P33MX_HUMAN - dbPTM
P33MX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P33MX_HUMAN
UniProt AC Q96A73
Protein Name Putative monooxygenase p33MONOX
Gene Name KIAA1191
Organism Homo sapiens (Human).
Sequence Length 305
Subcellular Localization Cytoplasm.
Protein Description Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth..
Protein Sequence MASRQPEVPALEASAPLGKMSLPIGIYRRAVSYDDTLEDPAPMTPPPSDMGSVPWKPVIPERKYQHLAKVEEGEASLPSPAMTLSSAIDSVDKVPVVKAKATHVIMNSLITKQTQESIQHFERQAGLRDAGYTPHKGLTTEETKYLRVAEALHKLKLQSGEVTKEERQPASAQSTPSTTPHSSPKQRPRGWFTSGSSTALPGPNPSTMDSGSGDKDRNLSDKWSLFGPRSLQKYDSGSFATQAYRGAQKPSPLELIRAQANRMAEDPAALKPPKMDIPVMEGKKQPPRAHNLKPRDLNVLTPTGF
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
14PhosphorylationEVPALEASAPLGKMS
CCCCCCCCCCCCCCC		22.5020068231
21PhosphorylationSAPLGKMSLPIGIYR
CCCCCCCCCCCEEEE		34.1820068231
27PhosphorylationMSLPIGIYRRAVSYD
CCCCCEEEEECCCCC		6.7125106551
32PhosphorylationGIYRRAVSYDDTLED
EEEEECCCCCCCCCC		23.1220068231
33PhosphorylationIYRRAVSYDDTLEDP
EEEECCCCCCCCCCC		15.9629449344
36PhosphorylationRAVSYDDTLEDPAPM
ECCCCCCCCCCCCCC		29.2020068231
44PhosphorylationLEDPAPMTPPPSDMG
CCCCCCCCCCCCCCC		31.4227050516
48PhosphorylationAPMTPPPSDMGSVPW
CCCCCCCCCCCCCCC		46.1028102081
79PhosphorylationEGEASLPSPAMTLSS
HCCCCCCCCCCCHHH		30.5028857561
117PhosphorylationITKQTQESIQHFERQ
HHHHHHHHHHHHHHH		20.1028857561
132PhosphorylationAGLRDAGYTPHKGLT
HCCCCCCCCCCCCCC		20.8628796482
133PhosphorylationGLRDAGYTPHKGLTT
CCCCCCCCCCCCCCH		20.2828796482
136MethylationDAGYTPHKGLTTEET
CCCCCCCCCCCHHHH		57.74115972007
144UbiquitinationGLTTEETKYLRVAEA
CCCHHHHHHHHHHHH		45.63-
159PhosphorylationLHKLKLQSGEVTKEE
HHHHHCCCCCCCHHH		47.5626074081
163PhosphorylationKLQSGEVTKEERQPA
HCCCCCCCHHHCCCC		28.5626074081
171PhosphorylationKEERQPASAQSTPST
HHHCCCCCCCCCCCC		33.2623927012
174PhosphorylationRQPASAQSTPSTTPH
CCCCCCCCCCCCCCC		41.8423927012
175PhosphorylationQPASAQSTPSTTPHS
CCCCCCCCCCCCCCC		14.8023927012
177PhosphorylationASAQSTPSTTPHSSP
CCCCCCCCCCCCCCC		45.0323927012
178PhosphorylationSAQSTPSTTPHSSPK
CCCCCCCCCCCCCCC		45.6230266825
179PhosphorylationAQSTPSTTPHSSPKQ
CCCCCCCCCCCCCCC		24.2830266825
182PhosphorylationTPSTTPHSSPKQRPR
CCCCCCCCCCCCCCC		49.9223927012
183PhosphorylationPSTTPHSSPKQRPRG
CCCCCCCCCCCCCCC		32.8420201521
220PhosphorylationGDKDRNLSDKWSLFG
CCCCCCCCHHCCCCC		40.4728857561
224PhosphorylationRNLSDKWSLFGPRSL
CCCCHHCCCCCCHHH		21.4028857561
234PhosphorylationGPRSLQKYDSGSFAT
CCHHHHCCCCCCCHH		11.4630631047
236PhosphorylationRSLQKYDSGSFATQA
HHHHCCCCCCCHHHH		32.9928555341
238PhosphorylationLQKYDSGSFATQAYR
HHCCCCCCCHHHHHC		18.7028857561
244PhosphorylationGSFATQAYRGAQKPS
CCCHHHHHCCCCCCC		10.36-
245MethylationSFATQAYRGAQKPSP
CCHHHHHCCCCCCCH		36.67115481037
251PhosphorylationYRGAQKPSPLELIRA
HCCCCCCCHHHHHHH		49.5025159151
301PhosphorylationPRDLNVLTPTGF---
CCCCCCCCCCCC---		17.9624719451
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 P33MX_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P33MX_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 P33MX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
HSP7C_HUMANHSPA8physical
26186194
HSP76_HUMANHSPA6physical
26186194
CARM1_HUMANCARM1physical
26186194
CARM1_HUMANCARM1physical
28514442
GRP75_HUMANHSPA9physical
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 P33MX_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; THR-178; THR-179;SER-182 AND SER-183, AND MASS SPECTROMETRY.

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