RGMA_HUMAN - dbPTM
RGMA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGMA_HUMAN
UniProt AC Q96B86
Protein Name Repulsive guidance molecule A
Gene Name RGMA
Organism Homo sapiens (Human).
Sequence Length 450
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor.
Protein Description Member of the repulsive guidance molecule (RGM) family that performs several functions in the developing and adult nervous system. Regulates cephalic neural tube closure, inhibits neurite outgrowth and cortical neuron branching, and the formation of mature synapses. Binding to its receptor NEO1/neogenin induces activation of RHOA-ROCK1/Rho-kinase signaling pathway through UNC5B-ARHGEF12/LARG-PTK2/FAK1 cascade, leading to collapse of the neuronal growth cone and neurite outgrowth inhibition. Furthermore, RGMA binding to NEO1/neogenin leads to HRAS inactivation by influencing HRAS-PTK2/FAK1-AKT1 pathway. It also functions as a bone morphogenetic protein (BMP) coreceptor that may signal through SMAD1, SMAD5, and SMAD8..
Protein Sequence MQPPRERLVVTGRAGWMGMGRGAGRSALGFWPTLAFLLCSFPAATSPCKILKCNSEFWSATSGSHAPASDDTPEFCAALRSYALCTRRTARTCRGDLAYHSAVHGIEDLMSQHNCSKDGPTSQPRLRTLPPAGDSQERSDSPEICHYEKSFHKHSATPNYTHCGLFGDPHLRTFTDRFQTCKVQGAWPLIDNNYLNVQVTNTPVLPGSAATATSKLTIIFKNFQECVDQKVYQAEMDELPAAFVDGSKNGGDKHGANSLKITEKVSGQHVEIQAKYIGTTIVVRQVGRYLTFAVRMPEEVVNAVEDWDSQGLYLCLRGCPLNQQIDFQAFHTNAEGTGARRLAAASPAPTAPETFPYETAVAKCKEKLPVEDLYYQACVFDLLTTGDVNFTLAAYYALEDVKMLHSNKDKLHLYDRTRDLPGRAAAGLPLAPRPLLGALVPLLALLPVFC
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
114N-linked_GlycosylationEDLMSQHNCSKDGPT
HHHHHHCCCCCCCCC
24.91UniProtKB CARBOHYD
128PhosphorylationTSQPRLRTLPPAGDS
CCCCCCCCCCCCCCC
48.48-
136PhosphorylationLPPAGDSQERSDSPE
CCCCCCCCCCCCCCC
55.66-
159N-linked_GlycosylationHKHSATPNYTHCGLF
CCCCCCCCCCCCCCC
50.40UniProtKB CARBOHYD
276PhosphorylationHVEIQAKYIGTTIVV
EEEEEEEECCCEEEE
13.96-
350O-linked_GlycosylationAAASPAPTAPETFPY
HHCCCCCCCCCCCCH
57.88OGP
354PhosphorylationPAPTAPETFPYETAV
CCCCCCCCCCHHHHH
28.9323917254
357PhosphorylationTAPETFPYETAVAKC
CCCCCCCHHHHHHHH
23.0123917254
359PhosphorylationPETFPYETAVAKCKE
CCCCCHHHHHHHHHH
22.1623917254
389N-linked_GlycosylationLLTTGDVNFTLAAYY
HHCCCCHHHHHHHHH
29.00UniProtKB CARBOHYD
424GPI-anchorTRDLPGRAAAGLPLA
CCCCCCCCCCCCCCC
13.95-

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 RGMA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGMA_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 RGMA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELOB_HUMANTCEB2physical
26496610
NCOR2_HUMANNCOR2physical
26496610
TXNIP_HUMANTXNIPphysical
26496610
HIPK2_HUMANHIPK2physical
26496610
PPHLN_HUMANPPHLN1physical
26496610
SMAG2_HUMANSAMD4Bphysical
26496610
BDP1_HUMANBDP1physical
26496610
CLK4_HUMANCLK4physical
26496610
ANO3_HUMANANO3physical
26496610
NBEL1_HUMANNBEAL1physical
26496610
SPICE_HUMANSPICE1physical
26496610

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

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Related Literatures of Post-Translational Modification

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