UBA7_HUMAN - dbPTM
UBA7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBA7_HUMAN
UniProt AC P41226
Protein Name Ubiquitin-like modifier-activating enzyme 7
Gene Name UBA7
Organism Homo sapiens (Human).
Sequence Length 1012
Subcellular Localization
Protein Description Activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein..
Protein Sequence MDALDASKLLDEELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHTGDITEDLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLFCDFGEDFTVQDPTEAEPLTAAIQHISQGSPGILTLRKGANTHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGDTTTFSRYLRGGAITEVKRPKTVRHKSLDTALLQPHVVAQSSQEVHHAHCLHQAFCALHKFQHLHGRPPQPWDPVDAETVVGLARDLEPLKRTEEEPLEEPLDEALVRTVALSSAGVLSPMVAMLGAVAAQEVLKAISRKFMPLDQWLYFDALDCLPEDGELLPSPEDCALRGSRYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVIPLTYPLDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMPHVTEAYRAPASAAASEDAPYPVCTVRYFPSTAEHTLQWARHEFEELFRLSAETINHHQQAHTSLADMDEPQTLTLLKPVLGVLRVRPQNWQDCVAWALGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQDTHLLYVLAAANLYAQMHGLPGSQDWTALRELLKLLPQPDPQQMAPIFASNLELASASAEFGPEQQKELNKALEVWSVGPPLKPLMFEKDDDSNFHVDFVVAAASLRCQNYGIPPVNRAQSKRIVGQIIPAIATTTAAVAGLLGLELYKVVSGPRPRSAFRHSYLHLAENYLIRYMPFAPAIQTFHHLKWTSWDRLKVPAGQPERTLESLLAHLQEQHGLRVRILLHGSALLYAAGWSPEKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCEGDDEDTAFPPLHYEL
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
8UbiquitinationMDALDASKLLDEELY
CCCCHHHHHCCHHHH		55.58-
15PhosphorylationKLLDEELYSRQLYVL
HHCCHHHHHCCCHHH		12.7023532336
16PhosphorylationLLDEELYSRQLYVLG
HCCHHHHHCCCHHHC		26.6124719451
20PhosphorylationELYSRQLYVLGSPAM
HHHHCCCHHHCCHHH		5.8127642862
24PhosphorylationRQLYVLGSPAMQRIQ
CCCHHHCCHHHHHHC		12.8130108239
134UbiquitinationAKLEEQLKVGTLCHK
HHHHHHHCHHCCHHH		38.0129967540
196UbiquitinationPGILTLRKGANTHYF
CCEEEEECCCCCEEE		66.5422505724
241PhosphorylationGSLEIGDTTTFSRYL
CCEEECCCCCCHHHH		23.6324043423
242PhosphorylationSLEIGDTTTFSRYLR
CEEECCCCCCHHHHC		30.5024043423
243PhosphorylationLEIGDTTTFSRYLRG
EEECCCCCCHHHHCC		23.0024043423
245PhosphorylationIGDTTTFSRYLRGGA
ECCCCCCHHHHCCCC		20.2324043423
257UbiquitinationGGAITEVKRPKTVRH
CCCCCEECCCCCCCC		57.6729967540
266PhosphorylationPKTVRHKSLDTALLQ
CCCCCCCCHHHHHHC		25.9228397838
330UbiquitinationARDLEPLKRTEEEPL
HHCCCCCCCCCCCCC		68.91-
429UbiquitinationFGAGFQEKLRRQHYL
ECCCHHHHHHHCCEE		36.19-
461PhosphorylationVGLGAGNSGGLTVVD
HCCCCCCCCCEEEEE		33.0629978859
465PhosphorylationAGNSGGLTVVDMDHI
CCCCCCEEEEECCHH		23.0429978859
475PhosphorylationDMDHIERSNLSRQFL
ECCHHHCCCCCHHHH		29.3629978859
478PhosphorylationHIERSNLSRQFLFRS
HHHCCCCCHHHHHCC		28.4329978859
485PhosphorylationSRQFLFRSQDVGRPK
CHHHHHCCCCCCCCH		24.3327251275
492UbiquitinationSQDVGRPKAEVAAAA
CCCCCCCHHHHHHHH		56.68-
514PhosphorylationLQVIPLTYPLDPTTE
CEEEECCCCCCCCCC		14.96-
524PhosphorylationDPTTEHIYGDNFFSR
CCCCCCCCCCCHHHC		21.97-
547PhosphorylationDSFQARRYVAARCTH
HHHHHHHHHHHHHHH		6.7329052541
553PhosphorylationRYVAARCTHYLKPLL
HHHHHHHHHHHHHHH		14.1729052541
555PhosphorylationVAARCTHYLKPLLEA
HHHHHHHHHHHHHHC		9.7729052541
696UbiquitinationLRHFPPNKVLEDGTP
HHHCCCCCCCCCCCC		54.7129967540
771PhosphorylationQMAPIFASNLELASA
HCHHHHHHHHHHHHH		31.0627251275
777PhosphorylationASNLELASASAEFGP
HHHHHHHHHHHHHCH		35.0727251275
879PhosphorylationVSGPRPRSAFRHSYL
HCCCCCCHHHHHHHH		34.15-
884PhosphorylationPRSAFRHSYLHLAEN
CCHHHHHHHHHHHHH		25.7430108239
885PhosphorylationRSAFRHSYLHLAENY
CHHHHHHHHHHHHHH		7.6330108239
892PhosphorylationYLHLAENYLIRYMPF
HHHHHHHHHHHHCCC		8.6019835603
896PhosphorylationAENYLIRYMPFAPAI
HHHHHHHHCCCHHHH		11.3519835603
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 UBA7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBA7_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 UBA7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ISG15_HUMANISG15physical
16189514
ISG15_HUMANISG15physical
22693631
ISG15_HUMANISG15physical
25416956
UB2L6_HUMANUBE2L6physical
19250909
UB2L3_HUMANUBE2L3physical
19250909
UB2E1_HUMANUBE2E1physical
16428300
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 UBA7_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory