MARH7_HUMAN - dbPTM
MARH7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARH7_HUMAN
UniProt AC Q9H992
Protein Name E3 ubiquitin-protein ligase MARCH7
Gene Name 7-Mar
Organism Homo sapiens (Human).
Sequence Length 704
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates..
Protein Sequence MESKPSRIPRRISVQPSSSLSARMMSGSRGSSLNDTYHSRDSSFRLDSEYQSTSASASASPFQSAWYSESEITQGARSRSQNQQRDHDSKRPKLSCTNCTTSAGRNVGNGLNTLSDSSWRHSQVPRSSSMVLGSFGTDLMRERRDLERRTDSSISNLMDYSHRSGDFTTSSYVQDRVPSYSQGARPKENSMSTLQLNTSSTNHQLPSEHQTILSSRDSRNSLRSNFSSRESESSRSNTQPGFSYSSSRDEAPIISNSERVVSSQRPFQESSDNEGRRTTRRLLSRIASSMSSTFFSRRSSQDSLNTRSLNSENSYVSPRILTASQSRSNVPSASEVPDNRASEASQGFRFLRRRWGLSSLSHNHSSESDSENFNQESEGRNTGPWLSSSLRNRCTPLFSRRRREGRDESSRIPTSDTSSRSHIFRRESNEVVHLEAQNDPLGAAANRPQASAASSSATTGGSTSDSAQGGRNTGISGILPGSLFRFAVPPALGSNLTDNVMITVDIIPSGWNSADGKSDKTKSAPSRDPERLQKIKESLLLEDSEEEEGDLCRICQMAAASSSNLLIEPCKCTGSLQYVHQDCMKKWLQAKINSGSSLEAVTTCELCKEKLELNLEDFDIHELHRAHANEQAEYEFISSGLYLVVLLHLCEQSFSDMMGNTNEPSTRVRFINLARTLQAHMEDLETSEDDSEEDGDHNRTFDIA
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
1Acetylation-------MESKPSRI
-------CCCCCCCC
13.6522814378
3Phosphorylation-----MESKPSRIPR
-----CCCCCCCCCC
48.8728152594
4Ubiquitination----MESKPSRIPRR
----CCCCCCCCCCC
33.43-
6Phosphorylation--MESKPSRIPRRIS
--CCCCCCCCCCCCE
46.7217081983
13PhosphorylationSRIPRRISVQPSSSL
CCCCCCCEECCCCHH
16.9429978859
17PhosphorylationRRISVQPSSSLSARM
CCCEECCCCHHHHHH
18.5727732954
18PhosphorylationRISVQPSSSLSARMM
CCEECCCCHHHHHHH
41.8227732954
19PhosphorylationISVQPSSSLSARMMS
CEECCCCHHHHHHHC
30.5927732954
21PhosphorylationVQPSSSLSARMMSGS
ECCCCHHHHHHHCCC
18.7727732954
26PhosphorylationSLSARMMSGSRGSSL
HHHHHHHCCCCCCCC
25.0330576142
28PhosphorylationSARMMSGSRGSSLND
HHHHHCCCCCCCCCC
26.5930622161
29MethylationARMMSGSRGSSLNDT
HHHHCCCCCCCCCCC
53.16115482579
31PhosphorylationMMSGSRGSSLNDTYH
HHCCCCCCCCCCCCC
30.4626434776
32PhosphorylationMSGSRGSSLNDTYHS
HCCCCCCCCCCCCCC
33.7328857561
36PhosphorylationRGSSLNDTYHSRDSS
CCCCCCCCCCCCCCC
23.2828152594
37PhosphorylationGSSLNDTYHSRDSSF
CCCCCCCCCCCCCCC
10.7228152594
39PhosphorylationSLNDTYHSRDSSFRL
CCCCCCCCCCCCCCC
27.6328152594
50PhosphorylationSFRLDSEYQSTSASA
CCCCCCCHHCCCCCC
16.2430576142
53PhosphorylationLDSEYQSTSASASAS
CCCCHHCCCCCCCCC
16.8830576142
55UbiquitinationSEYQSTSASASASPF
CCHHCCCCCCCCCCC
14.81-
56PhosphorylationEYQSTSASASASPFQ
CHHCCCCCCCCCCCC
23.6430576142
93UbiquitinationDHDSKRPKLSCTNCT
CCCCCCCCCCCCCCC
58.00-
102PhosphorylationSCTNCTTSAGRNVGN
CCCCCCCCCCCCCCC
15.57-
127PhosphorylationRHSQVPRSSSMVLGS
CCCCCCCHHHHHHHH
22.2428857561
128PhosphorylationHSQVPRSSSMVLGSF
CCCCCCHHHHHHHHH
24.5928857561
129PhosphorylationSQVPRSSSMVLGSFG
CCCCCHHHHHHHHHH
17.7328857561
134PhosphorylationSSSMVLGSFGTDLMR
HHHHHHHHHHHHHHH
19.1524719451
137PhosphorylationMVLGSFGTDLMRERR
HHHHHHHHHHHHHHH
24.7724719451
150PhosphorylationRRDLERRTDSSISNL
HHHHHHHCCCHHHHH
46.5923312004
152PhosphorylationDLERRTDSSISNLMD
HHHHHCCCHHHHHHH
29.0323312004
153PhosphorylationLERRTDSSISNLMDY
HHHHCCCHHHHHHHH
32.6123312004
155PhosphorylationRRTDSSISNLMDYSH
HHCCCHHHHHHHHCC
26.3423312004
160PhosphorylationSISNLMDYSHRSGDF
HHHHHHHHCCCCCCC
7.7527642862
171PhosphorylationSGDFTTSSYVQDRVP
CCCCCCCHHHHHCCC
27.5128555341
172PhosphorylationGDFTTSSYVQDRVPS
CCCCCCHHHHHCCCC
11.2527642862
179PhosphorylationYVQDRVPSYSQGARP
HHHHCCCCCCCCCCC
34.2627642862
214PhosphorylationSEHQTILSSRDSRNS
CCHHHHHCCHHHHHH
21.3424719451
215PhosphorylationEHQTILSSRDSRNSL
CHHHHHCCHHHHHHH
36.3424719451
218PhosphorylationTILSSRDSRNSLRSN
HHHCCHHHHHHHHHH
32.05-
221PhosphorylationSSRDSRNSLRSNFSS
CCHHHHHHHHHHCCC
24.8526437602
238PhosphorylationSESSRSNTQPGFSYS
CHHCCCCCCCCCCCC
37.0722817900
243PhosphorylationSNTQPGFSYSSSRDE
CCCCCCCCCCCCCCC
29.9822817900
245PhosphorylationTQPGFSYSSSRDEAP
CCCCCCCCCCCCCCC
22.1922817900
246PhosphorylationQPGFSYSSSRDEAPI
CCCCCCCCCCCCCCC
22.5928348404
247PhosphorylationPGFSYSSSRDEAPII
CCCCCCCCCCCCCCC
37.5028348404
270PhosphorylationSQRPFQESSDNEGRR
CCCCCCCCCCCHHHH
32.0123186163
271PhosphorylationQRPFQESSDNEGRRT
CCCCCCCCCCHHHHH
43.6430576142
284PhosphorylationRTTRRLLSRIASSMS
HHHHHHHHHHHHHHH
26.66-
288PhosphorylationRLLSRIASSMSSTFF
HHHHHHHHHHHHHHH
24.9723917254
289PhosphorylationLLSRIASSMSSTFFS
HHHHHHHHHHHHHHH
17.4223186163
296PhosphorylationSMSSTFFSRRSSQDS
HHHHHHHHCCCCCCC
23.6929759185
299PhosphorylationSTFFSRRSSQDSLNT
HHHHHCCCCCCCCCC
31.1026699800
300PhosphorylationTFFSRRSSQDSLNTR
HHHHCCCCCCCCCCC
35.8730576142
303PhosphorylationSRRSSQDSLNTRSLN
HCCCCCCCCCCCCCC
18.8423312004
314PhosphorylationRSLNSENSYVSPRIL
CCCCCCCCCCCHHHE
23.9028796482
315PhosphorylationSLNSENSYVSPRILT
CCCCCCCCCCHHHEE
19.2730183078
317PhosphorylationNSENSYVSPRILTAS
CCCCCCCCHHHEECC
10.5421712546
324PhosphorylationSPRILTASQSRSNVP
CHHHEECCCCCCCCC
24.37-
326PhosphorylationRILTASQSRSNVPSA
HHEECCCCCCCCCCH
34.8730576142
358PhosphorylationLRRRWGLSSLSHNHS
HHHHHCCHHCCCCCC
25.8726434776
359PhosphorylationRRRWGLSSLSHNHSS
HHHHCCHHCCCCCCC
38.6426434776
361PhosphorylationRWGLSSLSHNHSSES
HHCCHHCCCCCCCCC
24.9626434776
365PhosphorylationSSLSHNHSSESDSEN
HHCCCCCCCCCCCCC
40.9125850435
366PhosphorylationSLSHNHSSESDSENF
HCCCCCCCCCCCCCC
33.3030576142
368PhosphorylationSHNHSSESDSENFNQ
CCCCCCCCCCCCCCC
48.6725850435
370PhosphorylationNHSSESDSENFNQES
CCCCCCCCCCCCCCC
43.6625850435
377PhosphorylationSENFNQESEGRNTGP
CCCCCCCCCCCCCCH
35.2724719451
387PhosphorylationRNTGPWLSSSLRNRC
CCCCHHHCHHHHHCC
17.6323401153
388PhosphorylationNTGPWLSSSLRNRCT
CCCHHHCHHHHHCCH
31.0829978859
389PhosphorylationTGPWLSSSLRNRCTP
CCHHHCHHHHHCCHH
28.1529978859
395PhosphorylationSSLRNRCTPLFSRRR
HHHHHCCHHHHHHHH
21.5721712546
406MethylationSRRRREGRDESSRIP
HHHHHCCCCCCCCCC
39.5124377495
406DimethylationSRRRREGRDESSRIP
HHHHHCCCCCCCCCC
39.51-
428PhosphorylationSHIFRRESNEVVHLE
CEEEECCCCCEEEEE
36.16-
498UbiquitinationALGSNLTDNVMITVD
CCCCCCCCCEEEEEE
49.22-
522UbiquitinationDGKSDKTKSAPSRDP
CCCCCCCCCCCCCCH
50.81-
536UbiquitinationPERLQKIKESLLLED
HHHHHHHHHHHHCCC
48.57-
538PhosphorylationRLQKIKESLLLEDSE
HHHHHHHHHHCCCCC
21.2230624053
544PhosphorylationESLLLEDSEEEEGDL
HHHHCCCCCCCCCCH
37.2219664994
548UbiquitinationLEDSEEEEGDLCRIC
CCCCCCCCCCHHHHH
62.38-
553UbiquitinationEEEGDLCRICQMAAA
CCCCCHHHHHHHHHH
39.76-
561PhosphorylationICQMAAASSSNLLIE
HHHHHHHCCCCEEEE
29.5828348404
562PhosphorylationCQMAAASSSNLLIEP
HHHHHHCCCCEEEEE
20.6528348404
563PhosphorylationQMAAASSSNLLIEPC
HHHHHCCCCEEEEEC
29.0628348404
570UbiquitinationSNLLIEPCKCTGSLQ
CCEEEEECCCCCCCH
3.5221906983
572UbiquitinationLLIEPCKCTGSLQYV
EEEEECCCCCCCHHC
7.12-
585UbiquitinationYVHQDCMKKWLQAKI
HCCHHHHHHHHHHHH
47.32-
586UbiquitinationVHQDCMKKWLQAKIN
CCHHHHHHHHHHHHC
26.67-
591UbiquitinationMKKWLQAKINSGSSL
HHHHHHHHHCCCCCC
29.47-
597PhosphorylationAKINSGSSLEAVTTC
HHHCCCCCCHHHHHH
33.48-
608UbiquitinationVTTCELCKEKLELNL
HHHHHHHHHHHCCCH
71.1921906983
610UbiquitinationTCELCKEKLELNLED
HHHHHHHHHCCCHHH
32.53-
666PhosphorylationGNTNEPSTRVRFINL
CCCCCCHHHHHHHHH
43.8524719451
676PhosphorylationRFINLARTLQAHMED
HHHHHHHHHHHHHHH
20.0227732954
686PhosphorylationAHMEDLETSEDDSEE
HHHHHHHCCCCCCCC
44.7218669648
687PhosphorylationHMEDLETSEDDSEED
HHHHHHCCCCCCCCC
29.6518669648
691PhosphorylationLETSEDDSEEDGDHN
HHCCCCCCCCCCCCC
56.0328348404

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
-KUbiquitinationE3 ubiquitin ligaseMARCHF7Q9H992
PMID:18410486

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MARH7_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 MARH7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI65_HUMANTRIM65physical
22493164
UBC_HUMANUBCphysical
16868077
UB2D3_HUMANUBE2D3physical
24905733
UBC12_HUMANUBE2Mphysical
24905733
UBE2N_HUMANUBE2Nphysical
24905733
UB2D1_HUMANUBE2D1physical
24905733
PP2BA_HUMANPPP3CAphysical
24905733
PP2BB_HUMANPPP3CBphysical
24905733
MARH7_HUMANMARCH7physical
24905733
UB2D2_HUMANUBE2D2physical
24905733
UB2E1_HUMANUBE2E1physical
24905733
TAU_HUMANMAPTphysical
24905733
UBE2K_HUMANUBE2Kphysical
16868077
NLRP3_HUMANNLRP3physical
25594175
UBE2K_HUMANUBE2Kphysical
18410486
UBE2N_HUMANUBE2Nphysical
18410486
USP9X_HUMANUSP9Xphysical
18410486
UBP7_HUMANUSP7physical
18410486
IQCB1_HUMANIQCB1physical
28498859

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 MARH7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-686; SER-687 ANDSER-691, AND MASS SPECTROMETRY.

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