a TRAF2-dependent manner (PubMed:14749717). Interacts with calcineurin subunit PPP3R1 and with PPM1L (PubMed:17456047) (By similarity). Interacts (via N-terminus) with RAF1 and this interaction inhibits the proapoptotic function of MAP3K5 (PubMed:11427728). Interacts with DAB2IP (via N-terminus C2 domain); the interaction occurs in a TNF-alpha-dependent manner (PubMed:15310755). Interacts with DUSP13/DUSP13A; may positively regulate apoptosis (PubMed:20358250). Interacts with DAXX (PubMed:9743501). Interacts with RC3H2 (PubMed:24448648).By similarity29 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-476263,EBI-296087
APPP050672EBI-476263,EBI-77613
ARRB1P494073EBI-476263,EBI-743313
ARRB2P321212EBI-476263,EBI-714559
DAB2IPQ5VWQ82EBI-476263,EBI-2871881
DAXXQ9UER77EBI-476263,EBI-77321
FASP254452EBI-476263,EBI-494743
MAP2K3P467342EBI-476263,EBI-602462
Map3k6Q9WTR23EBI-476263,EBI-1254790From a different organism.
MCRS1Q96EZ83EBI-476263,EBI-348259
PPP3R1P630982EBI-476263,EBI-915984
SMN2Q166373EBI-476263,EBI-395421
TXNP105992EBI-476263,EBI-594644
YWHABP319463EBI-476263,EBI-359815
YWHAZP631044EBI-476263,EBI-347088
ZNF622Q969S314EBI-476263,EBI-2687480

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110381. 82 interactions.
DIPiDIP-29516N.
IntActiQ99683. 41 interactions.
MINTiMINT-99796.
STRINGi9606.ENSP00000351908.

Chemistry

BindingDBiQ99683.

Structurei

Secondary structure

1
1374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi673 – 6753Combined sources
Beta strandi681 – 6833Combined sources
Beta strandi685 – 6884Combined sources
Beta strandi693 – 6997Combined sources
Turni700 – 7023Combined sources
Beta strandi705 – 7128Combined sources
Helixi725 – 7295Combined sources
Beta strandi740 – 7467Combined sources
Beta strandi749 – 7557Combined sources
Beta strandi758 – 7614Combined sources
Helixi762 – 7687Combined sources
Helixi777 – 79620Combined sources
Helixi806 – 8083Combined sources
Beta strandi809 – 8124Combined sources
Turni813 – 8153Combined sources
Beta strandi818 – 8203Combined sources
Turni823 – 8253Combined sources
Beta strandi827 – 8293Combined sources
Helixi843 – 8453Combined sources
Helixi848 – 8536Combined sources
Helixi854 – 8574Combined sources
Helixi860 – 87617Combined sources
Helixi882 – 8843Combined sources
Helixi887 – 89711Combined sources
Helixi909 – 91810Combined sources
Turni923 – 9253Combined sources
Helixi929 – 9335Combined sources
Helixi936 – 9383Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLQX-ray2.30A/B659-951[»]
3VW6X-ray2.40A/B671-939[»]
4BF2X-ray2.11A/B660-977[»]
4BHNX-ray2.30A/B660-977[»]
4BIBX-ray2.43A/B660-977[»]
4BICX-ray2.62A/B660-977[»]
4BIDX-ray2.80A/B660-977[»]
4BIEX-ray2.36A/B660-977[»]
ProteinModelPortaliQ99683.
SMRiQ99683. Positions 670-940.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99683.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini680 – 938259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1245 – 128541Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4279. Eukaryota.
ENOG410XQGS. LUCA.
GeneTreeiENSGT00800000124036.
HOGENOMiHOG000293286.
HOVERGENiHBG006305.
InParanoidiQ99683.
KOiK04426.
OMAiTELHCKK.
OrthoDBiEOG091G00SJ.
PhylomeDBiQ99683.
TreeFamiTF105115.

Family and domain databases

InterProiIPR025136. DUF4071.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR013761. SAM/pointed.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13281. DUF4071. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99683-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSTEADEGIT FSVPPFAPSG FCTIPEGGIC RRGGAAAVGE GEEHQLPPPP
60 70 80 90 100
PGSFWNVESA AAPGIGCPAA TSSSSATRGR GSSVGGGSRR TTVAYVINEA
110 120 130 140 150
SQGQLVVAES EALQSLREAC ETVGATLETL HFGKLDFGET TVLDRFYNAD
160 170 180 190 200
IAVVEMSDAF RQPSLFYHLG VRESFSMANN IILYCDTNSD SLQSLKEIIC
210 220 230 240 250
QKNTMCTGNY TFVPYMITPH NKVYCCDSSF MKGLTELMQP NFELLLGPIC
260 270 280 290 300
LPLVDRFIQL LKVAQASSSQ YFRESILNDI RKARNLYTGK ELAAELARIR
310 320 330 340 350
QRVDNIEVLT ADIVINLLLS YRDIQDYDSI VKLVETLEKL PTFDLASHHH
360 370 380 390 400
VKFHYAFALN RRNLPGDRAK ALDIMIPMVQ SEGQVASDMY CLVGRIYKDM
410 420 430 440 450
FLDSNFTDTE SRDHGASWFK KAFESEPTLQ SGINYAVLLL AAGHQFESSF
460 470 480 490 500
ELRKVGVKLS SLLGKKGNLE KLQSYWEVGF FLGASVLAND HMRVIQASEK
510 520 530 540 550
LFKLKTPAWY LKSIVETILI YKHFVKLTTE QPVAKQELVD FWMDFLVEAT
560 570 580 590 600
KTDVTVVRFP VLILEPTKIY QPSYLSINNE VEEKTISIWH VLPDDKKGIH
610 620 630 640 650
EWNFSASSVR GVSISKFEER CCFLYVLHNS DDFQIYFCTE LHCKKFFEMV
660 670 680 690 700
NTITEEKGRS TEEGDCESDL LEYDYEYDEN GDRVVLGKGT YGIVYAGRDL
710 720 730 740 750
SNQVRIAIKE IPERDSRYSQ PLHEEIALHK HLKHKNIVQY LGSFSENGFI
760 770 780 790 800
KIFMEQVPGG SLSALLRSKW GPLKDNEQTI GFYTKQILEG LKYLHDNQIV
810 820 830 840 850
HRDIKGDNVL INTYSGVLKI SDFGTSKRLA GINPCTETFT GTLQYMAPEI
860 870 880 890 900
IDKGPRGYGK AADIWSLGCT IIEMATGKPP FYELGEPQAA MFKVGMFKVH
910 920 930 940 950
PEIPESMSAE AKAFILKCFE PDPDKRACAN DLLVDEFLKV SSKKKKTQPK
960 970 980 990 1000
LSALSAGSNE YLRSISLPVP VLVEDTSSSS EYGSVSPDTE LKVDPFSFKT
1010 1020 1030 1040 1050
RAKSCGERDV KGIRTLFLGI PDENFEDHSA PPSPEEKDSG FFMLRKDSER
1060 1070 1080 1090 1100
RATLHRILTE DQDKIVRNLM ESLAQGAEEP KLKWEHITTL IASLREFVRS
1110 1120 1130 1140 1150
TDRKIIATTL SKLKLELDFD SHGISQVQVV LFGFQDAVNK VLRNHNIKPH
1160 1170 1180 1190 1200
WMFALDSIIR KAVQTAITIL VPELRPHFSL ASESDTADQE DLDVEDDHEE
1210 1220 1230 1240 1250
QPSNQTVRRP QAVIEDAVAT SGVSTLSSTV SHDSQSAHRS LNVQLGRMKI
1260 1270 1280 1290 1300
ETNRLLEELV RKEKELQALL HRAIEEKDQE IKHLKLKSQP IEIPELPVFH
1310 1320 1330 1340 1350
LNSSGTNTED SELTDWLRVN GADEDTISRF LAEDYTLLDV LYYVTRDDLK
1360 1370
CLRLRGGMLC TLWKAIIDFR NKQT
Length:1,374
Mass (Da):154,537
Last modified:May 1, 1997 - v1
Checksum:i265BDC65968AF985
GO
Isoform 2 (identifier: Q99683-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-753: Missing.

Note: No experimental confirmation available.
Show »
Length:621
Mass (Da):69,839
Checksum:i7EFE3AD82F6AB9FF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1006 – 10061G → R.1 Publication
Corresponds to variant rs45626535 [ dbSNP | Ensembl ].
VAR_040693
Natural varianti1214 – 12141I → T.1 Publication
Corresponds to variant rs56379668 [ dbSNP | Ensembl ].
VAR_040694
Natural varianti1250 – 12501I → V.1 Publication
Corresponds to variant rs35551087 [ dbSNP | Ensembl ].
VAR_040695
Natural varianti1314 – 13141T → I.1 Publication
Corresponds to variant rs45599539 [ dbSNP | Ensembl ].
VAR_040696
Natural varianti1315 – 13151D → N.1 Publication
Corresponds to variant rs41288957 [ dbSNP | Ensembl ].
VAR_040697

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 753753Missing in isoform 2. 1 PublicationVSP_056182Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67156 mRNA. Translation: AAC50894.1.
D84476 mRNA. Translation: BAA12684.2.
AK294507 mRNA. Translation: BAG57723.1.
AL024508, AL121933 Genomic DNA. Translation: CAI20176.1.
AL121933, AL024508 Genomic DNA. Translation: CAI15470.1.
BC054503 mRNA. Translation: AAH54503.1.
BC088829 mRNA. Translation: AAH88829.1.
CCDSiCCDS5179.1. [Q99683-1]
RefSeqiNP_005914.1. NM_005923.3. [Q99683-1]
UniGeneiHs.186486.

Genome annotation databases

EnsembliENST00000359015; ENSP00000351908; ENSG00000197442. [Q99683-1]
GeneIDi4217.
KEGGihsa:4217.
UCSCiuc003qhc.4. human. [Q99683-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67156 mRNA. Translation: AAC50894.1.
D84476 mRNA. Translation: BAA12684.2.
AK294507 mRNA. Translation: BAG57723.1.
AL024508, AL121933 Genomic DNA. Translation: CAI20176.1.
AL121933, AL024508 Genomic DNA. Translation: CAI15470.1.
BC054503 mRNA. Translation: AAH54503.1.
BC088829 mRNA. Translation: AAH88829.1.
CCDSiCCDS5179.1. [Q99683-1]
RefSeqiNP_005914.1. NM_005923.3. [Q99683-1]
UniGeneiHs.186486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLQX-ray2.30A/B659-951[»]
3VW6X-ray2.40A/B671-939[»]
4BF2X-ray2.11A/B660-977[»]
4BHNX-ray2.30A/B660-977[»]
4BIBX-ray2.43A/B660-977[»]
4BICX-ray2.62A/B660-977[»]
4BIDX-ray2.80A/B660-977[»]
4BIEX-ray2.36A/B660-977[»]
ProteinModelPortaliQ99683.
SMRiQ99683. Positions 670-940.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110381. 82 interactions.
DIPiDIP-29516N.
IntActiQ99683. 41 interactions.
MINTiMINT-99796.
STRINGi9606.ENSP00000351908.

Chemistry

BindingDBiQ99683.
ChEMBLiCHEMBL5285.
GuidetoPHARMACOLOGYi2080.

PTM databases

iPTMnetiQ99683.
PhosphoSiteiQ99683.

Polymorphism and mutation databases

BioMutaiMAP3K5.
DMDMi6685617.

Proteomic databases

EPDiQ99683.
MaxQBiQ99683.
PaxDbiQ99683.
PeptideAtlasiQ99683.
PRIDEiQ99683.

Protocols and materials databases

DNASUi4217.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359015; ENSP00000351908; ENSG00000197442. [Q99683-1]
GeneIDi4217.
KEGGihsa:4217.
UCSCiuc003qhc.4. human. [Q99683-1]

Organism-specific databases

CTDi4217.
GeneCardsiMAP3K5.
HGNCiHGNC:6857. MAP3K5.
HPAiCAB007824.
MIMi602448. gene.
neXtProtiNX_Q99683.
PharmGKBiPA30601.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4279. Eukaryota.
ENOG410XQGS. LUCA.
GeneTreeiENSGT00800000124036.
HOGENOMiHOG000293286.
HOVERGENiHBG006305.
InParanoidiQ99683.
KOiK04426.
OMAiTELHCKK.
OrthoDBiEOG091G00SJ.
PhylomeDBiQ99683.
TreeFamiTF105115.

Enzyme and pathway databases

BRENDAi2.7.12.2. 2681.
ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
SignaLinkiQ99683.
SIGNORiQ99683.

Miscellaneous databases

ChiTaRSiMAP3K5. human.
EvolutionaryTraceiQ99683.
GeneWikiiASK1.
GenomeRNAii4217.
PROiQ99683.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197442.
CleanExiHS_MAP3K5.
GenevisibleiQ99683. HS.

Family and domain databases

InterProiIPR025136. DUF4071.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR013761. SAM/pointed.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13281. DUF4071. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiM3K5_HUMAN
AccessioniPrimary (citable) accession number: Q99683
Secondary accession number(s): A6NIA0
, B4DGB2, Q5THN3, Q99461
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: September 7, 2016
This is version 177 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 6
    Human chromosome 6: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.