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Q99683

- M3K5_HUMAN

UniProt

Q99683 - M3K5_HUMAN

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Protein

Mitogen-activated protein kinase kinase kinase 5

Gene

MAP3K5

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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. 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. Ser-83 and Ser-1033 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2. Phosphorylation of Ser-966 induces association of MAP3K5/ASK1 with the 14-3-3 family proteins, which suppresses MAP3K5/ASK1 activity. Calcium/calmodulin-activated protein phosphatase calcineurin (PPP3CA) has been shown to directly dephosphorylate this site. SOCS1 binds to ASK1 by recognizing phosphorylation of Tyr-718 and induces MAP3K5/ASK1 degradation in endothelial cells. Also dephosphorylated and activated by PGAM5. Contains an N-terminal autoinhibitory domain.14 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

  1. ATP binding Source: UniProtKB
  2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB
  4. MAP kinase kinase kinase activity Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. protein kinase activity Source: UniProtKB
  7. protein phosphatase binding Source: BHF-UCL

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
  2. activation of JUN kinase activity Source: ProtInc
  3. activation of MAPKK activity Source: BHF-UCL
  4. apoptotic signaling pathway Source: ProtInc
  5. cellular response to hydrogen peroxide Source: BHF-UCL
  6. cellular response to reactive nitrogen species Source: Ensembl
  7. innate immune response Source: UniProtKB-KW
  8. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
  9. JNK cascade Source: UniProtKB
  10. MAPK cascade Source: UniProtKB
  11. positive regulation of apoptotic process Source: UniProtKB
  12. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  13. positive regulation of neuron death Source: ParkinsonsUK-UCL
  14. programmed necrotic cell death Source: Ensembl
  15. protein phosphorylation Source: ParkinsonsUK-UCL
  16. response to ischemia Source: Ensembl
  17. 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.
ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
SignaLinkiQ99683.

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
ProteomesiUP000005640: 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

  1. cytosol Source: Reactome
  2. endoplasmic reticulum Source: UniProtKB-KW
  3. 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. 2 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.

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 – 9581Phosphoserine1 Publication
Modified residuei966 – 9661Phosphoserine3 Publications
Modified residuei976 – 9761PhosphothreonineBy similarity
Modified residuei1029 – 10291Phosphoserine2 Publications
Modified residuei1033 – 10331Phosphoserine5 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 PGAM5.16 Publications
Ubiquitinated. Tumor necrosis factor (TNF) induces TNFR2-dependent ubiquitination leading to proteasomal degradation.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ99683.
PaxDbiQ99683.
PRIDEiQ99683.

PTM databases

PhosphoSiteiQ99683.

Expressioni

Tissue specificityi

Abundantly expressed in heart and pancreas.

Inductioni

By TNF. Inhibited by HIV-1 Nef.

Gene expression databases

BgeeiQ99683.
CleanExiHS_MAP3K5.
ExpressionAtlasiQ99683. baseline and differential.
GenevestigatoriQ99683.

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. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF. 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. Interacts with ARRB2, BIRC2, DAB2IP, IGF1R, MAP3K6/ASK2, PGAM5, PIM1, PPP5C, SOCS1, STUB1, TRAF2, TRAF6 and TXN. Interacts with ERN1 in a TRAF2-dependent manner. Interacts with calcineurin subunit PPP3R1 and with PPM1L (By similarity). Interacts (via N-terminus) with RAF1 and this interaction inhibits the proapoptotic function of MAP3K5. Interacts with DAB2IP (via N-terminus C2 domain); the interaction occurs in a TNF-alpha-dependent manner. Interacts with DUSP13/DUSP13A; may positively regulate apoptosis.By similarity28 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
YWHAZP631043EBI-476263,EBI-347088
ZNF622Q969S314EBI-476263,EBI-2687480

Protein-protein interaction databases

BioGridi110381. 75 interactions.
DIPiDIP-29516N.
IntActiQ99683. 39 interactions.
MINTiMINT-99796.
STRINGi9606.ENSP00000351908.

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 641-962.
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

eggNOGiCOG0515.
GeneTreeiENSGT00760000119077.
HOVERGENiHBG006305.
InParanoidiQ99683.
KOiK04426.
OMAiTELHCKK.
OrthoDBiEOG7WDN1P.
PhylomeDBiQ99683.
TreeFamiTF105115.

Family and domain databases

InterProiIPR025136. DUF4071.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR013761. SAM/pointed.
IPR002290. Ser/Thr_dual-sp_kinase.
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. Align

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.3. human. [Q99683-1]

Polymorphism databases

DMDMi6685617.

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 .
CCDSi CCDS5179.1. [Q99683-1 ]
RefSeqi NP_005914.1. NM_005923.3. [Q99683-1 ]
UniGenei Hs.186486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CLQ X-ray 2.30 A/B 659-951 [» ]
3VW6 X-ray 2.40 A/B 671-939 [» ]
4BF2 X-ray 2.11 A/B 660-977 [» ]
4BHN X-ray 2.30 A/B 660-977 [» ]
4BIB X-ray 2.43 A/B 660-977 [» ]
4BIC X-ray 2.62 A/B 660-977 [» ]
4BID X-ray 2.80 A/B 660-977 [» ]
4BIE X-ray 2.36 A/B 660-977 [» ]
ProteinModelPortali Q99683.
SMRi Q99683. Positions 641-962.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110381. 75 interactions.
DIPi DIP-29516N.
IntActi Q99683. 39 interactions.
MINTi MINT-99796.
STRINGi 9606.ENSP00000351908.

Chemistry

BindingDBi Q99683.
ChEMBLi CHEMBL5285.
GuidetoPHARMACOLOGYi 2080.

PTM databases

PhosphoSitei Q99683.

Polymorphism databases

DMDMi 6685617.

Proteomic databases

MaxQBi Q99683.
PaxDbi Q99683.
PRIDEi Q99683.

Protocols and materials databases

DNASUi 4217.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359015 ; ENSP00000351908 ; ENSG00000197442 . [Q99683-1 ]
GeneIDi 4217.
KEGGi hsa:4217.
UCSCi uc003qhc.3. human. [Q99683-1 ]

Organism-specific databases

CTDi 4217.
GeneCardsi GC06M136878.
HGNCi HGNC:6857. MAP3K5.
HPAi CAB007824.
MIMi 602448. gene.
neXtProti NX_Q99683.
PharmGKBi PA30601.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119077.
HOVERGENi HBG006305.
InParanoidi Q99683.
KOi K04426.
OMAi TELHCKK.
OrthoDBi EOG7WDN1P.
PhylomeDBi Q99683.
TreeFami TF105115.

Enzyme and pathway databases

BRENDAi 2.7.12.2. 2681.
Reactomei REACT_169436. Oxidative Stress Induced Senescence.
SignaLinki Q99683.

Miscellaneous databases

ChiTaRSi MAP3K5. human.
EvolutionaryTracei Q99683.
GeneWikii ASK1.
GenomeRNAii 4217.
NextBioi 16633.
PROi Q99683.
SOURCEi Search...

Gene expression databases

Bgeei Q99683.
CleanExi HS_MAP3K5.
ExpressionAtlasi Q99683. baseline and differential.
Genevestigatori Q99683.

Family and domain databases

InterProi IPR025136. DUF4071.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR013761. SAM/pointed.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF13281. DUF4071. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Amygdala.
  4. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye and Lung.
  6. "Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1."
    Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y., Kawabata M., Miyazono K., Ichijo H.
    EMBO J. 17:2596-2606(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TXN, ENZYME REGULATION, FUNCTION.
  7. Cited for: ENZYME REGULATION, INTERACTION WITH TRAF2, FUNCTION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX, MUTAGENESIS OF LYS-709.
  9. "Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins."
    Zhang L., Chen J., Fu H.
    Proc. Natl. Acad. Sci. U.S.A. 96:8511-8515(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH 14-3-3 PROTEINS, ENZYME REGULATION, MUTAGENESIS OF SER-966, FUNCTION.
  10. "Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation."
    Hatai T., Matsuzawa A., Inoshita S., Mochida Y., Kuroda T., Sakamaki K., Kuida K., Yonehara S., Ichijo H., Takeda K.
    J. Biol. Chem. 275:26576-26581(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  11. "Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin."
    Liu H., Nishitoh H., Ichijo H., Kyriakis J.M.
    Mol. Cell. Biol. 20:2198-2208(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH TRAF2, ENZYME REGULATION, FUNCTION.
  12. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2.
  13. "Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in response to oxidative stress."
    Morita K., Saitoh M., Tobiume K., Matsuura H., Enomoto S., Nishitoh H., Ichijo H.
    EMBO J. 20:6028-6036(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP5C, DEPHOSPHORYLATION AT THR-838, SUBCELLULAR LOCATION, ENZYME REGULATION, FUNCTION.
  14. "Apoptosis signal-regulating kinase 1 (ASK1) is an intracellular inducer of keratinocyte differentiation."
    Sayama K., Hanakawa Y., Shirakata Y., Yamasaki K., Sawada Y., Sun L., Yamanishi K., Ichijo H., Hashimoto K.
    J. Biol. Chem. 276:999-1004(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KERATINOCYTE DIFFERENTIATION.
  15. "Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1."
    Kim A.H., Khursigara G., Sun X., Franke T.F., Chao M.V.
    Mol. Cell. Biol. 21:893-901(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-83, ENZYME REGULATION, FUNCTION.
  16. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 NEF, INHIBITION BY HIV-1 NEF.
  17. "Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism."
    Chen J., Fujii K., Zhang L., Roberts T., Fu H.
    Proc. Natl. Acad. Sci. U.S.A. 98:7783-7788(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAF1.
  18. Cited for: INTERACTION WITH TRAF2 AND ERN1, ENZYME REGULATION, FUNCTION IN ER STRESS RESPONSE.
  19. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, ENZYME REGULATION, PHOSPHORYLATION AT THR-838.
  20. "Type 1 insulin-like growth factor receptor (IGF-IR) signaling inhibits apoptosis signal-regulating kinase 1 (ASK1)."
    Galvan V., Logvinova A., Sperandio S., Ichijo H., Bredesen D.E.
    J. Biol. Chem. 278:13325-13332(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGF1R, PHOSPHORYLATION, ENZYME REGULATION, SUBCELLULAR LOCATION.
  21. "AKT2 inhibition of cisplatin-induced JNK/p38 and Bax activation by phosphorylation of ASK1: implication of AKT2 in chemoresistance."
    Yuan Z.Q., Feldman R.I., Sussman G.E., Coppola D., Nicosia S.V., Cheng J.Q.
    J. Biol. Chem. 278:23432-23440(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-83, ENZYME REGULATION, FUNCTION.
  22. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2IP.
  23. "Interaction of apoptosis signal-regulating kinase 1 with isoforms of 14-3-3 proteins."
    Subramanian R.R., Zhang H., Wang H., Ichijo H., Miyashita T., Fu H.
    Exp. Cell Res. 294:581-591(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YWHAB; YWHAE; YWHAH; YWHAQ; YWHAZ AND SFN, FUNCTION, SUBCELLULAR LOCATION.
  24. "Activation of apoptosis signal-regulating kinase 1 by reactive oxygen species through dephosphorylation at serine 967 and 14-3-3 dissociation."
    Goldman E.H., Chen L., Fu H.
    J. Biol. Chem. 279:10442-10449(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-966, ENZYME REGULATION, FUNCTION.
  25. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2IP.
  26. "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] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-966 AND SER-1033, MUTAGENESIS OF SER-966 AND SER-1033, INTERACTION WITH YWHAG.
  27. "C-terminus of heat shock protein 70-interacting protein facilitates degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis signal-regulating kinase 1-dependent apoptosis."
    Hwang J.R., Zhang C., Patterson C.
    Cell Stress Chaperones 10:147-156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STUB1, UBIQUITINATION.
  28. "Tumor necrosis factor alpha-induced desumoylation and cytoplasmic translocation of homeodomain-interacting protein kinase 1 are critical for apoptosis signal-regulating kinase 1-JNK/p38 activation."
    Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.
    J. Biol. Chem. 280:15061-15070(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
  29. "Recruitment of tumor necrosis factor receptor-associated factor family proteins to apoptosis signal-regulating kinase 1 signalosome is essential for oxidative stress-induced cell death."
    Noguchi T., Takeda K., Matsuzawa A., Saegusa K., Nakano H., Gohda J., Inoue J., Ichijo H.
    J. Biol. Chem. 280:37033-37040(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH TRAF2, FUNCTION.
  30. "SOCS1 inhibits tumor necrosis factor-induced activation of ASK1-JNK inflammatory signaling by mediating ASK1 degradation."
    He Y., Zhang W., Zhang R., Zhang H., Min W.
    J. Biol. Chem. 281:5559-5566(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-718, INTERACTION WITH SOCS1, ENZYME REGULATION.
  31. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPM1L.
  32. "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] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH MAP3K5, PHOSPHORYLATION AT THR-838, MUTAGENESIS OF LYS-709.
  33. "Tumor necrosis factor receptor 2 signaling induces selective c-IAP1-dependent ASK1 ubiquitination and terminates mitogen-activated protein kinase signaling."
    Zhao Y., Conze D.B., Hanover J.A., Ashwell J.D.
    J. Biol. Chem. 282:7777-7782(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIRC2, UBIQUITINATION, FUNCTION.
  34. "RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation."
    Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.
    J. Biol. Chem. 282:14788-14796(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2IP.
  35. "Thioredoxin and TRAF family proteins regulate reactive oxygen species-dependent activation of ASK1 through reciprocal modulation of the N-terminal homophilic interaction of ASK1."
    Fujino G., Noguchi T., Matsuzawa A., Yamauchi S., Saitoh M., Takeda K., Ichijo H.
    Mol. Cell. Biol. 27:8152-8163(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF2; TRAF6 AND TXN.
  36. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2.
  37. "Murine protein serine/threonine kinase 38 activates apoptosis signal-regulating kinase 1 via Thr 838 phosphorylation."
    Jung H., Seong H.A., Ha H.
    J. Biol. Chem. 283:34541-34553(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-838.
  38. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  39. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  40. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis."
    Gu J.J., Wang Z., Reeves R., Magnuson N.S.
    Oncogene 28:4261-4271(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-83 BY PIM1, INTERACTION WITH PIM1.
  42. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PGAM5, PHOSPHORYLATION AT THR-838; SER-966 AND SER-1033.
  43. "Apoptosis signal-regulating kinase 1 in stress and immune response."
    Takeda K., Noguchi T., Naguro I., Ichijo H.
    Annu. Rev. Pharmacol. Toxicol. 48:199-225(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  44. "The roles of ASK family proteins in stress responses and diseases."
    Hattori K., Naguro I., Runchel C., Ichijo H.
    Cell Commun. Signal. 7:9-9(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  45. "Positive regulation of apoptosis signal-regulating kinase 1 by dual-specificity phosphatase 13A."
    Park J.E., Park B.C., Kim H.A., Song M., Park S.G., Lee D.H., Kim H.J., Choi H.K., Kim J.T., Cho S.
    Cell. Mol. Life Sci. 67:2619-2629(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP13.
  46. "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5."
    Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.
    Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-838, DEPHOSPHORYLATION AT THR-838 BY PPP5C.
  47. "Structural and functional characterization of the human protein kinase ASK1."
    Bunkoczi G., Salah E., Filippakopoulos P., Fedorov O., Muller S., Sobott F., Parker S.A., Zhang H., Min W., Turk B.E., Knapp S.
    Structure 15:1215-1226(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 659-951, PHOSPHORYLATION AT THR-813; THR-838 AND THR-842.
  48. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-1006; THR-1214; VAL-1250; ILE-1314 AND ASN-1315.

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: November 26, 2014
This is version 160 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

External Data

Dasty 3