MA2B2_HUMAN - dbPTM
MA2B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MA2B2_HUMAN
UniProt AC Q9Y2E5
Protein Name Epididymis-specific alpha-mannosidase
Gene Name MAN2B2
Organism Homo sapiens (Human).
Sequence Length 1009
Subcellular Localization Secreted .
Protein Description
Protein Sequence MGQLCWLPLLAPLLLLRPPGVQSAGPIRAFVVPHSHMDVGWVYTVQESMRAYAANVYTSVVEELARGQQRRFIAVEQEFFRLWWDGVASDQQKYQVRQLLEEGRLEFVIGGQVMHDEAVTHLDDQILQLTEGHGFLYETFGIRPQFSWHVDPFGASATTPTLFALAGFNAHLGSRIDYDLKAAMQEARGLQFVWRGSPSLSERQEIFTHIMDQYSYCTPSHIPFSNRSGFYWNGVAVFPKPPQDGVYPNMSEPVTPANINLYAEALVANVKQRAAWFRTPHVLWPWGCDKQFFNASVQFANMDPLLDHINSHAAELGVSVQYATLGDYFRALHALNVTWRVRDHHDFLPYSTEPFQAWTGFYTSRSSLKGLARRASALLYAGESMFTRYLWPAPRGHLDPTWALQQLQQLRWAVSEVQHHDAITGTESPKVRDMYATHLASGMLGMRKLMASIVLDELQPQAPMAASSDAGPAGHFASVYNPLAWTVTTIVTLTVGFPGVRVTDEAGHPVPSQIQNSTETPSAYDLLILTTIPGLSYRHYNIRPTAGAQEGTQEPAATVASTLQFGRRLRRRTSHAGRYLVPVANDCYIVLLDQDTNLMHSIWERQSNRTVRVTQEFLEYHVNGDVKQGPISDNYLFTPGKAAVPAWEAVEMEIVAGQLVTEIRQYFYRNMTAQNYTYAIRSRLTHVPQGHDGELLCHRIEQEYQAGPLELNREAVLRTSTNLNSQQVIYSDNNGYQMQRRPYVSYVNNSIARNYYPMVQSAFMEDGKSRLVLLSERAHGISSQGNGQVEVMLHRRLWNNFDWDLGYNLTLNDTSVVHPVLWLLLGSWSLTTALRQRSALALQHRPVVLFGDLAGTAPKLPGPQQQEAVTLPPNLHLQILSIPGWRYSSNHTEHSQNLRKGHRGEAQADLRRVLLRLYHLYEVGEDPVLSQPVTVNLEAVLQALGSVVAVEERSLTGTWDLSMLHRWSWRTGPGRHRGDTTSPSRPPGGPIITVHPKEIRTFFIHFQQQ
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
35PhosphorylationRAFVVPHSHMDVGWV
EEEECCCCCCCCCEE		17.90-
93 (in isoform 2)Ubiquitination-31.8321906983
93 (in isoform 1)Ubiquitination-31.8321906983
93UbiquitinationGVASDQQKYQVRQLL
CCCCHHHHHHHHHHH		31.8321906983
181 (in isoform 2)Ubiquitination-31.0721906983
181 (in isoform 1)Ubiquitination-31.0721906983
181UbiquitinationSRIDYDLKAAMQEAR
CCCCHHHHHHHHHHH		31.072190698
199PhosphorylationFVWRGSPSLSERQEI
EEECCCCCHHHHHHH		46.3421712546
225PhosphorylationTPSHIPFSNRSGFYW
CCCCCCCCCCCCCCC		26.44-
226N-linked_GlycosylationPSHIPFSNRSGFYWN
CCCCCCCCCCCCCCC		42.38UniProtKB CARBOHYD
249N-linked_GlycosylationPQDGVYPNMSEPVTP
CCCCCCCCCCCCCCH		29.00UniProtKB CARBOHYD
294N-linked_GlycosylationGCDKQFFNASVQFAN
CCCHHHHCEEEEECC		32.37UniProtKB CARBOHYD
336N-linked_GlycosylationFRALHALNVTWRVRD
HHHHHHHCCEEEECC		29.92UniProtKB CARBOHYD
435PhosphorylationSPKVRDMYATHLASG
CHHHHHHHHHHHHHC		16.79-
437PhosphorylationKVRDMYATHLASGML
HHHHHHHHHHHHCCH		10.43-
516N-linked_GlycosylationPVPSQIQNSTETPSA
CCCHHCCCCCCCCCH		53.1519159218
608N-linked_GlycosylationSIWERQSNRTVRVTQ
HHHHHHCCCEEEEEH		34.99UniProtKB CARBOHYD
670N-linked_GlycosylationIRQYFYRNMTAQNYT
HHHHHHHHCCCCCHH		22.30UniProtKB CARBOHYD
675N-linked_GlycosylationYRNMTAQNYTYAIRS
HHHCCCCCHHEEHHH		28.75UniProtKB CARBOHYD
677PhosphorylationNMTAQNYTYAIRSRL
HCCCCCHHEEHHHCC		17.6428851738
748N-linked_GlycosylationRPYVSYVNNSIARNY
CCCEEECCCHHHHHC		28.44UniProtKB CARBOHYD
755PhosphorylationNNSIARNYYPMVQSA
CCHHHHHCHHHHHHH		11.9129978859
756PhosphorylationNSIARNYYPMVQSAF
CHHHHHCHHHHHHHC		6.6029978859
761PhosphorylationNYYPMVQSAFMEDGK
HCHHHHHHHCCCCCC		16.4429978859
768UbiquitinationSAFMEDGKSRLVLLS
HHCCCCCCEEEEEEE		44.73-
769PhosphorylationAFMEDGKSRLVLLSE
HCCCCCCEEEEEEEE		36.0529978859
783PhosphorylationERAHGISSQGNGQVE
ECCCCCCCCCCCEEE		39.9422210691
808N-linked_GlycosylationFDWDLGYNLTLNDTS
CCCCCCCCEECCCCC		25.42UniProtKB CARBOHYD
812N-linked_GlycosylationLGYNLTLNDTSVVHP
CCCCEECCCCCHHHH		45.32UniProtKB CARBOHYD
856PhosphorylationLFGDLAGTAPKLPGP
EECCCCCCCCCCCCH		33.8918785766
890N-linked_GlycosylationPGWRYSSNHTEHSQN
CCCCCCCCCHHHHCH		39.91UniProtKB CARBOHYD
984O-linked_GlycosylationRGDTTSPSRPPGGPI
CCCCCCCCCCCCCCE		58.13OGP
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 MA2B2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MA2B2_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 MA2B2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MA2B2_HUMAN !!
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 MA2B2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-516, AND MASSSPECTROMETRY.

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