RN19B_HUMAN - dbPTM
RN19B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN19B_HUMAN
UniProt AC Q6ZMZ0
Protein Name E3 ubiquitin-protein ligase RNF19B
Gene Name RNF19B
Organism Homo sapiens (Human).
Sequence Length 732
Subcellular Localization Cytoplasmic granule membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. [PubMed: 16709802]
Protein Sequence MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTLHSVFSASARGRRARAKPQAEPPPPAAQPPPAPAPAAAQGPPPEALPAEPAAEAEAEAAAAAAEPGFDDEEAAEGGGPGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLIGAPVGISLIAGIAIPAMVIGIPVYVGRKIHSRYEGRKTSKHKRNLAITGGVTLSVIASPVIAAVSVGIGVPIMLAYVYGVVPISLCRGGGCGVSTANGKGVKIEFDEDDGPITVADAWRALKNPSIGESSIEGLTSVLSTSGSPTDGLSVMQGPYSETASFAALSGGTLSGGILSSGKGKYSRLEVQADVQKEIFPKDTASLGAISDNASTRAMAGSIISSYNPQDRECNNMEIQVDIEAKPSHYQLVSGSSTEDSLHVHAQMAENEEEGSGGGGSEEDPPCRHQSCEQKDCLASKPWDISLAQPESIRSDLESSDAQSDDVPDITSDECGSPRSHTAACPSTPRAQGAPSPSAHMNLSALAEGQTVLKPEGGEARV
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
7Phosphorylation-MGSEKDSESPRSTS
-CCCCCCCCCCCCCC		51.5524719451
9PhosphorylationGSEKDSESPRSTSLH
CCCCCCCCCCCCCCC		29.5726437602
12PhosphorylationKDSESPRSTSLHAAA
CCCCCCCCCCCCCCC		26.2324719451
13PhosphorylationDSESPRSTSLHAAAP
CCCCCCCCCCCCCCC		36.2728348404
14PhosphorylationSESPRSTSLHAAAPD
CCCCCCCCCCCCCCC		21.2825159151
147UbiquitinationRSCRDCLRHYLRLEI
HHHHHHHHHHHHHEE		23.8021890473
187UbiquitinationADPPLMHKYEEFMLR
CCCCCHHHHHHHHHH		40.15-
187UbiquitinationADPPLMHKYEEFMLR
CCCCCHHHHHHHHHH		40.15-
187UbiquitinationADPPLMHKYEEFMLR
CCCCCHHHHHHHHHH		40.15-
236 (in isoform 3)Ubiquitination-14.0821890473
266PhosphorylationAQTLRVRTKHTSGLS
HHHHCCCCCCCCCCC		25.0726434776
267UbiquitinationQTLRVRTKHTSGLSY
HHHCCCCCCCCCCCC		34.03-
267UbiquitinationQTLRVRTKHTSGLSY
HHHCCCCCCCCCCCC		34.03-
269PhosphorylationLRVRTKHTSGLSYGQ
HCCCCCCCCCCCCCC		26.5026434776
270 (in isoform 2)Phosphorylation-37.14-
270PhosphorylationRVRTKHTSGLSYGQE
CCCCCCCCCCCCCCC		37.1426434776
273 (in isoform 2)Phosphorylation-30.64-
273PhosphorylationTKHTSGLSYGQESGP
CCCCCCCCCCCCCCC		30.6426434776
274PhosphorylationKHTSGLSYGQESGPA
CCCCCCCCCCCCCCH		28.0626434776
278PhosphorylationGLSYGQESGPADDIK
CCCCCCCCCCHHHCC		42.0425332170
337 (in isoform 4)Ubiquitination-24.7421890473
337UbiquitinationPSGCTFWGKKPWSRK
CCCCCCCCCCCCCHH		24.74-
337 (in isoform 2)Ubiquitination-24.7421890473
337UbiquitinationPSGCTFWGKKPWSRK
CCCCCCCCCCCCCHH		24.7421890473
338 (in isoform 1)Ubiquitination-46.3821890473
338UbiquitinationSGCTFWGKKPWSRKK
CCCCCCCCCCCCHHH		46.3822817900
338UbiquitinationSGCTFWGKKPWSRKK
CCCCCCCCCCCCHHH		46.38-
339UbiquitinationGCTFWGKKPWSRKKK
CCCCCCCCCCCHHHH		48.0221890473
393PhosphorylationSRYEGRKTSKHKRNL
HCCCCCCCCCCCCCE		41.4626133373
453UbiquitinationCGVSTANGKGVKIEF
CCEECCCCCCCEEEE		26.15-
453UbiquitinationCGVSTANGKGVKIEF
CCEECCCCCCCEEEE		26.15-
454UbiquitinationGVSTANGKGVKIEFD
CEECCCCCCCEEEEC		61.41-
480PhosphorylationWRALKNPSIGESSIE
HHHHHCCCCCCHHHH		53.25-
482 (in isoform 3)Phosphorylation-32.83-
484PhosphorylationKNPSIGESSIEGLTS
HCCCCCCHHHHHHHH		31.25-
554PhosphorylationKEIFPKDTASLGAIS
HHHCCCCCCCCCCCC		25.0324114839
556PhosphorylationIFPKDTASLGAISDN
HCCCCCCCCCCCCCC		29.4525159151
561PhosphorylationTASLGAISDNASTRA
CCCCCCCCCCHHHHH		25.0324114839
565PhosphorylationGAISDNASTRAMAGS
CCCCCCHHHHHHCHH		25.3625627689
572PhosphorylationSTRAMAGSIISSYNP
HHHHHCHHHHHCCCC		13.76-
583 (in isoform 2)Phosphorylation-50.30-
682PhosphorylationDDVPDITSDECGSPR
CCCCCCCCCCCCCCC		31.5724114839
698PhosphorylationHTAACPSTPRAQGAP
CCCCCCCCCCCCCCC		11.26-
706PhosphorylationPRAQGAPSPSAHMNL
CCCCCCCCCCCCCCH		30.84-
721PhosphorylationSALAEGQTVLKPEGG
HHHHCCCEEECCCCC		38.37-
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 RN19B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN19B_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 RN19B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2L3_HUMANUBE2L3physical
16709802
UB2L6_HUMANUBE2L6physical
16709802
BTG4_HUMANBTG4physical
16709802
MOONR_HUMANKIAA0753physical
28514442
VP13C_HUMANVPS13Cphysical
28514442
UBB_HUMANUBBphysical
28514442
UBP4_HUMANUSP4physical
28514442
DDX49_HUMANDDX49physical
28514442
UBP15_HUMANUSP15physical
28514442
UBP46_HUMANUSP46physical
28514442
F91A1_HUMANFAM91A1physical
28514442
MPP5_HUMANMPP5physical
28514442
CPNE7_HUMANCPNE7physical
28514442
WDR20_HUMANWDR20physical
28514442
CDC27_HUMANCDC27physical
28514442
UBP22_HUMANUSP22physical
28514442
VP13A_HUMANVPS13Aphysical
28514442
UBP12_HUMANUSP12physical
28514442
DEN6A_HUMANDENND6Aphysical
28514442
WDR11_HUMANWDR11physical
28514442
HSDL1_HUMANHSDL1physical
28514442
TBB3_HUMANTUBB3physical
28514442
TPC2A_HUMANTRAPPC2physical
28514442
TPC2B_HUMANTRAPPC2physical
28514442
AP3M1_HUMANAP3M1physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
AP1M1_HUMANAP1M1physical
28514442
PK3CA_HUMANPIK3CAphysical
28514442
NEK9_HUMANNEK9physical
28514442
P85B_HUMANPIK3R2physical
28514442
ST7_HUMANST7physical
28514442
LETM1_HUMANLETM1physical
28514442
PK3CB_HUMANPIK3CBphysical
28514442
LGR4_HUMANLGR4physical
28514442
ZMYM4_HUMANZMYM4physical
28514442
P85A_HUMANPIK3R1physical
28514442
LTN1_HUMANLTN1physical
28514442
ARL17_HUMANARL17Aphysical
28514442
WDR48_HUMANWDR48physical
28514442
XPR1_HUMANXPR1physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN19B_HUMAN

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Related Literatures of Post-Translational Modification

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