dbPTM

RIR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RIR1_HUMAN
UniProt AC	P23921
Protein Name	Ribonucleoside-diphosphate reductase large subunit
Gene Name	RRM1
Organism	Homo sapiens (Human).
Sequence Length	792
Subcellular Localization	Cytoplasm.
Protein Description	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides..
Protein Sequence	MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MHVIKRDGRQER ---CCEECCCCCCHH	43.26	-
17	2-Hydroxyisobutyrylation	QERVMFDKITSRIQK CHHHCHHHHHHHHHH	36.30	-
17	Acetylation	QERVMFDKITSRIQK CHHHCHHHHHHHHHH	36.30	19608861
17	Ubiquitination	QERVMFDKITSRIQK CHHHCHHHHHHHHHH	36.30	21890473
24	Acetylation	KITSRIQKLCYGLNM HHHHHHHHHHHCCCC	37.85	25953088
24	Ubiquitination	KITSRIQKLCYGLNM HHHHHHHHHHHCCCC	37.85	21906983
70	Ubiquitination	TAATLTTKHPDYAIL HHHHHCCCCCCHHHH	48.15	-
74	Phosphorylation	LTTKHPDYAILAARI HCCCCCCHHHHHHHH	10.45	-
80	Methylation	DYAILAARIAVSNLH CHHHHHHHHHHHHHC	16.28	115492899
88	2-Hydroxyisobutyrylation	IAVSNLHKETKKVFS HHHHHHCHHHHHHHH	70.96	-
88	Ubiquitination	IAVSNLHKETKKVFS HHHHHHCHHHHHHHH	70.96	-
92	Ubiquitination	NLHKETKKVFSDVME HHCHHHHHHHHHHHH	56.80	21906983
102	Phosphorylation	SDVMEDLYNYINPHN HHHHHHHHHHHCCCC	20.45	17360941
104	Phosphorylation	VMEDLYNYINPHNGK HHHHHHHHHCCCCCC	6.63	17360941
111	Ubiquitination	YINPHNGKHSPMVAK HHCCCCCCCCCCHHH	46.34	21906983
113	Phosphorylation	NPHNGKHSPMVAKST CCCCCCCCCCHHHHH	20.41	20068231
118	Ubiquitination	KHSPMVAKSTLDIVL CCCCCHHHHHHHEEE	32.34	-
119	Phosphorylation	HSPMVAKSTLDIVLA CCCCHHHHHHHEEEE	25.19	28450419
120	Phosphorylation	SPMVAKSTLDIVLAN CCCHHHHHHHEEEEC	27.95	28450419
128	2-Hydroxyisobutyrylation	LDIVLANKDRLNSAI HHEEEECHHHCCEEE	38.32	-
128	Ubiquitination	LDIVLANKDRLNSAI HHEEEECHHHCCEEE	38.32	21906983
133	Phosphorylation	ANKDRLNSAIIYDRD ECHHHCCEEEEECCC	25.99	23312004
137	Phosphorylation	RLNSAIIYDRDFSYN HCCEEEEECCCCCCC	9.98	20068231
142	Phosphorylation	IIYDRDFSYNYFGFK EEECCCCCCCCCCCE	19.43	21712546
149	Ubiquitination	SYNYFGFKTLERSYL CCCCCCCEECCEEEE	53.21	21906983
154	Phosphorylation	GFKTLERSYLLKING CCEECCEEEEEEECC	15.68	24719451
155	Phosphorylation	FKTLERSYLLKINGK CEECCEEEEEEECCE	23.44	24719451
158	Ubiquitination	LERSYLLKINGKVAE CCEEEEEEECCEECC	31.37	21890473
162	Ubiquitination	YLLKINGKVAERPQH EEEEECCEECCCCCE	33.51	-
180	Ubiquitination	RVSVGIHKEDIDAAI EEEECCCHHHHHHHH	55.98	21906983
202	Phosphorylation	ERWFTHASPTLFNAG HHHCCCCCCCCCCCC	15.71	21601212
232	Phosphorylation	DDSIEGIYDTLKQCA CCCHHHHHHHHHHHH	17.46	28796482
234	Phosphorylation	SIEGIYDTLKQCALI CHHHHHHHHHHHHHH	20.91	28796482
236	Ubiquitination	EGIYDTLKQCALISK HHHHHHHHHHHHHHH	45.48	21906983
243	Acetylation	KQCALISKSAGGIGV HHHHHHHHCCCCCHH	37.01	26051181
243	Ubiquitination	KQCALISKSAGGIGV HHHHHHHHCCCCCHH	37.01	-
253	O-linked_Glycosylation	GGIGVAVSCIRATGS CCCHHHHEEEEECCC	8.29	28510447
253	Phosphorylation	GGIGVAVSCIRATGS CCCHHHHEEEEECCC	8.29	21712546
292	2-Hydroxyisobutyrylation	YVDQGGNKRPGAFAI EECCCCCCCCCEEEE	64.34	-
320	"N6,N6-dimethyllysine"	DLKKNTGKEEQRARD CHHCCCCCHHHHHHH	56.91	-
320	Methylation	DLKKNTGKEEQRARD CHHCCCCCHHHHHHH	56.91	23644510
320	Ubiquitination	DLKKNTGKEEQRARD CHHCCCCCHHHHHHH	56.91	-
369	Ubiquitination	VWGEEFEKLYASYEK HHHHHHHHHHHHHHH	52.71	-
376	2-Hydroxyisobutyrylation	KLYASYEKQGRVRKV HHHHHHHHCCCHHHH	50.23	-
376	Acetylation	KLYASYEKQGRVRKV HHHHHHHHCCCHHHH	50.23	19608861
376	Ubiquitination	KLYASYEKQGRVRKV HHHHHHHHCCCHHHH	50.23	21890473
414	Ubiquitination	YKDSCNRKSNQQNLG EECCCCCCCCCCCCC	39.50	21906983
415	Phosphorylation	KDSCNRKSNQQNLGT ECCCCCCCCCCCCCC	36.31	25159151
422	Phosphorylation	SNQQNLGTIKCSNLC CCCCCCCCCEECCHH	22.04	20068231
424	Ubiquitination	QQNLGTIKCSNLCTE CCCCCCCEECCHHHH	31.30	-
437	Phosphorylation	TEIVEYTSKDEVAVC HHHHHCCCCCCHHHH	36.89	21601212
464	Ubiquitination	SEHTYDFKKLAEVTK CCCCCCHHHHHHHHH	43.94	-
465	Ubiquitination	EHTYDFKKLAEVTKV CCCCCHHHHHHHHHH	53.58	21906983
471	2-Hydroxyisobutyrylation	KKLAEVTKVVVRNLN HHHHHHHHHHHCCCH	37.90	-
471	Ubiquitination	KKLAEVTKVVVRNLN HHHHHHHHHHHCCCH	37.90	21906983
479	Ubiquitination	VVVRNLNKIIDINYY HHHCCCHHCCCEEEE	44.18	-
485	Phosphorylation	NKIIDINYYPVPEAC HHCCCEEEEECCHHH	14.96	28152594
486	Phosphorylation	KIIDINYYPVPEACL HCCCEEEEECCHHHH	8.02	28152594
494	Phosphorylation	PVPEACLSNKRHRPI ECCHHHHCCCCCCCC	39.94	28152594
496	Acetylation	PEACLSNKRHRPIGI CHHHHCCCCCCCCCC	46.32	23954790
496	Ubiquitination	PEACLSNKRHRPIGI CHHHHCCCCCCCCCC	46.32	21906983
548	Ubiquitination	EASCDLAKEQGPYET HHHCHHHHHHCCCCC	58.84	-
553	Phosphorylation	LAKEQGPYETYEGSP HHHHHCCCCCCCCCC	27.94	28152594
555	Phosphorylation	KEQGPYETYEGSPVS HHHCCCCCCCCCCCC	22.49	28152594
556	Phosphorylation	EQGPYETYEGSPVSK HHCCCCCCCCCCCCC	13.32	28152594
559	Phosphorylation	PYETYEGSPVSKGIL CCCCCCCCCCCCCEE	15.36	28152594
563	Ubiquitination	YEGSPVSKGILQYDM CCCCCCCCCEEEEEC	50.64	-
582	Ubiquitination	PTDLWDWKVLKEKIA CCCCCCHHHHHHHHH	34.91	-
587	Ubiquitination	DWKVLKEKIAKYGIR CHHHHHHHHHHHCCC	46.51	-
590	Acetylation	VLKEKIAKYGIRNSL HHHHHHHHHCCCCCE	47.70	25953088
590	Ubiquitination	VLKEKIAKYGIRNSL HHHHHHHHHCCCCCE	47.70	21890473
596	Phosphorylation	AKYGIRNSLLIAPMP HHHCCCCCEEEEECC	18.07	24144214
604	Phosphorylation	LLIAPMPTASTAQIL EEEEECCCCCHHHHH	27.30	21712546
606	O-linked_Glycosylation	IAPMPTASTAQILGN EEECCCCCHHHHHCC	27.10	28510447
606	Phosphorylation	IAPMPTASTAQILGN EEECCCCCHHHHHCC	27.10	24144214
607	Phosphorylation	APMPTASTAQILGNN EECCCCCHHHHHCCC	21.81	24144214
616	Phosphorylation	QILGNNESIEPYTSN HHHCCCCCCCCCCCC	34.08	24144214
620	Phosphorylation	NNESIEPYTSNIYTR CCCCCCCCCCCCCEE	15.26	24144214
621	Phosphorylation	NESIEPYTSNIYTRR CCCCCCCCCCCCEEC	26.47	24144214
622	Phosphorylation	ESIEPYTSNIYTRRV CCCCCCCCCCCEECC	18.52	24144214
625	Phosphorylation	EPYTSNIYTRRVLSG CCCCCCCCEECCCCC	9.84	24144214
626	Phosphorylation	PYTSNIYTRRVLSGE CCCCCCCEECCCCCC	14.27	24144214
631	Phosphorylation	IYTRRVLSGEFQIVN CCEECCCCCCCEEEC	33.16	28450419
643	Ubiquitination	IVNPHLLKDLTERGL EECHHHHHHHHHCCC	57.99	21890473
655	Sulfoxidation	RGLWHEEMKNQIIAC CCCCCHHHHHCEEEE	4.50	30846556
656	Ubiquitination	GLWHEEMKNQIIACN CCCCHHHHHCEEEEC	49.32	-
677	Ubiquitination	PEIPDDLKQLYKTVW CCCCHHHHHHHHHHH	45.30	-
681	Ubiquitination	DDLKQLYKTVWEISQ HHHHHHHHHHHHHCH	45.23	21906983
682	O-linked_Glycosylation	DLKQLYKTVWEISQK HHHHHHHHHHHHCHH	19.79	28510447
689	Acetylation	TVWEISQKTVLKMAA HHHHHCHHHHHHHHH	33.53	25953088
689	Ubiquitination	TVWEISQKTVLKMAA HHHHHCHHHHHHHHH	33.53	21906983
693	Acetylation	ISQKTVLKMAAERGA HCHHHHHHHHHHCCC	23.35	26051181
693	Ubiquitination	ISQKTVLKMAAERGA HCHHHHHHHHHHCCC	23.35	21906983
721	Phosphorylation	EPNYGKLTSMHFYGW CCCCCCCEEEEECCC	27.73	24719451
722	Phosphorylation	PNYGKLTSMHFYGWK CCCCCCEEEEECCCC	22.24	28348404
726	Phosphorylation	KLTSMHFYGWKQGLK CCEEEEECCCCCCCC	13.85	29978859
729	Acetylation	SMHFYGWKQGLKTGM EEEECCCCCCCCCEE	30.08	25953088
729	Ubiquitination	SMHFYGWKQGLKTGM EEEECCCCCCCCCEE	30.08	-
733	Ubiquitination	YGWKQGLKTGMYYLR CCCCCCCCCEEEEEC	50.27	-
734	O-linked_Glycosylation	GWKQGLKTGMYYLRT CCCCCCCCEEEEECC	32.02	28510447
734	Phosphorylation	GWKQGLKTGMYYLRT CCCCCCCCEEEEECC	32.02	21406692
737	Phosphorylation	QGLKTGMYYLRTRPA CCCCCEEEEECCCCC	10.74	21406692
738	Phosphorylation	GLKTGMYYLRTRPAA CCCCEEEEECCCCCC	4.84	21406692
741	Phosphorylation	TGMYYLRTRPAANPI CEEEEECCCCCCCCE	38.11	21406692
751	Phosphorylation	AANPIQFTLNKEKLK CCCCEEEEECHHHHC	17.04	25159151
754	Acetylation	PIQFTLNKEKLKDKE CEEEEECHHHHCCHH	60.38	26051181
754	Ubiquitination	PIQFTLNKEKLKDKE CEEEEECHHHHCCHH	60.38	21890473
756	Ubiquitination	QFTLNKEKLKDKEKV EEEECHHHHCCHHHC	63.55	-
762	Ubiquitination	EKLKDKEKVSKEEEE HHHCCHHHCCHHHHH	58.51	-
764	O-linked_Glycosylation	LKDKEKVSKEEEEKE HCCHHHCCHHHHHHH	45.47	28510447
765	Ubiquitination	KDKEKVSKEEEEKER CCHHHCCHHHHHHHH	72.61	-
770	Ubiquitination	VSKEEEEKERNTAAM CCHHHHHHHHHHHHH	66.31	-
774	Phosphorylation	EEEKERNTAAMVCSL HHHHHHHHHHHHHCC	23.24	21712546
780	O-linked_Glycosylation	NTAAMVCSLENRDEC HHHHHHHCCCCCCCC	27.58	28510447
780	Phosphorylation	NTAAMVCSLENRDEC HHHHHHHCCCCCCCC	27.58	22617229
792	Phosphorylation	DECLMCGS------- CCCCCCCC-------	31.92	29978859

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF2	Q99496	PMID:24614341
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1	P35226	PMID:24614341

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RIR1_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 RIR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RIR2_HUMAN	RRM2	physical	14583450
RIR2B_HUMAN	RRM2B	physical	14583450
LRIF1_HUMAN	LRIF1	physical	16169070
RIR1_HUMAN	RRM1	physical	11781084
RIR2_HUMAN	RRM2	physical	11781084
KAT5_HUMAN	KAT5	physical	20159953
RIR2_HUMAN	RRM2	physical	20159953
RIR2B_HUMAN	RRM2B	physical	20159953
SPHM_HUMAN	SGSH	physical	22939629
SUCB1_HUMAN	SUCLA2	physical	22939629
TM177_HUMAN	TMEM177	physical	22939629
TNPO1_HUMAN	TNPO1	physical	22863883
RING2_HUMAN	RNF2	physical	24614341
BMI1_HUMAN	BMI1	physical	24614341
RIR1_HUMAN	RRM1	physical	25416956
RIR2_HUMAN	RRM2	physical	26344197
MDM2_HUMAN	MDM2	physical	26228206
RIR2B_HUMAN	RRM2B	physical	28514442
GLRX3_HUMAN	GLRX3	physical	28514442
RIR2_HUMAN	RRM2	physical	28514442
ARL5B_HUMAN	ARL5B	physical	28514442

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 RIR1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-376, AND MASSSPECTROMETRY.	19608861 [Abstract]