dbPTM

RENT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RENT2_HUMAN
UniProt AC	Q9HAU5
Protein Name	Regulator of nonsense transcripts 2
Gene Name	UPF2
Organism	Homo sapiens (Human).
Sequence Length	1272
Subcellular Localization	Cytoplasm, perinuclear region .
Protein Description	Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA..
Protein Sequence	MPAERKKPASMEEKDSLPNNKEKDCSERRTVSSKERPKDDIKLTAKKEVSKAPEDKKKRLEDDKRKKEDKERKKKDEEKVKAEEESKKKEEEEKKKHQEEERKKQEEQAKRQQEEEAAAQMKEKEESIQLHQEAWERHHLRKELRSKNQNAPDSRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKISDVNCAVHLCSLFHQRYADFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKNIINADRESHTHVSVVISFCRHCGDDIAGLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEEFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAILFKDNEKSCQNKESNKDDTKEAKESKENKEVSSPDDLELELENLEINDDTLELEGGDEAEDLTKKLLDEQEQEDEEASTGSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVKKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKDSKDSMTEGENLEEDEEEEEGGAETEEQSGNESEVNEPEEEEGSDNDDDEGEEEEEENTDYLTDSNKENETDEENTEVMIKGGGLKHVPCVEDEDFIQALDKMMLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGEAESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	AERKKPASMEEKDSL CCCCCCCCHHHHCCC	34.94	28348404
26	Phosphorylation	NNKEKDCSERRTVSS CCCCCCHHHCCCCCC	44.25	28258704
30	Phosphorylation	KDCSERRTVSSKERP CCHHHCCCCCCCCCC	30.84	23312004
32	Phosphorylation	CSERRTVSSKERPKD HHHCCCCCCCCCCCC	34.77	28258704
33	Phosphorylation	SERRTVSSKERPKDD HHCCCCCCCCCCCCH	33.91	28258704
58	Trimethylation	KAPEDKKKRLEDDKR CCCHHHHHHHHHHHH	68.88	-
58	Methylation	KAPEDKKKRLEDDKR CCCHHHHHHHHHHHH	68.88	23644510
75	Acetylation	EDKERKKKDEEKVKA HHHHHHHHHHHHHHH	73.70	7681983
79	Acetylation	RKKKDEEKVKAEEES HHHHHHHHHHHHHHH	47.16	7681993
103	Ubiquitination	KHQEEERKKQEEQAK HHHHHHHHHHHHHHH	63.19	-
110	Ubiquitination	KKQEEQAKRQQEEEA HHHHHHHHHHHHHHH	50.89	24816145
121	Sulfoxidation	EEEAAAQMKEKEESI HHHHHHHHHHHHHHH	5.33	28465586
213	Acetylation	VASIVEAKLKISDVN HHHHHHHHHCCCHHH	36.49	26051181
233	Phosphorylation	CSLFHQRYADFAPSL HHHHHHHHHHHHHHH	12.17	-
239	Phosphorylation	RYADFAPSLLQVWKK HHHHHHHHHHHHHHH	37.98	-
256	Phosphorylation	EARKEEKTPNITKLR HHHHHCCCCCHHHHH	25.50	18452278
260	Ubiquitination	EEKTPNITKLRTDLR HCCCCCHHHHHHHHH	30.57	24816145
260	Phosphorylation	EEKTPNITKLRTDLR HCCCCCHHHHHHHHH	30.57	18452278
264	Phosphorylation	PNITKLRTDLRFIAE CCHHHHHHHHHHHEE	50.23	18452278
285	Phosphorylation	FTDKEGLSLIYEQLK EECHHHHHHHHHHHH	24.47	-
288	Phosphorylation	KEGLSLIYEQLKNII HHHHHHHHHHHHHHH	11.69	-
345	Phosphorylation	FPPSEIISPEKQQPF CCHHHCCCHHHCCHH	32.44	-
359	Phosphorylation	FQNLLKEYFTSLTKH HHHHHHHHHHHHHHH	15.57	22817900
365	Acetylation	EYFTSLTKHLKRDHR HHHHHHHHHHHHHHH	52.84	25953088
388	Ubiquitination	NRRILHSKGELSEDR HHHHHHHCCCCCCHH	45.73	29967540
392	Phosphorylation	LHSKGELSEDRHKQY HHHCCCCCCHHHHHH	32.90	28348404
397	Ubiquitination	ELSEDRHKQYEEFAM CCCCHHHHHHHHHHH	56.31	29967540
399	Phosphorylation	SEDRHKQYEEFAMSY CCHHHHHHHHHHHHH	23.41	24043423
405	Phosphorylation	QYEEFAMSYQKLLAN HHHHHHHHHHHHHHC	22.45	26270265
406	Phosphorylation	YEEFAMSYQKLLANS HHHHHHHHHHHHHCC	9.15	26270265
460	Ubiquitination	DLEGGIWEDEDARNF CCCCCCCCCHHHHHH	49.99	24816145
468	Phosphorylation	DEDARNFYENLIDLK CHHHHHHHHHHHHHH	13.88	27642862
484	Acetylation	FVPAILFKDNEKSCQ HHHHHHCCCCHHHHC	57.08	26051181
500	O-linked_Glycosylation	KESNKDDTKEAKESK CCCCCCHHHHHHHHH	40.70	30379171
506	Phosphorylation	DTKEAKESKENKEVS HHHHHHHHHHCCCCC	44.56	30576142
513	Phosphorylation	SKENKEVSSPDDLEL HHHCCCCCCCHHHHH	36.93	28102081
514	Phosphorylation	KENKEVSSPDDLELE HHCCCCCCCHHHHHH	37.21	28102081
597	Phosphorylation	DFCMNMNTKANRKKL HHHHHCCCHHHHHHH	22.29	21406692
663	Ubiquitination	DQINIETKNKTVRFI HHEEEECCCCEEEEE	43.59	24816145
744	Phosphorylation	AMHLDARYVTMVENA HCCCCHHHHEEEECC	11.29	23401153
746	Phosphorylation	HLDARYVTMVENAYY CCCHHHHEEEECCHH	13.43	23401153
749	Ubiquitination	ARYVTMVENAYYYCN HHHHEEEECCHHCCC	25.89	24816145
752	Phosphorylation	VTMVENAYYYCNPPP HEEEECCHHCCCCCC	13.42	23401153
753	Phosphorylation	TMVENAYYYCNPPPA EEEECCHHCCCCCCH	10.11	23401153
754	Phosphorylation	MVENAYYYCNPPPAE EEECCHHCCCCCCHH	3.51	23401153
767	Malonylation	AEKTVKKKRPPLQEY HHHCCCCCCCCHHHH	65.50	26320211
780	Phosphorylation	EYVRKLLYKDLSKVT HHHHHHHHHHHHHCC	16.94	29083192
781	Ubiquitination	YVRKLLYKDLSKVTT HHHHHHHHHHHHCCH	52.76	29967540
784	Phosphorylation	KLLYKDLSKVTTEKV HHHHHHHHHCCHHHH	34.90	29083192
787	Phosphorylation	YKDLSKVTTEKVLRQ HHHHHHCCHHHHHHH	32.73	29083192
788	Phosphorylation	KDLSKVTTEKVLRQM HHHHHCCHHHHHHHH	36.47	29083192
790	Malonylation	LSKVTTEKVLRQMRK HHHCCHHHHHHHHHC	44.47	30639696
863	Ubiquitination	GMEVNQPKFNQRRIS CCCCCCCCCCHHHHH	47.37	24816145
937	Phosphorylation	GQYFDRGSSKRKLDC HHHCCCCCCCCCHHE	33.31	24260401
941	Acetylation	DRGSSKRKLDCFLVY CCCCCCCCHHEEEHH	53.03	7671065
964	Acetylation	KSLEVWTKDHPFPID HHHHHHCCCCCCCCC	38.02	11925883
974	Phosphorylation	PFPIDIDYMISDTLE CCCCCHHHHHHHHHH	9.18	22817900
1088	Phosphorylation	DSNKENETDEENTEV CCCCCCCCCCCCCEE	61.36	29255136
1093	Phosphorylation	NETDEENTEVMIKGG CCCCCCCCEEEEECC	32.98	20068231
1107	Glutathionylation	GGLKHVPCVEDEDFI CCCCCCCCCCCHHHH	5.21	22555962
1152	Ubiquitination	HLKSQLRKGPPLGGG HHHHHHHCCCCCCCC	81.83	24816145
1216	Phosphorylation	RMRMKKLTLDINERQ HHHHHHHHHCCHHHH	31.12	23312004
1228	Phosphorylation	ERQEQEDYQEMLQSL HHHHHHHHHHHHHHH	12.96	28796482
1234	Phosphorylation	DYQEMLQSLAQRPAP HHHHHHHHHHCCCCC	23.01	29978859
1244	Phosphorylation	QRPAPANTNRERRPR CCCCCCCCCCCCCCC	37.45	23312004
1266	Methylation	PNADLIFKTGGRRR- CCCCEEEECCCCCC-	38.99	115978941

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 RENT2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RENT2_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 RENT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS25_HUMAN	RPS25	physical	15231747
IF4A1_HUMAN	EIF4A1	physical	11073994
XRN2_HUMAN	XRN2	physical	15231747
RENT2_HUMAN	UPF2	physical	14527413
REN3B_HUMAN	UPF3B	physical	14527413
DCP2_HUMAN	DCP2	physical	14527413
XRN1_HUMAN	XRN1	physical	14527413
EXOSX_HUMAN	EXOSC10	physical	14527413
EXOS2_HUMAN	EXOSC2	physical	14527413
EXOS4_HUMAN	EXOSC4	physical	14527413
PARN_HUMAN	PARN	physical	14527413
SMG1_HUMAN	SMG1	physical	11544179
RENT1_HUMAN	UPF1	physical	11544179
REN3A_HUMAN	UPF3A	physical	11163187
REN3B_HUMAN	UPF3B	physical	11163187
RENT1_HUMAN	UPF1	physical	11163187
RENT1_HUMAN	UPF1	physical	16488880
HBB_HUMAN	HBB	physical	21145460
REN3B_HUMAN	UPF3B	physical	16452507
RBM8A_HUMAN	RBM8A	physical	16452507
SMG1_HUMAN	SMG1	physical	16452507
RENT1_HUMAN	UPF1	physical	16452507
RS15_HUMAN	RPS15	physical	15231747
RL5_HUMAN	RPL5	physical	15231747
RS7_HUMAN	RPS7	physical	15231747
PHB2_HUMAN	PHB2	physical	15231747
MLP3B_HUMAN	MAP1LC3B	physical	15231747
NOB1_HUMAN	NOB1	physical	15231747
RL13_HUMAN	RPL13	physical	15231747
REN3B_HUMAN	UPF3B	physical	15231747
PAIRB_HUMAN	SERBP1	physical	15231747
RNPS1_HUMAN	RNPS1	physical	15231747
BLM_HUMAN	BLM	physical	15231747
K1C18_HUMAN	KRT18	physical	15231747
TBB2A_HUMAN	TUBB2A	physical	15231747
ENOA_HUMAN	ENO1	physical	15231747
AT1B3_HUMAN	ATP1B3	physical	15231747
ITB1_HUMAN	ITGB1	physical	15231747
RM40_HUMAN	MRPL40	physical	15231747
TOP3B_HUMAN	TOP3B	physical	15231747
CALR_HUMAN	CALR	physical	15231747
E4F1_HUMAN	E4F1	physical	15231747
HBAZ_HUMAN	HBZ	physical	15231747
TZAP_HUMAN	ZBTB48	physical	15231747
HS3SA_HUMAN	HS3ST3A1	physical	15231747
HSF2B_HUMAN	HSF2BP	physical	15231747
CIZ1_HUMAN	CIZ1	physical	15231747
NOMO1_HUMAN	NOMO1	physical	15231747
RRP7A_HUMAN	RRP7A	physical	15231747
WNK1_HUMAN	WNK1	physical	15231747
ZGPAT_HUMAN	ZGPAT	physical	15231747
SUMO3_HUMAN	SUMO3	physical	15231747
TYSY_HUMAN	TYMS	physical	15231747
MIF_HUMAN	MIF	physical	15231747
RS6_HUMAN	RPS6	physical	15231747
CMTD1_HUMAN	COMTD1	physical	15231747
NDUA7_HUMAN	NDUFA7	physical	15231747
LDHA_HUMAN	LDHA	physical	15231747
RL8_HUMAN	RPL8	physical	15231747
CY24A_HUMAN	CYBA	physical	15231747
KITH_HUMAN	TK1	physical	15231747
SERF2_HUMAN	SERF2	physical	15231747
CENPU_HUMAN	CENPU	physical	15231747
G45IP_HUMAN	GADD45GIP1	physical	15231747
HMGA1_HUMAN	HMGA1	physical	15231747
PLCA_HUMAN	AGPAT1	physical	15231747
NOP53_HUMAN	GLTSCR2	physical	15231747
MTEF3_HUMAN	MTERF3	physical	15231747
ZNF44_HUMAN	ZNF44	physical	15231747
RSRC2_HUMAN	RSRC2	physical	15231747
TNNI2_HUMAN	TNNI2	physical	15231747
ABCF2_HUMAN	ABCF2	physical	15231747
PITX1_HUMAN	PITX1	physical	15231747
REQU_HUMAN	DPF2	physical	15231747
EXOS8_HUMAN	EXOSC8	physical	15231747
EXOS6_HUMAN	EXOSC6	physical	15231747
DCP2_HUMAN	DCP2	physical	15231747
TTP_HUMAN	ZFP36	physical	15231747
DCP1B_HUMAN	DCP1B	physical	15231747
EXOSX_HUMAN	EXOSC10	physical	15231747
EXOS1_HUMAN	EXOSC1	physical	15231747
ZN408_HUMAN	ZNF408	physical	15231747
LSM1_HUMAN	LSM1	physical	15231747
SK2L2_HUMAN	SKIV2L2	physical	15231747
MAP1A_HUMAN	MAP1A	physical	15231747
NAR4_HUMAN	ART4	physical	15231747
REN3B_HUMAN	UPF3B	physical	26344197

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 RENT2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1088, AND MASSSPECTROMETRY.	19413330 [Abstract]