RINI_HUMAN - dbPTM
RINI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RINI_HUMAN
UniProt AC P13489
Protein Name Ribonuclease inhibitor
Gene Name RNH1
Organism Homo sapiens (Human).
Sequence Length 461
Subcellular Localization Cytoplasm.
Protein Description Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis..
Protein Sequence MSLDIQSLDIQCEELSDARWAELLPLLQQCQVVRLDDCGLTEARCKDISSALRVNPALAELNLRSNELGDVGVHCVLQGLQTPSCKIQKLSLQNCCLTGAGCGVLSSTLRTLPTLQELHLSDNLLGDAGLQLLCEGLLDPQCRLEKLQLEYCSLSAASCEPLASVLRAKPDFKELTVSNNDINEAGVRVLCQGLKDSPCQLEALKLESCGVTSDNCRDLCGIVASKASLRELALGSNKLGDVGMAELCPGLLHPSSRLRTLWIWECGITAKGCGDLCRVLRAKESLKELSLAGNELGDEGARLLCETLLEPGCQLESLWVKSCSFTAACCSHFSSVLAQNRFLLELQISNNRLEDAGVRELCQGLGQPGSVLRVLWLADCDVSDSSCSSLAATLLANHSLRELDLSNNCLGDAGILQLVESVRQPGCLLEQLVLYDIYWSEEMEDRLQALEKDKPSLRVIS
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
2Phosphorylation------MSLDIQSLD
------CCCCCCCCC		34.4522617229
2Acetylation------MSLDIQSLD
------CCCCCCCCC		34.4522223895
7Phosphorylation-MSLDIQSLDIQCEE
-CCCCCCCCCCCCHH		28.4825849741
16PhosphorylationDIQCEELSDARWAEL
CCCCHHHCCHHHHHH		32.2927251275
30GlutathionylationLLPLLQQCQVVRLDD
HHHHHHHCCEEEECC		1.8222555962
38GlutathionylationQVVRLDDCGLTEARC
CEEEECCCCCCCHHH		4.8622555962
38S-nitrosylationQVVRLDDCGLTEARC
CEEEECCCCCCCHHH		4.8622178444
38S-nitrosocysteineQVVRLDDCGLTEARC
CEEEECCCCCCCHHH		4.86-
45GlutathionylationCGLTEARCKDISSAL
CCCCCHHHCCHHHHH		6.3122555962
46UbiquitinationGLTEARCKDISSALR
CCCCHHHCCHHHHHH		53.17-
65PhosphorylationLAELNLRSNELGDVG
HHHHCCCCCCCCCHH		37.5120068231
75S-nitrosylationLGDVGVHCVLQGLQT
CCCHHHHHHHCCCCC		2.8022178444
82PhosphorylationCVLQGLQTPSCKIQK
HHHCCCCCCCCCEEE		23.3925159151
84PhosphorylationLQGLQTPSCKIQKLS
HCCCCCCCCCEEECC		31.2828122231
85S-nitrosylationQGLQTPSCKIQKLSL
CCCCCCCCCEEECCC		4.7822178444
86AcetylationGLQTPSCKIQKLSLQ
CCCCCCCCEEECCCC		53.1325953088
86UbiquitinationGLQTPSCKIQKLSLQ
CCCCCCCCEEECCCC		53.1321906983
89AcetylationTPSCKIQKLSLQNCC
CCCCCEEECCCCCCC		43.4425953088
89UbiquitinationTPSCKIQKLSLQNCC
CCCCCEEECCCCCCC		43.4421890473
89UbiquitinationTPSCKIQKLSLQNCC
CCCCCEEECCCCCCC		43.4421890473
89UbiquitinationTPSCKIQKLSLQNCC
CCCCCEEECCCCCCC		43.4421906983
89UbiquitinationTPSCKIQKLSLQNCC
CCCCCEEECCCCCCC		43.4421890473
91PhosphorylationSCKIQKLSLQNCCLT
CCCEEECCCCCCCCC		34.6415755456
98PhosphorylationSLQNCCLTGAGCGVL
CCCCCCCCCCCCHHH		15.8622817900
108PhosphorylationGCGVLSSTLRTLPTL
CCHHHHHHHHHCCCH		19.5119690332
169AcetylationLASVLRAKPDFKELT
HHHHHHCCCCCCEEE		38.397430875
173UbiquitinationLRAKPDFKELTVSNN
HHCCCCCCEEEECCC		60.2321890473
173UbiquitinationLRAKPDFKELTVSNN
HHCCCCCCEEEECCC		60.2321890473
173UbiquitinationLRAKPDFKELTVSNN
HHCCCCCCEEEECCC		60.2321890473
173UbiquitinationLRAKPDFKELTVSNN
HHCCCCCCEEEECCC		60.2321890473
176PhosphorylationKPDFKELTVSNNDIN
CCCCCEEEECCCCCC		23.9925693802
178PhosphorylationDFKELTVSNNDINEA
CCCEEEECCCCCCHH		25.3621712546
195UbiquitinationRVLCQGLKDSPCQLE
HHHHCCCCCCCCCEE		64.08-
195MalonylationRVLCQGLKDSPCQLE
HHHHCCCCCCCCCEE		64.0832601280
195AcetylationRVLCQGLKDSPCQLE
HHHHCCCCCCCCCEE		64.0825953088
1952-HydroxyisobutyrylationRVLCQGLKDSPCQLE
HHHHCCCCCCCCCEE		64.08-
205AcetylationPCQLEALKLESCGVT
CCCEEEEEHHHCCCC		58.2026822725
205UbiquitinationPCQLEALKLESCGVT
CCCEEEEEHHHCCCC		58.20-
225PhosphorylationDLCGIVASKASLREL
HHHHHHHCHHHHHHH		20.1920068231
226UbiquitinationLCGIVASKASLRELA
HHHHHHCHHHHHHHH		32.0521906983
228PhosphorylationGIVASKASLRELALG
HHHHCHHHHHHHHCC		31.5330622161
238UbiquitinationELALGSNKLGDVGMA
HHHCCCCCCCCCCHH		56.39-
248S-nitrosocysteineDVGMAELCPGLLHPS
CCCHHHHCCCCCCCC		1.57-
248S-nitrosylationDVGMAELCPGLLHPS
CCCHHHHCCCCCCCC		1.5722178444
248GlutathionylationDVGMAELCPGLLHPS
CCCHHHHCCCCCCCC		1.5722555962
283UbiquitinationLCRVLRAKESLKELS
HHHHHHHHHHHHHHH		41.2121906983
285PhosphorylationRVLRAKESLKELSLA
HHHHHHHHHHHHHCC		43.9925693802
287UbiquitinationLRAKESLKELSLAGN
HHHHHHHHHHHCCCC		66.9221906983
290PhosphorylationKESLKELSLAGNELG
HHHHHHHHCCCCCHH		19.7726657352
321UbiquitinationQLESLWVKSCSFTAA
EEEEEEECCCHHHHH		33.88-
362GlutathionylationDAGVRELCQGLGQPG
HHHHHHHHHCCCCCC		2.3022555962
409GlutathionylationELDLSNNCLGDAGIL
HHCCCCCCCCHHHHH		5.4122555962
409S-nitrosylationELDLSNNCLGDAGIL
HHCCCCCCCCHHHHH		5.4122178444
452UbiquitinationDRLQALEKDKPSLRV
HHHHHHHHCCCCCEE		72.4221890473
452UbiquitinationDRLQALEKDKPSLRV
HHHHHHHHCCCCCEE		72.4221890473
4522-HydroxyisobutyrylationDRLQALEKDKPSLRV
HHHHHHHHCCCCCEE		72.42-
452AcetylationDRLQALEKDKPSLRV
HHHHHHHHCCCCCEE		72.4225953088
452UbiquitinationDRLQALEKDKPSLRV
HHHHHHHHCCCCCEE		72.4221890473
452UbiquitinationDRLQALEKDKPSLRV
HHHHHHHHCCCCCEE		72.4221906983
454UbiquitinationLQALEKDKPSLRVIS
HHHHHHCCCCCEECC		47.8021890473
454UbiquitinationLQALEKDKPSLRVIS
HHHHHHCCCCCEECC		47.8021890473
454UbiquitinationLQALEKDKPSLRVIS
HHHHHHCCCCCEECC		47.8021906983
454UbiquitinationLQALEKDKPSLRVIS
HHHHHHCCCCCEECC		47.8021890473
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 RINI_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RINI_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 RINI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANGI_HUMANANGphysical
9311977
UBQL2_HUMANUBQLN2physical
22939629
TEBP_HUMANPTGES3physical
22863883
SDCB1_HUMANSDCBPphysical
25416956
CDC20_HUMANCDC20physical
26496610
LMO7_HUMANLMO7physical
26496610
PSMD2_HUMANPSMD2physical
26496610
M4K4_HUMANMAP4K4physical
26496610
THOC4_HUMANALYREFphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RINI_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND MASSSPECTROMETRY.

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