HERC4_HUMAN - dbPTM
HERC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HERC4_HUMAN
UniProt AC Q5GLZ8
Protein Name Probable E3 ubiquitin-protein ligase HERC4
Gene Name HERC4
Organism Homo sapiens (Human).
Sequence Length 1057
Subcellular Localization Cytoplasm, cytosol . shows a punctate cytoplasmic distribution.
Protein Description Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates..
Protein Sequence MLCWGNASFGQLGLGGIDEEIVLEPRKSDFFINKRVRDVGCGLRHTVFVLDDGTVYTCGCNDLGQLGHEKSRKKPEQVVALDAQNIVAVSCGEAHTLALNDKGQVYAWGLDSDGQLGLVGSEECIRVPRNIKSLSDIQIVQVACGYYHSLALSKASEVFCWGQNKYGQLGLGTDCKKQTSPQLLKSLLGIPFMQVAAGGAHSFVLTLSGAIFGWGRNKFGQLGLNDENDRYVPNLLKSLRSQKIVYICCGEDHTAALTKEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGSIVTEIACGRQHTSAFVPSSGRIYSFGLGGNGQLGTGSTSNRKSPFTVKGNWYPYNGQCLPDIDSEEYFCVKRIFSGGDQSFSHYSSPQNCGPPDDFRCPNPTKQIWTVNEALIQKWLSYPSGRFPVEIANEIDGTFSSSGCLNGSFLAVSNDDHYRTGTRFSGVDMNAARLLFHKLIQPDHPQISQQVAASLEKNLIPKLTSSLPDVEALRFYLTLPECPLMSDSNNFTTIAIPFGTALVNLEKAPLKVLENWWSVLEPPLFLKIVELFKEVVVHLLKLYKIGIPPSERRIFNSFLHTALKVLEILHRVNEKMGQIIQYDKFYIHEVQELIDIRNDYINWVQQQAYGMDVNHGLTELADIPVTICTYPFVFDAQAKTTLLQTDAVLQMQMAIDQAHRQNVSSLFLPVIESVNPCLILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIWFSDKTFEDSDLFHLIGVICGLAIYNCTIVDLHFPLALYKKLLKKKPSLDDLKELMPDVGRSMQQLLDYPEDDIEETFCLNFTITVENFGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSLKLVIQSTGGGEEYLPVSHTCFNLLDLPKYTEKETLRSKLIQAIDHNEGFSLI
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
27UbiquitinationEIVLEPRKSDFFINK
EEEECCCCCCCEECC		66.16-
342-HydroxyisobutyrylationKSDFFINKRVRDVGC
CCCCEECCHHHCCCC		47.67-
34UbiquitinationKSDFFINKRVRDVGC
CCCCEECCHHHCCCC		47.67-
70UbiquitinationLGQLGHEKSRKKPEQ
HHHCCCHHHCCCCHH		50.30-
108 (in isoform 6)Ubiquitination-7.0921890473
146PhosphorylationIVQVACGYYHSLALS
HHHHHHCHHHHHHHH		9.6325884760
147PhosphorylationVQVACGYYHSLALSK
HHHHHCHHHHHHHHC		3.1125884760
165UbiquitinationVFCWGQNKYGQLGLG
EEEECCCCCCCCCCC		42.76-
176UbiquitinationLGLGTDCKKQTSPQL
CCCCCCCCCCCCHHH		51.21-
177UbiquitinationGLGTDCKKQTSPQLL
CCCCCCCCCCCHHHH		66.20-
180PhosphorylationTDCKKQTSPQLLKSL
CCCCCCCCHHHHHHH		14.2525159151
218UbiquitinationIFGWGRNKFGQLGLN
HHCCCCCCCCCCCCC		49.8921906983
218 (in isoform 2)Ubiquitination-49.8921890473
218 (in isoform 1)Ubiquitination-49.8921890473
218 (in isoform 3)Ubiquitination-49.8921890473
237 (in isoform 2)Ubiquitination-51.08-
237UbiquitinationRYVPNLLKSLRSQKI
CCHHHHHHHHCCCCE		51.08-
243UbiquitinationLKSLRSQKIVYICCG
HHHHCCCCEEEEEEC		35.07-
246PhosphorylationLRSQKIVYICCGEDH
HCCCCEEEEEECCCC		7.54-
318PhosphorylationPSSGRIYSFGLGGNG
CCCCCEEEEECCCCC		15.5125690035
331PhosphorylationNGQLGTGSTSNRKSP
CCCCCCCCCCCCCCC		28.6225690035
332PhosphorylationGQLGTGSTSNRKSPF
CCCCCCCCCCCCCCC		31.2225690035
336UbiquitinationTGSTSNRKSPFTVKG
CCCCCCCCCCCEEEC		67.73-
342UbiquitinationRKSPFTVKGNWYPYN
CCCCCEEECCEECCC		43.39-
359 (in isoform 6)Ubiquitination-53.6321890473
365UbiquitinationSEEYFCVKRIFSGGD
CCCEEEEEEEECCCC		40.74-
378 (in isoform 6)Ubiquitination-15.0521890473
379PhosphorylationDQSFSHYSSPQNCGP
CCCCCCCCCCCCCCC		30.0725627689
380PhosphorylationQSFSHYSSPQNCGPP
CCCCCCCCCCCCCCC		24.2825627689
383 (in isoform 6)Ubiquitination-35.7821890473
397UbiquitinationFRCPNPTKQIWTVNE
CCCCCCCCEEEECCH		40.83-
409UbiquitinationVNEALIQKWLSYPSG
CCHHHHHHHHCCCCC		43.01-
460SulfoxidationTRFSGVDMNAARLLF
CCCCCCCCHHHHHHH		3.2330846556
469 (in isoform 2)Ubiquitination-39.6921890473
469UbiquitinationAARLLFHKLIQPDHP
HHHHHHHHHHCCCCH		39.6921890473
469 (in isoform 1)Ubiquitination-39.6921890473
469 (in isoform 3)Ubiquitination-39.6921890473
488 (in isoform 3)Ubiquitination-63.4521890473
488 (in isoform 1)Ubiquitination-63.4521890473
488 (in isoform 2)Ubiquitination-63.4521890473
488UbiquitinationQVAASLEKNLIPKLT
HHHHHHHHCCHHHHH		63.4521890473
493 (in isoform 2)Ubiquitination-58.3621890473
493 (in isoform 1)Ubiquitination-58.3621890473
493 (in isoform 3)Ubiquitination-58.3621890473
493UbiquitinationLEKNLIPKLTSSLPD
HHHCCHHHHHCCCCC		58.3621890473
572UbiquitinationEVVVHLLKLYKIGIP
HHHHHHHHHHHCCCC		57.01-
606UbiquitinationILHRVNEKMGQIIQY
HHHHHHHHHHHHEEE		43.03-
671PhosphorylationVFDAQAKTTLLQTDA
ECCCCCCHHHHHHHH		26.2024043423
672PhosphorylationFDAQAKTTLLQTDAV
CCCCCCHHHHHHHHH		25.4324043423
676PhosphorylationAKTTLLQTDAVLQMQ
CCHHHHHHHHHHHHH		26.3724043423
723SulfoxidationENIVGDAMEVLRKTK
CCCHHHHHHHHHHCC		4.3321406390
730UbiquitinationMEVLRKTKNIDYKKP
HHHHHHCCCCCCCCC		55.74-
769UbiquitinationMRELLDPKYGMFRYY
HHHHHCCCCCCEEEE		54.85-
780 (in isoform 6)Ubiquitination-42.3821890473
812 (in isoform 3)Ubiquitination-3.2721890473
827UbiquitinationLYKKLLKKKPSLDDL
HHHHHHHCCCCHHHH		70.64-
828UbiquitinationYKKLLKKKPSLDDLK
HHHHHHCCCCHHHHH		37.95-
830PhosphorylationKLLKKKPSLDDLKEL
HHHHCCCCHHHHHHH		54.0017287340
835UbiquitinationKPSLDDLKELMPDVG
CCCHHHHHHHCHHHH		56.66-
838SulfoxidationLDDLKELMPDVGRSM
HHHHHHHCHHHHHHH		2.5330846556
844PhosphorylationLMPDVGRSMQQLLDY
HCHHHHHHHHHHHCC		18.2724043423
851PhosphorylationSMQQLLDYPEDDIEE
HHHHHHCCCHHCCCC		14.4324043423
859PhosphorylationPEDDIEETFCLNFTI
CHHCCCCEEEEEEEE		13.5824043423
865PhosphorylationETFCLNFTITVENFG
CEEEEEEEEEEECCC		18.0524043423
867PhosphorylationFCLNFTITVENFGAT
EEEEEEEEEECCCCC		20.7920068231
874PhosphorylationTVENFGATEVKELVL
EEECCCCCCHHHHHH		41.5120068231
882 (in isoform 2)Ubiquitination-35.8121890473
886PhosphorylationLVLNGADTAVNKQNR
HHHCCCCCCCCHHHH		31.78-
890 (in isoform 1)Ubiquitination-42.2121890473
890UbiquitinationGADTAVNKQNRQEFV
CCCCCCCHHHHHHHH		42.2121890473
922UbiquitinationAFHAGFHKVCGGKVL
HHHCHHHHHHCCEEE		36.64-
954UbiquitinationYDWKELEKNTEYKGE
CCHHHHHHCCCCCCC		80.11-
959UbiquitinationLEKNTEYKGEYWAEH
HHHCCCCCCCCHHCC		38.75-
992PhosphorylationKQFLLFLTGSDRIPI
CCEEEEEECCCCCEE		27.57-
1003UbiquitinationRIPILGMKSLKLVIQ
CCEECCCCEEEEEEE		51.33-
1004PhosphorylationIPILGMKSLKLVIQS
CEECCCCEEEEEEEC		23.1121712546
1006UbiquitinationILGMKSLKLVIQSTG
ECCCCEEEEEEECCC		48.04-
1018PhosphorylationSTGGGEEYLPVSHTC
CCCCCCCEEEEECEE		16.4121712546
1024PhosphorylationEYLPVSHTCFNLLDL
CEEEEECEEEHHHCC		15.9921712546
1033UbiquitinationFNLLDLPKYTEKETL
EHHHCCCCCCCHHHH		72.59-
1037UbiquitinationDLPKYTEKETLRSKL
CCCCCCCHHHHHHHH		48.47-
1043UbiquitinationEKETLRSKLIQAIDH
CHHHHHHHHHHHHHC		43.08-
1055PhosphorylationIDHNEGFSLI-----
HHCCCCCCCC-----		35.69-
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 HERC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HERC4_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 HERC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HERC4_HUMANHERC4physical
22496338
UBC_HUMANUBCphysical
22496338
UB2D2_HUMANUBE2D2physical
22496338
UB2E3_HUMANUBE2E3physical
22496338
UB2J2_HUMANUBE2J2physical
22496338
NUBP2_HUMANNUBP2physical
22863883
RD23A_HUMANRAD23Aphysical
22863883
HERC4_HUMANHERC4physical
26949039
UB2L3_HUMANUBE2L3physical
26949039
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 HERC4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830, AND MASSSPECTROMETRY.

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