CHIN_HUMAN - dbPTM
CHIN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHIN_HUMAN
UniProt AC P15882
Protein Name N-chimaerin
Gene Name CHN1
Organism Homo sapiens (Human).
Sequence Length 459
Subcellular Localization
Protein Description GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance..
Protein Sequence MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRITCTCEVENRPKYYGREFHGMISREAADQLLIVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHVGYTTLNREPAYKKHMPVLKETHDERDSTGQDGVSEKRLTSLVRRATLKENEQIPKYEKIHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLKHVKKVYSCDLTTLVKAHTTKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDINIITGALKLYFRDLPIPLITYDAYPKFIESAKIMDPDEQLETLHEALKLLPPAHCETLRYLMAHLKRVTLHEKENLMNAENLGIVFGPTLMRSPELDAMAALNDIRYQRLVVELLIKNEDILF
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
2Acetylation------MALTLFDTD
------CCCCCCCCC		14.8419413330
8PhosphorylationMALTLFDTDEYRPPV
CCCCCCCCCCCCCCH		24.3224043423
11PhosphorylationTLFDTDEYRPPVWKS
CCCCCCCCCCCHHHH		31.0927642862
34PhosphorylationAPHPRRITCTCEVEN
CCCCCEEEEEEEECC		10.43-
36PhosphorylationHPRRITCTCEVENRP
CCCEEEEEEEECCCC		11.75-
42UbiquitinationCTCEVENRPKYYGRE
EEEEECCCCCCCCCC		18.6430230243
44AcetylationCEVENRPKYYGREFH
EEECCCCCCCCCCCC		48.1123749302
45PhosphorylationEVENRPKYYGREFHG
EECCCCCCCCCCCCC		17.52-
46PhosphorylationVENRPKYYGREFHGM
ECCCCCCCCCCCCCC		18.81-
56 (in isoform 2)Phosphorylation-27.0123663014
57 (in isoform 2)Phosphorylation-41.2223663014
60 (in isoform 2)Phosphorylation-46.8623663014
61 (in isoform 2)Phosphorylation-33.1823663014
69UbiquitinationLLIVAEGSYLIRESQ
EEEEEECCEEEEEHH		14.3130230243
76UbiquitinationSYLIRESQRQPGTYT
CEEEEEHHCCCCEEE		43.1929967540
143PhosphorylationKMTINPIYEHVGYTT
HCCCCCHHHHCCCCC		10.9729978859
148PhosphorylationPIYEHVGYTTLNREP
CHHHHCCCCCCCCCC		8.7529978859
149PhosphorylationIYEHVGYTTLNREPA
HHHHCCCCCCCCCCH		20.9129978859
150PhosphorylationYEHVGYTTLNREPAY
HHHCCCCCCCCCCHH		17.3529978859
157PhosphorylationTLNREPAYKKHMPVL
CCCCCCHHHHHCCCC		31.1427642862
185PhosphorylationGVSEKRLTSLVRRAT
CCCHHHHHHHHHHHH		24.85-
186PhosphorylationVSEKRLTSLVRRATL
CCHHHHHHHHHHHHH		29.4727134283
191UbiquitinationLTSLVRRATLKENEQ
HHHHHHHHHHHCCCC		13.5130230243
192PhosphorylationTSLVRRATLKENEQI
HHHHHHHHHHCCCCC		36.2329978859
194UbiquitinationLVRRATLKENEQIPK
HHHHHHHHCCCCCCC		54.8930230243
201UbiquitinationKENEQIPKYEKIHNF
HCCCCCCCCEEECCC		68.6129967540
202PhosphorylationENEQIPKYEKIHNFK
CCCCCCCCEEECCCE		19.6629083192
211UbiquitinationKIHNFKVHTFRGPHW
EECCCEEEEECCCHH		21.6330230243
237UbiquitinationIAQGVKCADCGLNVH
HHCCCCHHHCCCCHH		14.9230230243
243UbiquitinationCADCGLNVHKQCSKM
HHHCCCCHHHHHHCC		7.7930230243
266PhosphorylationLKHVKKVYSCDLTTL
HHHHHEEEECCHHHH		16.6829759185
267PhosphorylationKHVKKVYSCDLTTLV
HHHHEEEECCHHHHC		12.2524114839
271PhosphorylationKVYSCDLTTLVKAHT
EEEECCHHHHCHHCC		12.5829759185
272PhosphorylationVYSCDLTTLVKAHTT
EEECCHHHHCHHCCC		36.5329759185
290UbiquitinationMVVDMCIREIESRGL
CHHHHHHHHHHHCCC		33.6330230243
294PhosphorylationMCIREIESRGLNSEG
HHHHHHHHCCCCCCC		36.9922210691
299PhosphorylationIESRGLNSEGLYRVS
HHHCCCCCCCCEEEC		37.7822210691
303PhosphorylationGLNSEGLYRVSGFSD
CCCCCCCEEECCCHH		21.5922210691
316UbiquitinationSDLIEDVKMAFDRDG
HHHHHHHHHHHCCCC		36.5130230243
329PhosphorylationDGEKADISVNMYEDI
CCCEECEEEEEHHHH		14.16-
333UbiquitinationADISVNMYEDINIIT
ECEEEEEHHHHHHHH		12.7830230243
333PhosphorylationADISVNMYEDINIIT
ECEEEEEHHHHHHHH		12.78-
336UbiquitinationSVNMYEDINIITGAL
EEEEHHHHHHHHHHH		2.3930230243
340PhosphorylationYEDINIITGALKLYF
HHHHHHHHHHHHHHC		16.77-
342UbiquitinationDINIITGALKLYFRD
HHHHHHHHHHHHCCC		7.9030230243
346PhosphorylationITGALKLYFRDLPIP
HHHHHHHHCCCCCCC		8.59-
357PhosphorylationLPIPLITYDAYPKFI
CCCCEEEECCCHHHH		7.5030464169
362UbiquitinationITYDAYPKFIESAKI
EEECCCHHHHHHCCC		46.4230230243
368UbiquitinationPKFIESAKIMDPDEQ
HHHHHHCCCCCHHHH		48.0930230243
379UbiquitinationPDEQLETLHEALKLL
HHHHHHHHHHHHHHC		2.2230230243
385UbiquitinationTLHEALKLLPPAHCE
HHHHHHHHCCHHHHH		10.1230230243
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 CHIN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHIN_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 CHIN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C1_HUMANGTF3C1physical
16169070
RS3A_HUMANRPS3Aphysical
16169070
NCK2_HUMANNCK2physical
25416956
HEMK1_HUMANHEMK1physical
25416956
NCK2_HUMANNCK2physical
21516116
CHIO_HUMANCHN2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604356Duane retraction syndrome 2 (DURS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHIN_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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