dbPTM

NRIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NRIP1_HUMAN
UniProt AC	P48552
Protein Name	Nuclear receptor-interacting protein 1
Gene Name	NRIP1
Organism	Homo sapiens (Human).
Sequence Length	1158
Subcellular Localization	Nucleus . Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1.
Protein Description	Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors. Positive regulator of the circadian clock gene expression: stimulates transcription of ARNTL/BMAL1, CLOCK and CRY1 by acting as a coactivator for RORA and RORC..
Protein Sequence	MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTHGEELGS ------CCCHHHCCC	50.31	24043423
9	Phosphorylation	THGEELGSDVHQDSI CCHHHCCCCCCCHHH	49.43	24043423
15	Phosphorylation	GSDVHQDSIVLTYLE CCCCCCHHHHHHHHH	14.18	24043423
19	Phosphorylation	HQDSIVLTYLEGLLM CCHHHHHHHHHHHHH	18.37	24043423
20	Phosphorylation	QDSIVLTYLEGLLMH CHHHHHHHHHHHHHH	9.90	24043423
33	Phosphorylation	MHQAAGGSGTAVDKK HHHHCCCCCCCCCCC	31.86	24043423
35	Phosphorylation	QAAGGSGTAVDKKSA HHCCCCCCCCCCCCC	25.79	24043423
56	Phosphorylation	QNFNISGSAFPTCQS CCEEECCCCCCCCCC	21.68	22210691
60	Phosphorylation	ISGSAFPTCQSNGPV ECCCCCCCCCCCCCE	19.41	22210691
73	Phosphorylation	PVLNTHTYQGSGMLH CEECCCEECCCCCEE	11.85	22210691
89	Phosphorylation	KKARLLQSSEDWNAA HHHHHHCCCCCHHHH	35.35	29978859
90	Phosphorylation	KARLLQSSEDWNAAK HHHHHCCCCCHHHHH	26.98	29978859
97	Methylation	SEDWNAAKRKRLSDS CCCHHHHHHHHHHHH	56.92	115976721
97	Ubiquitination	SEDWNAAKRKRLSDS CCCHHHHHHHHHHHH	56.92	21890473
102	Phosphorylation	AAKRKRLSDSIMNLN HHHHHHHHHHHHCCC	33.09	25159151
104	Phosphorylation	KRKRLSDSIMNLNVK HHHHHHHHHHCCCHH	21.99	-
111	Sumoylation	SIMNLNVKKEALLAG HHHCCCHHHHHHHHH	43.77	-
111	Acetylation	SIMNLNVKKEALLAG HHHCCCHHHHHHHHH	43.77	15879431
111	Sumoylation	SIMNLNVKKEALLAG HHHCCCHHHHHHHHH	43.77	28112733
122	Phosphorylation	LLAGMVDSVPKGKQD HHHHHCCCCCCCCHH	28.98	-
158	Acetylation	QQIRQSLKEQGYALS HHHHHHHHHCCCCCC	53.92	15879431
170	Sumoylation	ALSHDSLKVEKDLRC CCCCCCCCCCCCHHH	52.91	28112733
178	Phosphorylation	VEKDLRCYGVASSHL CCCCHHHHHHHHHHH	14.27	20068231
187	Phosphorylation	VASSHLKTLLKKSKV HHHHHHHHHHHHHCC	43.62	20068231
195	Sumoylation	LLKKSKVKDQKPDTN HHHHHCCCCCCCCCC	59.17	28112733
198	Sumoylation	KSKVKDQKPDTNLPD HHCCCCCCCCCCCCH	55.80	28112733
207	O-linked_Glycosylation	DTNLPDVTKNLIRDR CCCCCHHHHHHHHHH	22.92	30379171
207	Phosphorylation	DTNLPDVTKNLIRDR CCCCCHHHHHHHHHH	22.92	-
208	Ubiquitination	TNLPDVTKNLIRDRF CCCCHHHHHHHHHHH	49.99	-
218	Phosphorylation	IRDRFAESPHHVGQS HHHHHHCCCCCCCCC	26.55	25849741
225	Phosphorylation	SPHHVGQSGTKVMSE CCCCCCCCCCCCCCC	42.36	28348404
227	Phosphorylation	HHVGQSGTKVMSEPL CCCCCCCCCCCCCCC	26.22	28348404
239	Methylation	EPLSCAARLQAVASM CCCHHHHHHHHHHHH	14.60	4726607
252	Phosphorylation	SMVEKRASPATSPKP HHHHHHCCCCCCCCH	21.07	22617229
255	Phosphorylation	EKRASPATSPKPSVA HHHCCCCCCCCHHHH	49.28	22617229
256	Phosphorylation	KRASPATSPKPSVAC HHCCCCCCCCHHHHH	32.79	25849741
260	Phosphorylation	PATSPKPSVACSQLA CCCCCCHHHHHHHHH	28.59	28348404
264	Phosphorylation	PKPSVACSQLALLLS CCHHHHHHHHHHHHC	20.63	28348404
286	Acetylation	YSREHALKTQNANQA HHHHHHHHHCCHHHH	49.17	15879431
286	Ubiquitination	YSREHALKTQNANQA HHHHHHHHHCCHHHH	49.17	21906983
310	Acetylation	RLQENGQKDVGSYQL HHHHCCCCCCCCEEC	56.64	15879431
355	Phosphorylation	NPMGIIPSSPKNAGY CCCCCCCCCCCCCCC	49.19	25159151
356	Phosphorylation	PMGIIPSSPKNAGYK CCCCCCCCCCCCCCC	34.24	28857561
362	Phosphorylation	SSPKNAGYKNSLERN CCCCCCCCCCHHHHC	12.46	29396449
372	Sumoylation	SLERNNIKQAANNSL HHHHCCHHHHHHHHH	35.69	28112733
378	Phosphorylation	IKQAANNSLLLHLLK HHHHHHHHHHHHHHH	21.87	-
386	Phosphorylation	LLLHLLKSQTIPKPM HHHHHHHHCCCCCCC	32.31	29978859
388	Phosphorylation	LHLLKSQTIPKPMNG HHHHHHCCCCCCCCC	46.46	29978859
446	Acetylation	VPIDLSCKHRTEKSE EECCCCCCCCCCCCC	32.52	11509661
449	Phosphorylation	DLSCKHRTEKSESDQ CCCCCCCCCCCCCCC	47.70	22798277
452	Phosphorylation	CKHRTEKSESDQPVS CCCCCCCCCCCCCCC	35.78	22798277
454	Phosphorylation	HRTEKSESDQPVSLD CCCCCCCCCCCCCHH	48.95	22798277
459	Phosphorylation	SESDQPVSLDNFTQS CCCCCCCCHHHHHHH	36.37	22798277
464	Phosphorylation	PVSLDNFTQSLLNTW CCCHHHHHHHHHHCC	24.41	22798277
466	Phosphorylation	SLDNFTQSLLNTWDP CHHHHHHHHHHCCCC	31.59	22798277
481	Acetylation	KVPDVDIKEDQDTSK CCCCCCCCCCCCCCC	51.26	19666589
487	Phosphorylation	IKEDQDTSKNSKLNS CCCCCCCCCCCCCCH	37.82	-
508	Sumoylation	LQLLLGHKNEENVEK HHHHHCCCCHHHHHC	65.34	28112733
517	Phosphorylation	EENVEKNTSPQGVHN HHHHHCCCCCCCCCC	53.50	23312004
518	Phosphorylation	ENVEKNTSPQGVHND HHHHCCCCCCCCCCC	25.31	25849741
528	Acetylation	GVHNDVSKFNTQNYA CCCCCHHHCHHCCCC	42.34	-
528	Ubiquitination	GVHNDVSKFNTQNYA CCCCCHHHCHHCCCC	42.34	-
542	Phosphorylation	ARTSVIESPSTNRTT CCEEEEECCCCCCCC	17.02	26699800
544	Phosphorylation	TSVIESPSTNRTTPV EEEEECCCCCCCCCC	47.82	28985074
545	Phosphorylation	SVIESPSTNRTTPVS EEEECCCCCCCCCCC	31.91	26699800
548	Phosphorylation	ESPSTNRTTPVSTPP ECCCCCCCCCCCCCC	37.21	28985074
549	Phosphorylation	SPSTNRTTPVSTPPL CCCCCCCCCCCCCCC	20.61	27732954
552	Phosphorylation	TNRTTPVSTPPLLTS CCCCCCCCCCCCCCC	36.08	27732954
553	Phosphorylation	NRTTPVSTPPLLTSS CCCCCCCCCCCCCCC	29.20	29759185
558	Phosphorylation	VSTPPLLTSSKAGSP CCCCCCCCCCCCCCC	38.34	22115753
559	Phosphorylation	STPPLLTSSKAGSPI CCCCCCCCCCCCCCC	29.79	22115753
564	Phosphorylation	LTSSKAGSPINLSQH CCCCCCCCCCCCCCC	27.71	25159151
569	Phosphorylation	AGSPINLSQHSLVIK CCCCCCCCCCEEEEE	22.74	23312004
572	Phosphorylation	PINLSQHSLVIKWNS CCCCCCCEEEEECCC	19.39	23186163
579	Phosphorylation	SLVIKWNSPPYVCST EEEEECCCCCCEECC	26.57	28348404
590	Methylation	VCSTQSEKLTNTASN EECCCCHHHCCCCCC	66.90	19216533
596	Phosphorylation	EKLTNTASNHSMDLT HHHCCCCCCCCCCCC	32.79	-
599	Phosphorylation	TNTASNHSMDLTKSK CCCCCCCCCCCCCCC	20.45	-
603	Phosphorylation	SNHSMDLTKSKDPPG CCCCCCCCCCCCCCC	29.07	-
606	Acetylation	SMDLTKSKDPPGEKP CCCCCCCCCCCCCCC	75.66	-
626	Phosphorylation	AQNSATFSASKLLQN CCCCHHHCHHHHHHH	27.55	25627689
628	Phosphorylation	NSATFSASKLLQNLA CCHHHCHHHHHHHHH	23.72	25627689
649	Methylation	SMSVEEQRPSKQLLT CCCHHHHCCCCCCCC	40.51	4726603
652	Methylation	VEEQRPSKQLLTGNT HHHHCCCCCCCCCCC	47.88	19216533
656	Phosphorylation	RPSKQLLTGNTDKPI CCCCCCCCCCCCCCC	36.66	-
659	Phosphorylation	KQLLTGNTDKPIGMI CCCCCCCCCCCCCHH	46.90	-
671	Phosphorylation	GMIDRLNSPLLSNKT CHHHHCCCCCCCCCC	22.86	25849741
677	Ubiquitination	NSPLLSNKTNAVEEN CCCCCCCCCCHHHHC	39.52	-
688	Phosphorylation	VEENKAFSSQPTGPE HHHCCCCCCCCCCCC	32.68	22210691
689	Phosphorylation	EENKAFSSQPTGPEP HHCCCCCCCCCCCCC	33.45	22210691
731	Phosphorylation	KSEKKEKTPLRDEST CCCCCCCCCCCCCHH	28.75	17924679
756	Sumoylation	QILMVKIKSEPCDDL CEEEEEECCCCCCCC	42.95	-
756	Methylation	QILMVKIKSEPCDDL CEEEEEECCCCCCCC	42.95	19216533
756	Sumoylation	QILMVKIKSEPCDDL CEEEEEECCCCCCCC	42.95	28112733
798	Phosphorylation	SAPALPVSEDFKSEP CCCCCCCCCCCCCCC	29.52	23401153
802	Sumoylation	LPVSEDFKSEPVSPQ CCCCCCCCCCCCCHH	67.25	28112733
803	Phosphorylation	PVSEDFKSEPVSPQD CCCCCCCCCCCCHHH	47.31	28450419
807	Phosphorylation	DFKSEPVSPQDFSFS CCCCCCCCHHHCCCC	27.79	23401153
812	Phosphorylation	PVSPQDFSFSKNGLL CCCHHHCCCCHHCHH	36.58	28450419
814	Phosphorylation	SPQDFSFSKNGLLSR CHHHCCCCHHCHHHH	24.82	28450419
850	Methylation	EMALLESKNLCMVPK HHHHHHHCCCCCCCC	44.56	-
850	Sumoylation	EMALLESKNLCMVPK HHHHHHHCCCCCCCC	44.56	28112733
862	Phosphorylation	VPKKRKLYTEPLENP CCCCCCCCCCCCCCH	16.46	24719451
863	Phosphorylation	PKKRKLYTEPLENPF CCCCCCCCCCCCCHH	41.38	24719451
891	Phosphorylation	HSAPEVLYGSLLNQE CCCHHHHHHHCCCHH	15.16	27642862
901	Sumoylation	LLNQEELKFSRNDLE CCCHHHHCCCCCCEE	44.57	28112733
911	Phosphorylation	RNDLEFKYPAGHGSA CCCEEECCCCCCCCC	12.02	-
917	Phosphorylation	KYPAGHGSASESEHR CCCCCCCCCCHHHHH	23.97	23898821
921	Phosphorylation	GHGSASESEHRSWAR CCCCCCHHHHHHHHH	35.89	-
931	Sumoylation	RSWARESKSFNVLKQ HHHHHHCCHHHHHHH	55.07	-
931	Acetylation	RSWARESKSFNVLKQ HHHHHHCCHHHHHHH	55.07	15879431
931	Sumoylation	RSWARESKSFNVLKQ HHHHHHCCHHHHHHH	55.07	28112733
947	Methylation	LLSENCVRDLSPHRS HHCCCCCHHCCCCCC	41.16	4726599
954	Phosphorylation	RDLSPHRSNSVADSK HHCCCCCCCCHHHHH	30.35	20363803
963	Acetylation	SVADSKKKGHKNNVT CHHHHHCCCCCCCCC	70.73	20167786
966	Acetylation	DSKKKGHKNNVTNSK HHHCCCCCCCCCCCC	59.91	20167786
999	Phosphorylation	SSCMDNRTFSYPGVV CCCCCCCCCCCCCCE	24.16	22210691
1001	Phosphorylation	CMDNRTFSYPGVVKT CCCCCCCCCCCCEEC	29.79	22985185
1002	Phosphorylation	MDNRTFSYPGVVKTP CCCCCCCCCCCEECC	10.38	22210691
1008	Phosphorylation	SYPGVVKTPVSPTFP CCCCCEECCCCCCCH	19.81	23312004
1011	Phosphorylation	GVVKTPVSPTFPEHL CCEECCCCCCCHHHC	21.30	25849741
1013	Phosphorylation	VKTPVSPTFPEHLGC EECCCCCCCHHHCCC	44.29	23312004
1034	Phosphorylation	SGLLNGCSMPSEKGP CCCCCCCCCCCCCCC	34.82	20068231
1051	Ubiquitination	WVITDAEKNEYEKDS EEEEHHHHCCCCCCC	57.72	-
1069	Phosphorylation	TKTNPILYYMLQKGG CCCCHHHHHHHHCCC	6.37	17360941
1070	Phosphorylation	KTNPILYYMLQKGGN CCCHHHHHHHHCCCC	6.47	22210691
1078	Phosphorylation	MLQKGGNSVTSRETQ HHHCCCCCCCCCCCC	30.01	22210691
1095	Phosphorylation	DIWREASSAESVSQV HHHHHHHCCCCHHHH	43.00	-
1100	Phosphorylation	ASSAESVSQVTAKEE HHCCCCHHHHCCCHH	28.36	-
1105	Sumoylation	SVSQVTAKEELLPTA CHHHHCCCHHHCCCH	42.21	-
1105	Sumoylation	SVSQVTAKEELLPTA CHHHHCCCHHHCCCH	42.21	28112733
1105	Ubiquitination	SVSQVTAKEELLPTA CHHHHCCCHHHCCCH	42.21	-
1111	Phosphorylation	AKEELLPTAETKASF CCHHHCCCHHHHHHH	36.78	-
1115	Sumoylation	LLPTAETKASFFNLR HCCCHHHHHHHCCCC	33.27	28112733
1115	Ubiquitination	LLPTAETKASFFNLR HCCCHHHHHHHCCCC	33.27	21890473
1154	Sumoylation	LGSVLTIKKESE--- EEEEEEEEECCC---	45.30	-
1154	Sumoylation	LGSVLTIKKESE--- EEEEEEEEECCC---	45.30	28112733

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 NRIP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NRIP1_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
446	Acetylation	448 (2)	R ⇒ G	rs2229742	Birth weight	27680694

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NR0B1_HUMAN	NR0B1	physical	11459805
LDOC1_HUMAN	LDOC1	physical	16189514
TEX11_HUMAN	TEX11	physical	16189514
CEP70_HUMAN	CEP70	physical	16189514
CC85B_HUMAN	CCDC85B	physical	16189514
CTBP1_HUMAN	CTBP1	physical	15060175
CTBP2_HUMAN	CTBP2	physical	15060175
HDAC5_HUMAN	HDAC5	physical	15060175
GCR_HUMAN	NR3C1	physical	12773562
GCR_HUMAN	NR3C1	physical	11266503
1433T_HUMAN	YWHAQ	physical	11266503
RARA_HUMAN	RARA	physical	12549917
RXRA_HUMAN	RXRA	physical	12549917
JUN_HUMAN	JUN	physical	12554755
RARA_MOUSE	Rara	physical	12403842
RXRB_MOUSE	Rxrb	physical	12403842
ESR1_HUMAN	ESR1	physical	9115274
ESR1_HUMAN	ESR1	physical	8887632
CTBP1_HUMAN	CTBP1	physical	18374649
HDAC3_HUMAN	HDAC3	physical	17053781
CARM1_HUMAN	CARM1	physical	17053781
ANM1_HUMAN	PRMT1	physical	17053781
XPO1_HUMAN	XPO1	physical	17053781
IMB1_HUMAN	KPNB1	physical	17053781
ERR1_HUMAN	ESRRA	physical	16439465
ERR2_HUMAN	ESRRB	physical	16439465
ERR3_HUMAN	ESRRG	physical	16439465
GCR_HUMAN	NR3C1	physical	10659697
THA_HUMAN	THRA	physical	15130509
RARA_HUMAN	RARA	physical	10082574
ESR1_HUMAN	ESR1	physical	9192902
E2F1_HUMAN	E2F1	physical	20410059
ACTN2_HUMAN	ACTN2	physical	15604093
ERR1_HUMAN	ESRRA	physical	15604093
CIB1_HUMAN	CIB1	physical	15604093
NR1H2_HUMAN	NR1H2	physical	15604093
E2F1_HUMAN	E2F1	physical	22629304
A4_HUMAN	APP	physical	21832049
FHL1_HUMAN	FHL1	physical	19401155
CEP70_HUMAN	CEP70	physical	19060904
LDOC1_HUMAN	LDOC1	physical	19060904
DNMT1_HUMAN	DNMT1	physical	17972916
DNM3A_HUMAN	DNMT3A	physical	17972916
DNM3B_HUMAN	DNMT3B	physical	17972916
ARPC3_HUMAN	ARPC3	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681

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 NRIP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Acetylation of nuclear hormone receptor-interacting protein RIP140regulates binding of the transcriptional corepressor CtBP."; Vo N., Fjeld C., Goodman R.H.; Mol. Cell. Biol. 21:6181-6188(2001). Cited for: FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 ANDLYS-446, AND ACETYLATION AT LYS-446.	11509661 [Abstract]
Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-731, AND MASSSPECTROMETRY.	17924679 [Abstract]