RCC1L_HUMAN - dbPTM
RCC1L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCC1L_HUMAN
UniProt AC Q96I51
Protein Name RCC1-like G exchanging factor-like protein
Gene Name RCC1L {ECO:0000312|HGNC:HGNC:14948}
Organism Homo sapiens (Human).
Sequence Length 464
Subcellular Localization Mitochondrion membrane . Mitochondrion inner membrane .
Protein Description Guanine nucleotide exchange factor (GEF) for mitochondrial dynamin-related GTPase OPA1. Activates OPA1, by exchanging bound GDP for free GTP, and drives OPA1 and MFN1-dependent mitochondrial fusion. [PubMed: 28746876 Plays an essential role in mitochondrial ribosome biogenesis. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation of core subunits of the oxidative phosphorylation system]
Protein Sequence MALVALVAGARLGRRLSGPGLGRGHWTAARRSRSRREAAEAEAEVPVVQYVGERAARADRVFVWGFSFSGALGVPSFVVPSSGPGPRAGARPRRRIQPVPYRLELDQKISSAACGYGFTLLSSKTADVTKVWGMGLNKDSQLGFHRSRKDKTRGYEYVLEPSPVSLPLDRPQETRVLQVSCGRAHSLVLTDREGVFSMGNNSYGQCGRKVVENEIYSESHRVHRMQDFDGQVVQVACGQDHSLFLTDKGEVYSCGWGADGQTGLGHYNITSSPTKLGGDLAGVNVIQVATYGDCCLAVSADGGLFGWGNSEYLQLASVTDSTQVNVPRCLHFSGVGKVRQAACGGTGCAVLNGEGHVFVWGYGILGKGPNLVESAVPEMIPPTLFGLTEFNPEIQVSRIRCGLSHFAALTNKGELFVWGKNIRGCLGIGRLEDQYFPWRVTMPGEPVDVACGVDHMVTLAKSFI
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
17PhosphorylationARLGRRLSGPGLGRG
CCCCCCCCCCCCCCC
28122231
140PhosphorylationGMGLNKDSQLGFHRS
ECCCCCCCCCCCCCC
21406692
147PhosphorylationSQLGFHRSRKDKTRG
CCCCCCCCCCCCCCC
21406692
186PhosphorylationVSCGRAHSLVLTDRE
EECCCCCEEEEECCC
-
190PhosphorylationRAHSLVLTDREGVFS
CCCEEEEECCCCEEE
-
197PhosphorylationTDREGVFSMGNNSYG
ECCCCEEECCCCCCC
21406692
202PhosphorylationVFSMGNNSYGQCGRK
EEECCCCCCCCCCCC
21406692
203PhosphorylationFSMGNNSYGQCGRKV
EECCCCCCCCCCCCH
21406692
209UbiquitinationSYGQCGRKVVENEIY
CCCCCCCCHHHCCCC
21906983
209MalonylationSYGQCGRKVVENEIY
CCCCCCCCHHHCCCC
26320211
209UbiquitinationSYGQCGRKVVENEIY
CCCCCCCCHHHCCCC
22817900
216PhosphorylationKVVENEIYSESHRVH
CHHHCCCCCCCCCEE
25159151
217PhosphorylationVVENEIYSESHRVHR
HHHCCCCCCCCCEEE
-
262PhosphorylationGWGADGQTGLGHYNI
ECCCCCCCCCCCCCC
28787133
270PhosphorylationGLGHYNITSSPTKLG
CCCCCCCCCCCCCCC
25627689
271PhosphorylationLGHYNITSSPTKLGG
CCCCCCCCCCCCCCC
25627689
272PhosphorylationGHYNITSSPTKLGGD
CCCCCCCCCCCCCCC
25627689
274PhosphorylationYNITSSPTKLGGDLA
CCCCCCCCCCCCCCC
28787133

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 RCC1L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RCC1L_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 RCC1L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RCC1L_HUMANWBSCR16physical
27499296
TRUB2_HUMANTRUB2physical
27499296
CF203_HUMANC6orf203physical
27499296
NDK6_HUMANNME6physical
27499296
NRDC_HUMANNRD1physical
27499296
DHRS4_HUMANDHRS4physical
27499296
MPPB_HUMANPMPCBphysical
27499296
MPPA_HUMANPMPCAphysical
27499296
STAR7_HUMANSTARD7physical
27499296
NUD19_HUMANNUDT19physical
27499296
CLPB_HUMANCLPBphysical
27499296
ECH1_HUMANECH1physical
27499296
NGRN_HUMANNGRNphysical
27667664
NDK6_HUMANNME6physical
27667664
TRUB2_HUMANTRUB2physical
27667664
FAKD2_HUMANFASTKD2physical
27667664
RUSD3_HUMANRPUSD3physical
27667664
TEFM_HUMANTEFMphysical
27667664
GTPBA_HUMANGTPBP10physical
27667664
TBRG4_HUMANTBRG4physical
27667664
RUSD4_HUMANRPUSD4physical
27667664
RM20_HUMANMRPL20physical
27667664

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RCC1L_HUMAN

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Related Literatures of Post-Translational Modification

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