RINT1_HUMAN - dbPTM
RINT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RINT1_HUMAN
UniProt AC Q6NUQ1
Protein Name RAD50-interacting protein 1
Gene Name RINT1
Organism Homo sapiens (Human).
Sequence Length 792
Subcellular Localization Cytoplasm. Endoplasmic reticulum membrane
Peripheral membrane protein.
Protein Description Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. May play a role in cell cycle checkpoint control. [PubMed: 11096100 Essential for telomere length control]
Protein Sequence MLPAGEIGASPAAPCCSESGDERKNLEEKSDINVTVLIGSKQVSEGTDNGDLPSYVSAFIEKEVGNDLKSLKKLDKLIEQRTVSKMQLEEQVLTISSEIPKRIRSALKNAEESKQFLNQFLEQETHLFSAINSHLLTAQPWMDDLGTMISQIEEIERHLAYLKWISQIEELSDNIQQYLMTNNVPEAASTLVSMAELDIKLQESSCTHLLGFMRATVKFWHKILKDKLTSDFEEILAQLHWPFIAPPQSQTVGLSRPASAPEIYSYLETLFCQLLKLQTSDELLTEPKQLPEKYSLPASPSVILPIQVMLTPLQKRFRYHFRGNRQTNVLSKPEWYLAQVLMWIGNHTEFLDEKIQPILDKVGSLVNARLEFSRGLMMLVLEKLATDIPCLLYDDNLFCHLVDEVLLFERELHSVHGYPGTFASCMHILSEETCFQRWLTVERKFALQKMDSMLSSEAAWVSQYKDITDVDEMKVPDCAETFMTLLLVITDRYKNLPTASRKLQFLELQKDLVDDFRIRLTQVMKEETRASLGFRYCAILNAVNYISTVLADWADNVFFLQLQQAALEVFAENNTLSKLQLGQLASMESSVFDDMINLLERLKHDMLTRQVDHVFREVKDAAKLYKKERWLSLPSQSEQAVMSLSSSACPLLLTLRDHLLQLEQQLCFSLFKIFWQMLVEKLDVYIYQEIILANHFNEGGAAQLQFDMTRNLFPLFSHYCKRPENYFKHIKEACIVLNLNVGSALLLKDVLQSASGQLPATAALNEVGIYKLAQQDVEILLNLRTNWPNTGK
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
10PhosphorylationPAGEIGASPAAPCCS
CCCCCCCCCCCCCCC		15.1725159151
17PhosphorylationSPAAPCCSESGDERK
CCCCCCCCCCCCHHC		41.3225627689
19PhosphorylationAAPCCSESGDERKNL
CCCCCCCCCCHHCCC		34.9425159151
30UbiquitinationRKNLEEKSDINVTVL
HCCCCHHCCCEEEEE		47.1833845483
62UbiquitinationYVSAFIEKEVGNDLK
HHHHHHHHHHCCCHH		53.5429967540
69MalonylationKEVGNDLKSLKKLDK
HHHCCCHHHHHHHHH		57.5130639696
69UbiquitinationKEVGNDLKSLKKLDK
HHHCCCHHHHHHHHH		57.5129967540
73UbiquitinationNDLKSLKKLDKLIEQ
CCHHHHHHHHHHHHH		68.1829967540
85UbiquitinationIEQRTVSKMQLEEQV
HHHCCCCCHHHHHHH		26.7429967540
94PhosphorylationQLEEQVLTISSEIPK
HHHHHHHHHCHHHHH		21.69-
96PhosphorylationEEQVLTISSEIPKRI
HHHHHHHCHHHHHHH		19.38-
97PhosphorylationEQVLTISSEIPKRIR
HHHHHHCHHHHHHHH		35.38-
101UbiquitinationTISSEIPKRIRSALK
HHCHHHHHHHHHHHH		67.1429967540
108UbiquitinationKRIRSALKNAEESKQ
HHHHHHHHCHHHHHH		54.5533845483
161UbiquitinationEIERHLAYLKWISQI
HHHHHHHHHHHHHHH		18.3821963094
169UbiquitinationLKWISQIEELSDNIQ
HHHHHHHHHHHHHHH		45.2929967540
184UbiquitinationQYLMTNNVPEAASTL
HHHHHCCCHHHHHHH		5.0024816145
194UbiquitinationAASTLVSMAELDIKL
HHHHHHHHHHHCHHH		2.3421963094
202UbiquitinationAELDIKLQESSCTHL
HHHCHHHCHHHHHHH		43.4529967540
210UbiquitinationESSCTHLLGFMRATV
HHHHHHHHHHHHHHH		3.7429967540
217UbiquitinationLGFMRATVKFWHKIL
HHHHHHHHHHHHHHH		4.7424816145
229PhosphorylationKILKDKLTSDFEEIL
HHHHHHCCCCHHHHH		31.8029978859
230PhosphorylationILKDKLTSDFEEILA
HHHHHCCCCHHHHHH		51.2229978859
249PhosphorylationPFIAPPQSQTVGLSR
CCCCCCCCCCCCCCC		33.3229978859
251PhosphorylationIAPPQSQTVGLSRPA
CCCCCCCCCCCCCCC		23.0729978859
288UbiquitinationDELLTEPKQLPEKYS
HHHCCCCCCCCCCCC		59.2329967540
295PhosphorylationKQLPEKYSLPASPSV
CCCCCCCCCCCCCCC		38.6622210691
301PhosphorylationYSLPASPSVILPIQV
CCCCCCCCCEEEEEE		21.2122210691
387UbiquitinationVLEKLATDIPCLLYD
HHHHHHHCCCEEECC		36.9129967540
420UbiquitinationHSVHGYPGTFASCMH
HHCCCCCCHHHHHHH		25.6129967540
424UbiquitinationGYPGTFASCMHILSE
CCCCHHHHHHHHHCC		14.0521963094
432UbiquitinationCMHILSEETCFQRWL
HHHHHCCCCHHHHHH		47.7229967540
447UbiquitinationTVERKFALQKMDSML
HHHHHHHHHHHHHHH		5.9124816145
468PhosphorylationVSQYKDITDVDEMKV
HHCCCCCCCCCCCCC		39.85-
500O-linked_GlycosylationYKNLPTASRKLQFLE
HCCCCCHHHHHHHHH		32.2131637018
502UbiquitinationNLPTASRKLQFLELQ
CCCCHHHHHHHHHHH		44.1121963094
510UbiquitinationLQFLELQKDLVDDFR
HHHHHHHHHHHHHHH		66.7029967540
525UbiquitinationIRLTQVMKEETRASL
HHHHHHHHHHHHHHH		54.2524816145
635PhosphorylationERWLSLPSQSEQAVM
HHCCCCCCHHHHHHH		52.19-
650UbiquitinationSLSSSACPLLLTLRD
HHCCCHHHHHHHHHH		26.2629967540
654PhosphorylationSACPLLLTLRDHLLQ
CHHHHHHHHHHHHHH		21.51-
669PhosphorylationLEQQLCFSLFKIFWQ
HHHHHHHHHHHHHHH		31.7224719451
728UbiquitinationKRPENYFKHIKEACI
CCCHHHHHHHHHHHH		33.7829967540
743PhosphorylationVLNLNVGSALLLKDV
HEECCCCHHHHHHHH		16.0927251275
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 RINT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RINT1_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 RINT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZW10_HUMANZW10physical
15029241
STX18_HUMANSTX18physical
15029241
RAD50_HUMANRAD50physical
11096100
YLPM1_HUMANYLPM1physical
22939629
RBL2_HUMANRBL2physical
16600870
RBL1_HUMANRBL1physical
16600870
RB_HUMANRB1physical
16600870
RAD50_HUMANRAD50physical
16600870
SH24A_HUMANSH2D4Aphysical
25416956
RSRC2_HUMANRSRC2physical
25416956
SCNM1_HUMANSCNM1physical
25416956
ZN655_HUMANZNF655physical
25416956
CC121_HUMANCCDC121physical
25416956
F124B_HUMANFAM124Bphysical
25416956
CSPP1_HUMANCSPP1physical
25416956
EPC1_HUMANEPC1physical
25416956
F110A_HUMANFAM110Aphysical
25416956
F161A_HUMANFAM161Aphysical
25416956
ZN697_HUMANZNF697physical
25416956
SGF29_HUMANCCDC101physical
25416956
SFR1_HUMANSFR1physical
25416956
C19L2_HUMANCWF19L2physical
25416956
FA81B_HUMANFAM81Bphysical
25416956
RIBC1_HUMANRIBC1physical
25416956
TXLNA_HUMANTXLNAphysical
25416956
RTP5_HUMANRTP5physical
25416956
CE57L_HUMANCEP57L1physical
25416956
SCFD2_HUMANSCFD2physical
28514442
USE1_HUMANUSE1physical
28514442
NBAS_HUMANNBASphysical
28514442
CS025_HUMANC19orf25physical
28514442
SPAG5_HUMANSPAG5physical
28514442
ZW10_HUMANZW10physical
28514442
SC22B_HUMANSEC22Bphysical
28514442
SEC20_HUMANBNIP1physical
28514442
STX18_HUMANSTX18physical
28514442
VAMP3_HUMANVAMP3physical
28514442
BASI_HUMANBSGphysical
28514442
SNAA_HUMANNAPAphysical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RINT1_HUMAN

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Related Literatures of Post-Translational Modification

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