M3K13_HUMAN - dbPTM
M3K13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M3K13_HUMAN
UniProt AC O43283
Protein Name Mitogen-activated protein kinase kinase kinase 13
Gene Name MAP3K13 {ECO:0000312|HGNC:HGNC:6852}
Organism Homo sapiens (Human).
Sequence Length 966
Subcellular Localization Cytoplasm . Membrane
Peripheral membrane protein .
Protein Description Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B..
Protein Sequence MANFQEHLSCSSSPHLPFSESKTFNGLQDELTAMGNHPSPKLLEDQQEKGMVRTELIESVHSPVTTTVLTSVSEDSRDQFENSVLQLREHDESETAVSQGNSNTVDGESTSGTEDIKIQFSRSGSGSGGFLEGLFGCLRPVWNIIGKAYSTDYKLQQQDTWEVPFEEISELQWLGSGAQGAVFLGKFRAEEVAIKKVREQNETDIKHLRKLKHPNIIAFKGVCTQAPCYCIIMEYCAHGQLYEVLRAGRKITPRLLVDWSTGIASGMNYLHLHKIIHRDLKSPNVLVTHTDAVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSTCPDGFKILMKQTWQSKPRNRPSFRQTLMHLDIASADVLATPQETYFKSQAEWREEVKKHFEKIKSEGTCIHRLDEELIRRRREELRHALDIREHYERKLERANNLYMELSAIMLQLEMREKELIKREQAVEKKYPGTYKRHPVRPIIHPNAMEKLMKRKGVPHKSGMQTKRPDLLRSEGIPTTEVAPTASPLSGSPKMSTSSSKSRYRSKPRHRRGNSRGSHSDFAAILKNQPAQENSPHPTYLHQAQSQYPSLHHHNSLQQQYQQPPPAMSQSHHPRLNMHGQDIATCANNLRYFGPAAALRSPLSNHAQRQLPGSSPDLISTAMAADCWRSSEPDKGQAGPWGCCQADAYDPCLQCRPEQYGSLDIPSAEPVGRSPDLSKSPAHNPLLENAQSSEKTEENEFSGCRSESSLGTSHLGTPPALPRKTRPLQKSGDDSSEEEEGEVDSEVEFPRRQRPHRCISSCQSYSTFSSENFSVSDGEEGNTSDHSNSPDELADKLEDRLAEKLDDLLSQTPEIPIDISSHSDGLSDKECAVRRVKTQMSLGKLCVEERGYENPMQFEESDCDSSDGECSDATVRTNKHYSSATW
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
54PhosphorylationQEKGMVRTELIESVH
HHHCCHHHHHHHHCC
24.5924719451
57UbiquitinationGMVRTELIESVHSPV
CCHHHHHHHHCCCCC
2.7822505724
59PhosphorylationVRTELIESVHSPVTT
HHHHHHHHCCCCCCE
20.3824719451
121 (in isoform 6)Phosphorylation-14.7926270265
123 (in isoform 6)Phosphorylation-35.7926270265
126 (in isoform 6)Phosphorylation-33.5626270265
206UbiquitinationEQNETDIKHLRKLKH
HCCCCCHHHHHHCCC
39.1222505724
282PhosphorylationIIHRDLKSPNVLVTH
HHCCCCCCCCEEEEE
29.07-
288PhosphorylationKSPNVLVTHTDAVKI
CCCCEEEEECCEEEH
18.20-
296PhosphorylationHTDAVKISDFGTSKE
ECCEEEHHHCCCCHH
22.5924905233
300PhosphorylationVKISDFGTSKELSDK
EEHHHCCCCHHHCCC
36.3024905233
301PhosphorylationKISDFGTSKELSDKS
EHHHCCCCHHHCCCC
25.2224905233
305PhosphorylationFGTSKELSDKSTKMS
CCCCHHHCCCCCCCC
44.0524905233
308PhosphorylationSKELSDKSTKMSFAG
CHHHCCCCCCCCHHH
37.9524905233
309PhosphorylationKELSDKSTKMSFAGT
HHHCCCCCCCCHHHH
36.1824905233
312PhosphorylationSDKSTKMSFAGTVAW
CCCCCCCCHHHHHHH
17.3228348404
365PhosphorylationSSAIIWGVGSNSLHL
CCCEEEEECCCCEEC
4.5832142685
399PhosphorylationSKPRNRPSFRQTLMH
CCCCCCHHHHHHHHH
29.8023607784
403PhosphorylationNRPSFRQTLMHLDIA
CCHHHHHHHHHHHHH
23.0723607784
411PhosphorylationLMHLDIASADVLATP
HHHHHHHCCCCCCCC
25.9023607784
417PhosphorylationASADVLATPQETYFK
HCCCCCCCCHHHHCH
22.7323607784
421PhosphorylationVLATPQETYFKSQAE
CCCCCHHHHCHHHHH
29.0723607784
422PhosphorylationLATPQETYFKSQAEW
CCCCHHHHCHHHHHH
14.3023607784
474PhosphorylationDIREHYERKLERANN
HHHHHHHHHHHHHHH
41.5132142685
483PhosphorylationLERANNLYMELSAIM
HHHHHHHHHHHHHHH
7.23-
502AcetylationMREKELIKREQAVEK
HHHHHHHHHHHHHHH
63.6120167786
511PhosphorylationEQAVEKKYPGTYKRH
HHHHHHHCCCCCCCC
20.26-
541"N6,N6-dimethyllysine"KRKGVPHKSGMQTKR
HHHCCCCCCCCCCCC
42.51-
541MethylationKRKGVPHKSGMQTKR
HHHCCCCCCCCCCCC
42.51-
565PhosphorylationPTTEVAPTASPLSGS
CCCCCCCCCCCCCCC
29.9927732954
567PhosphorylationTEVAPTASPLSGSPK
CCCCCCCCCCCCCCC
28.9327732954
570PhosphorylationAPTASPLSGSPKMST
CCCCCCCCCCCCCCC
40.3826657352
572PhosphorylationTASPLSGSPKMSTSS
CCCCCCCCCCCCCCC
20.2626657352
578PhosphorylationGSPKMSTSSSKSRYR
CCCCCCCCCCCHHCC
25.88-
579PhosphorylationSPKMSTSSSKSRYRS
CCCCCCCCCCHHCCC
41.70-
672PhosphorylationTCANNLRYFGPAAAL
HHHHHCHHCCCHHHH
18.9623312004
681PhosphorylationGPAAALRSPLSNHAQ
CCHHHHHCCCCHHHH
30.9232142685
684PhosphorylationAALRSPLSNHAQRQL
HHHHCCCCHHHHHHC
29.9223312004
694PhosphorylationAQRQLPGSSPDLIST
HHHHCCCCCHHHHHH
36.4428348404
695PhosphorylationQRQLPGSSPDLISTA
HHHCCCCCHHHHHHH
28.4828348404
789PhosphorylationSGCRSESSLGTSHLG
CCCCCCCCCCCCCCC
27.11-
797PhosphorylationLGTSHLGTPPALPRK
CCCCCCCCCCCCCCC
32.2428348404
811PhosphorylationKTRPLQKSGDDSSEE
CCCCCCCCCCCCCCC
34.20-
892PhosphorylationLDDLLSQTPEIPIDI
HHHHHHCCCCCCCCC
21.3628348404
900PhosphorylationPEIPIDISSHSDGLS
CCCCCCCCCCCCCCC
20.4628348404
901PhosphorylationEIPIDISSHSDGLSD
CCCCCCCCCCCCCCC
27.6128348404
903PhosphorylationPIDISSHSDGLSDKE
CCCCCCCCCCCCCHH
35.0128348404
907PhosphorylationSSHSDGLSDKECAVR
CCCCCCCCCHHHHHH
52.7628348404
921PhosphorylationRRVKTQMSLGKLCVE
HHHHHHHHHCCHHHH
24.9327251275

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of M3K13_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M3K13_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of M3K13_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRDX3_HUMANPRDX3physical
12492477
M3K13_HUMANMAP3K13physical
11163770
MP2K7_HUMANMAP2K7physical
11726277
STAT3_HUMANSTAT3physical
21988832
H2A2C_HUMANHIST2H2ACphysical
28514442
SHIP2_HUMANINPPL1physical
28514442
KLH20_HUMANKLHL20physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of M3K13_HUMAN

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Related Literatures of Post-Translational Modification

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