RMP_HUMAN - dbPTM
RMP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RMP_HUMAN
UniProt AC O94763
Protein Name Unconventional prefoldin RPB5 interactor 1
Gene Name URI1
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization Nucleus. Cytoplasm. Mitochondrion. Cell projection, dendrite. Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 at mitochondrion.
Protein Description Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.; Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFDs and proteins with roles in transcription and ubiquitination..
Protein Sequence MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEKVVTNCQERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSDAAGDIVDIREEIKCDFEFKAKHRIAHKPHSKPKTSDIFEADIANDVKSKDLLADKELWARLEELERQEELLGELDSKPDTVIANGEDTTSSEEEKEDRNTNVNAMHQVTDSHTPCHKDVASSEPFSGQVNSQLNCSVNGSSSYHSDDDDDDDDDDDDDNIDDDDGDNDHEALGVGDNSIPTIYFSHTVEPKRVRINTGKNTTLKFSEKKEEAKRKRKNSTGSGHSAQELPTIRTPADIYRAFVDVVNGEYVPRKSILKSRSRENSVCSDTSESSAAEFDDRRGVLRSISCEEATCSDTSESILEEEPQENQKKLLPLSVTPEAFSGTVIEKEFVSPSLTPPPAIAHPALPTIPERKEVLLEASEETGKRVSKFKAARLQQKD
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
1Acetylation-------MEAPTVET
-------CCCCCCCC		10.0122814378
5Phosphorylation---MEAPTVETPPDP
---CCCCCCCCCCCC		37.7129255136
8PhosphorylationMEAPTVETPPDPSPP
CCCCCCCCCCCCCCC		35.4729255136
9 (in isoform 3)Phosphorylation-20.1424043423
12 (in isoform 3)Phosphorylation-55.2824043423
13PhosphorylationVETPPDPSPPSAPAP
CCCCCCCCCCCCCCC		57.7429255136
16PhosphorylationPPDPSPPSAPAPALV
CCCCCCCCCCCCCEE		50.7129255136
18 (in isoform 3)Phosphorylation-43.0124043423
22 (in isoform 3)Phosphorylation-3.8724043423
39AcetylationRLREEQEKVVTNCQE
HHHHHHHHHHHHHHH		41.5226051181
53UbiquitinationERIQHWKKVDNDYNA
HHHHHHHHHCCCHHH		50.0229967540
58PhosphorylationWKKVDNDYNALRERL
HHHHCCCHHHHHHHH		14.4827642862
140PhosphorylationKVMKNFESRVEFTED
HHHHHHHHHHHHHHH		37.1728555341
151SulfoxidationFTEDLQKMSDAAGDI
HHHHHHHHHHHCCCC		2.5721406390
160UbiquitinationDAAGDIVDIREEIKC
HHCCCCCCHHHHHCC		34.2621890473
168 (in isoform 2)Ubiquitination-40.9021890473
172MethylationIKCDFEFKAKHRIAH
HCCCEEECCCCCCCC		49.69115976753
182UbiquitinationHRIAHKPHSKPKTSD
CCCCCCCCCCCCCCC		53.9432015554
190UbiquitinationSKPKTSDIFEADIAN
CCCCCCCCCHHHHCC		3.1721890473
200UbiquitinationADIANDVKSKDLLAD
HHHCCCCCCCHHHCC		55.4332015554
206UbiquitinationVKSKDLLADKELWAR
CCCCHHHCCHHHHHH		32.8821890473
208UbiquitinationSKDLLADKELWARLE
CCHHHCCHHHHHHHH		49.4522817900
208 (in isoform 1)Ubiquitination-49.4521890473
229PhosphorylationELLGELDSKPDTVIA
HHHHHCCCCCCEEEE		59.7324144214
233PhosphorylationELDSKPDTVIANGED
HCCCCCCEEEECCCC		23.4924144214
241PhosphorylationVIANGEDTTSSEEEK
EEECCCCCCCCHHHH		25.0323898821
242PhosphorylationIANGEDTTSSEEEKE
EECCCCCCCCHHHHH		42.4523898821
243PhosphorylationANGEDTTSSEEEKED
ECCCCCCCCHHHHHH		37.5323898821
244PhosphorylationNGEDTTSSEEEKEDR
CCCCCCCCHHHHHHH		47.1125159151
266PhosphorylationHQVTDSHTPCHKDVA
HHHCCCCCCCCCCCC		31.4028555341
350PhosphorylationPKRVRINTGKNTTLK
CCEEEEECCCCCEEC		47.35-
354PhosphorylationRINTGKNTTLKFSEK
EEECCCCCEECHHHH		36.6732645325
354O-linked_GlycosylationRINTGKNTTLKFSEK
EEECCCCCEECHHHH		36.6730379171
355PhosphorylationINTGKNTTLKFSEKK
EECCCCCEECHHHHH		37.0329083192
355O-linked_GlycosylationINTGKNTTLKFSEKK
EECCCCCEECHHHHH		37.0330379171
359PhosphorylationKNTTLKFSEKKEEAK
CCCEECHHHHHHHHH		47.0925159151
372PhosphorylationAKRKRKNSTGSGHSA
HHHHHCCCCCCCCCC		36.8629255136
373PhosphorylationKRKRKNSTGSGHSAQ
HHHHCCCCCCCCCCC		44.7729255136
375PhosphorylationKRKNSTGSGHSAQEL
HHCCCCCCCCCCCCC		33.1623927012
378PhosphorylationNSTGSGHSAQELPTI
CCCCCCCCCCCCCCC		34.8630266825
384PhosphorylationHSAQELPTIRTPADI
CCCCCCCCCCCHHHH		35.4023403867
403PhosphorylationVDVVNGEYVPRKSIL
HHHHCCEEECHHHHH		19.7033259812
408PhosphorylationGEYVPRKSILKSRSR
CEEECHHHHHHCCCC		34.1426434776
412PhosphorylationPRKSILKSRSRENSV
CHHHHHHCCCCCCCC		31.8528985074
414PhosphorylationKSILKSRSRENSVCS
HHHHHCCCCCCCCCC		51.5425849741
418PhosphorylationKSRSRENSVCSDTSE
HCCCCCCCCCCCCCC		21.5422617229
421PhosphorylationSRENSVCSDTSESSA
CCCCCCCCCCCCCCC		41.5923663014
423PhosphorylationENSVCSDTSESSAAE
CCCCCCCCCCCCCHH		20.3523663014
424PhosphorylationNSVCSDTSESSAAEF
CCCCCCCCCCCCHHH		40.2423663014
426PhosphorylationVCSDTSESSAAEFDD
CCCCCCCCCCHHHCC		25.6623663014
427PhosphorylationCSDTSESSAAEFDDR
CCCCCCCCCHHHCCC		27.7023663014
440PhosphorylationDRRGVLRSISCEEAT
CCCCEECEEECCCCC		18.0723927012
442PhosphorylationRGVLRSISCEEATCS
CCEECEEECCCCCCC		19.4025159151
447PhosphorylationSISCEEATCSDTSES
EEECCCCCCCCCCHH		18.8023927012
449PhosphorylationSCEEATCSDTSESIL
ECCCCCCCCCCHHHH		39.3023927012
451PhosphorylationEEATCSDTSESILEE
CCCCCCCCCHHHHHH		20.3523927012
452PhosphorylationEATCSDTSESILEEE
CCCCCCCCHHHHHHC		34.0523927012
454PhosphorylationTCSDTSESILEEEPQ
CCCCCCHHHHHHCCC		32.0423927012
471PhosphorylationQKKLLPLSVTPEAFS
HHCCCCEECCHHHHC		23.2329523821
473PhosphorylationKLLPLSVTPEAFSGT
CCCCEECCHHHHCCC		16.4327050516
477UbiquitinationLSVTPEAFSGTVIEK
EECCHHHHCCCEEEE		7.0724816145
478PhosphorylationSVTPEAFSGTVIEKE
ECCHHHHCCCEEEEE		40.3729523821
480PhosphorylationTPEAFSGTVIEKEFV
CHHHHCCCEEEEEEC		19.6729523821
488PhosphorylationVIEKEFVSPSLTPPP
EEEEEECCCCCCCCC		17.6929255136
490PhosphorylationEKEFVSPSLTPPPAI
EEEECCCCCCCCCCC		37.0529255136
492PhosphorylationEFVSPSLTPPPAIAH
EECCCCCCCCCCCCC		37.7829255136
504PhosphorylationIAHPALPTIPERKEV
CCCCCCCCCCHHHHH		50.4422199227
507UbiquitinationPALPTIPERKEVLLE
CCCCCCCHHHHHHHH		72.9624816145
521AcetylationEASEETGKRVSKFKA
HHHHHHCHHHHHHHH		57.9826051181
525UbiquitinationETGKRVSKFKAARLQ
HHCHHHHHHHHHHHH		48.2924816145
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
372SPhosphorylationKinasePRKACAP17612
GPS
372SPhosphorylationKinaseP70S6KP23443
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
372SPhosphorylation

17936702
372SPhosphorylation

17936702
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 RMP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DMAP1_HUMANDMAP1physical
15367675
RMP_HUMANURI1physical
15367675
UXT_HUMANUXTphysical
21730289
A4_HUMANAPPphysical
21832049
PP1R7_HUMANPPP1R7physical
27173435
PFD2_HUMANPFDN2physical
28561026
PIHD1_HUMANPIH1D1physical
28561026
RPA1_HUMANPOLR1Aphysical
28561026
RPAC1_HUMANPOLR1Cphysical
28561026
RPB1_HUMANPOLR2Aphysical
28561026
RPB2_HUMANPOLR2Bphysical
28561026
RPAB1_HUMANPOLR2Ephysical
28561026
RPC1_HUMANPOLR3Aphysical
28561026
RPC2_HUMANPOLR3Bphysical
28561026
PP1A_HUMANPPP1CAphysical
28561026
PP1G_HUMANPPP1CCphysical
28561026
PRP8_HUMANPRPF8physical
28561026
RPAP2_HUMANRPAP2physical
28561026
RPAP3_HUMANRPAP3physical
28561026
RUVB1_HUMANRUVBL1physical
28561026
RUVB2_HUMANRUVBL2physical
28561026
TNG6_HUMANTANGO6physical
28561026
TSC1_HUMANTSC1physical
28561026
RMP_HUMANURI1physical
28561026
WDR92_HUMANWDR92physical
28561026
RPAP3_HUMANRPAP3physical
27780869
RPC1_HUMANPOLR3Aphysical
27780869
RPAB1_HUMANPOLR2Ephysical
27780869
WDR92_HUMANWDR92physical
27780869
LMNA_HUMANLMNAphysical
27780869
PFD6_HUMANPFDN6physical
27780869
PFD2_HUMANPFDN2physical
27780869
PIHD1_HUMANPIH1D1physical
27780869
PDRG1_HUMANPDRG1physical
27780869
RPC5_HUMANPOLR3Ephysical
27780869
UXT_HUMANUXTphysical
27780869
RPC2_HUMANPOLR3Bphysical
27780869
RPA1_HUMANPOLR1Aphysical
27780869
RPAC1_HUMANPOLR1Cphysical
27780869
PKP3_HUMANPKP3physical
27780869
RPC4_HUMANPOLR3Dphysical
27780869
1433B_HUMANYWHABphysical
27780869
RPAB3_HUMANPOLR2Hphysical
27780869
GPN3_HUMANGPN3physical
27780869
METK2_HUMANMAT2Aphysical
27780869
SPT6H_HUMANSUPT6Hphysical
27780869
K1C18_HUMANKRT18physical
27780869
PCBP2_HUMANPCBP2physical
27780869
NOP58_HUMANNOP58physical
27780869
PP2AB_HUMANPPP2CBphysical
27780869
TIF1B_HUMANTRIM28physical
27780869
RPB1_HUMANPOLR2Aphysical
27780869
NOC4L_HUMANNOC4Lphysical
27780869
ZCCHV_HUMANZC3HAV1physical
27780869
RPR1B_HUMANRPRD1Bphysical
27780869
DNJA2_HUMANDNAJA2physical
27780869
PFD5_HUMANPFDN5physical
27780869
PP1B_HUMANPPP1CBphysical
27780869
PP1A_HUMANPPP1CAphysical
27780869
2AAA_HUMANPPP2R1Aphysical
27780869
RUVB1_HUMANRUVBL1physical
27780869
RUVB2_HUMANRUVBL2physical
27780869
PP2AA_HUMANPPP2CAphysical
27780869
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 RMP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"URI is an oncogene amplified in ovarian cancer cells and is requiredfor their survival.";
Theurillat J.P., Metzler S.C., Henzi N., Djouder N., Helbling M.,Zimmermann A.K., Jacob F., Soltermann A., Caduff R.,Heinzelmann-Schwarz V., Moch H., Krek W.;
Cancer Cell 19:317-332(2011).
Cited for: FUNCTION, INTERACTION WITH PPP1CC, PHOSPHORYLATION AT SER-372,MUTAGENESIS OF SER-372, AND TISSUE SPECIFICITY.
"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexesactivates a negative feedback program that counters S6K1 survivalsignaling.";
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,Aebersold R., Hess D., Krek W.;
Mol. Cell 28:28-40(2007).
Cited for: FUNCTION IN DEPHOSPHORYLATION OF PPP1CC, PHOSPHORYLATION AT SER-372 BYRPS6KB1, MUTAGENESIS OF SER-372, SUBCELLULAR LOCATION, ANDIDENTIFICATION BY SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-241; THR-242; SER-243AND SER-244, AND MASS SPECTROMETRY.

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