RIMKB_HUMAN - dbPTM
RIMKB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIMKB_HUMAN
UniProt AC Q9ULI2
Protein Name Beta-citrylglutamate synthase B
Gene Name RIMKLB
Organism Homo sapiens (Human).
Sequence Length 386
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate..
Protein Sequence MCSSVAAKLWFLTDRRIREDYPQKEILRALKAKCCEEELDFRAVVMDEVVLTIEQGNLGLRINGELITAYPQVVVVRVPTPWVQSDSDITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEVLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRHEAPYLFQKYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGMDVCGIDLLMKDDGSFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPSGRLTRRMSLLSVVSTASETSEPELGPPASTAVDNMSASSSSVDSDPESTERELLTKLPGGLFNMNQLLANEIKLLVD
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
21PhosphorylationDRRIREDYPQKEILR
CCCCCCCCCHHHHHH
11.65-
24UbiquitinationIREDYPQKEILRALK
CCCCCCHHHHHHHHH
42.0729967540
31UbiquitinationKEILRALKAKCCEEE
HHHHHHHHHHHCCCC
44.8322817900
33UbiquitinationILRALKAKCCEEELD
HHHHHHHHHCCCCCC
37.5221963094
118PhosphorylationNCVNKFWTFQELAGH
HHHHHHHHHHHHCCC
20.6922210691
135PhosphorylationPLPDTFSYGGHENFA
CCCCCCCCCCCHHHH
23.9622210691
158UbiquitinationLEFPMVVKNTRGHRG
HCCCEEEECCCCCCC
40.9921963094
166UbiquitinationNTRGHRGKAVFLARD
CCCCCCCEEEEEECC
41.1427667366
174UbiquitinationAVFLARDKHHLADLS
EEEEECCCHHHHHHH
27.6321963094
194UbiquitinationEAPYLFQKYVKESHG
HHHHHHHHHHHHHHC
44.6821963094
197UbiquitinationYLFQKYVKESHGRDV
HHHHHHHHHHHCCCE
50.8622817900
272 (in isoform 2)Phosphorylation-23.5923879269
317PhosphorylationGRLTRRMSLLSVVST
CCHHHHHHHHHHHHC
25.0922468782
347PhosphorylationAVDNMSASSSSVDSD
HCCCCCCCCCCCCCC
24.36-
353PhosphorylationASSSSVDSDPESTER
CCCCCCCCCCHHHHH
53.56-
358PhosphorylationVDSDPESTERELLTK
CCCCCHHHHHHHHHC
37.08-
365UbiquitinationTERELLTKLPGGLFN
HHHHHHHCCCCCCCC
53.2921963094

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 RIMKB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIMKB_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 RIMKB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RIMKB_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIMKB_HUMAN

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Related Literatures of Post-Translational Modification

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