dbPTM

NOC3L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NOC3L_HUMAN
UniProt AC	Q8WTT2
Protein Name	Nucleolar complex protein 3 homolog
Gene Name	NOC3L
Organism	Homo sapiens (Human).
Sequence Length	800
Subcellular Localization	Nucleus, nucleolus. Nucleus speckle.
Protein Description	May be required for adipogenesis..
Protein Sequence	MKARRNKKQIPSFRKLIKTSKVKLENKLKNKQFKQQSTLKKYRKEQRKLRQAVKDAVSKKPIPLENPKEKRPGKRIEREEEEEEEALPLDMMDEDDLQLMKDLGQRVSFLTRDLSSSEPVHAKKRKHERIIDKYEKIPRTLQTAPEKELIHLLPIKDKSGIIPQTREKPVTDSNKDEEDQEEERELEEEIIEDPIQELTIEEHLIERKKKLQEKKMHIAALASAILSDPENNIKKLKELRSMLMEQDPDVAVTVRKLVIVSLMELFKDITPSYKIRPLTEAEKSTKTRKETQKLREFEEGLVSQYKFYLENLEQMVKDWKQRKLKKSNVVSLKAYKGLAEVAVKSLCELLVALPHFNFHNNIIVLIVPLMNDMSKLISEMCCEAVKKLFKQDKLGQASLGVIKVISGFVKGRNYEVRPEMLKTFLCLRIKEVEVKKDTEDINKPKKFMTFKEKRKSLSRMQRKWKKAEEKLERELREAEASESTEKKLKLHTETLNIVFVTYFRILKKAQRSPLLPAVLEGLAKFAHLINVEFFDDLLVVLHTLIESGDLSYQESLHCVQTAFHILSGQGDVLNIDPLKFYTHLYKTLFKLHAGATNEGVEIVLQCLDVMLTKRRKQVSQQRALAFIKRLCTLALHVLPNSSIGILATTRILMHTFPKTDLLLDSESQGSGVFLPELDEPEYCNAQNTALWELHALRRHYHPIVQRFAAHLIAGAPSEGSGALKPELSRRSATELFEAYSMAEMTFNPPVESSNPKIKGKFLQGDSFLNEDLNQLIKRYSSEVATESPLDFTKYLKTSLH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Acetylation	LIKTSKVKLENKLKN HHHHCHHHHHHHHCC	54.54	133323
34	Acetylation	KLKNKQFKQQSTLKK HHCCCHHHHHHHHHH	44.96	133325
37	Phosphorylation	NKQFKQQSTLKKYRK CCHHHHHHHHHHHHH	32.96	30108239
38	Phosphorylation	KQFKQQSTLKKYRKE CHHHHHHHHHHHHHH	37.95	30108239
40	Acetylation	FKQQSTLKKYRKEQR HHHHHHHHHHHHHHH	48.09	133321
59	Ubiquitination	AVKDAVSKKPIPLEN HHHHHHHCCCCCCCC	56.84	21890473
78	Ubiquitination	RPGKRIEREEEEEEE CCCCCCCCCHHHHHH	55.01	24816145
108	Phosphorylation	KDLGQRVSFLTRDLS HHHHHHHHHHHCCCC	19.41	25159151
115	Phosphorylation	SFLTRDLSSSEPVHA HHHHCCCCCCCCCCC	35.79	25159151
116	Phosphorylation	FLTRDLSSSEPVHAK HHHCCCCCCCCCCCC	46.12	25159151
117	Phosphorylation	LTRDLSSSEPVHAKK HHCCCCCCCCCCCCH	42.41	25159151
123	Acetylation	SSEPVHAKKRKHERI CCCCCCCCHHHHHHH	37.93	25953088
123	2-Hydroxyisobutyrylation	SSEPVHAKKRKHERI CCCCCCCCHHHHHHH	37.93	-
124	Acetylation	SEPVHAKKRKHERII CCCCCCCHHHHHHHH	68.42	25953088
133	Acetylation	KHERIIDKYEKIPRT HHHHHHHHHHHCCCC	44.92	26051181
134	Phosphorylation	HERIIDKYEKIPRTL HHHHHHHHHHCCCCC	20.78	-
147	Acetylation	TLQTAPEKELIHLLP CCCCCCHHHHEEEEE	57.68	25953088
159	Phosphorylation	LLPIKDKSGIIPQTR EEECCCCCCCCCCCC	45.41	-
171	Phosphorylation	QTREKPVTDSNKDEE CCCCCCCCCCCCCHH	42.09	19691289
173	Phosphorylation	REKPVTDSNKDEEDQ CCCCCCCCCCCHHHH	36.09	19691289
195	Ubiquitination	EEIIEDPIQELTIEE HHHHHCHHHHCCHHH	8.43	27667366
223	Phosphorylation	MHIAALASAILSDPE HHHHHHHHHHHCCCC	19.38	20068231
227	Phosphorylation	ALASAILSDPENNIK HHHHHHHCCCCCHHH	45.03	20068231
241	Phosphorylation	KKLKELRSMLMEQDP HHHHHHHHHHHHCCC	28.97	20068231
253	Phosphorylation	QDPDVAVTVRKLVIV CCCCHHHHHHHHHHH	12.59	20068231
261	Phosphorylation	VRKLVIVSLMELFKD HHHHHHHHHHHHHCC	15.75	24670416
273	Phosphorylation	FKDITPSYKIRPLTE HCCCCCCCCCCCCCH	16.19	-
274	Ubiquitination	KDITPSYKIRPLTEA CCCCCCCCCCCCCHH	36.25	22817900
284	Phosphorylation	PLTEAEKSTKTRKET CCCHHHHHCCCHHHH	27.00	26074081
285	Phosphorylation	LTEAEKSTKTRKETQ CCHHHHHCCCHHHHH	47.72	26074081
287	Phosphorylation	EAEKSTKTRKETQKL HHHHHCCCHHHHHHH	47.24	26074081
293	Ubiquitination	KTRKETQKLREFEEG CCHHHHHHHHHHHHH	57.86	24816145
333	Acetylation	KSNVVSLKAYKGLAE CCCCCCHHHHCCHHH	42.01	25953088
333	Sumoylation	KSNVVSLKAYKGLAE CCCCCCHHHHCCHHH	42.01	28112733
386	Acetylation	EMCCEAVKKLFKQDK HHHHHHHHHHHHCCC	51.29	25953088
390	Acetylation	EAVKKLFKQDKLGQA HHHHHHHHCCCCCCH	68.94	26051181
398	Phosphorylation	QDKLGQASLGVIKVI CCCCCCHHHHHHHHH	20.12	20068231
410	Ubiquitination	KVISGFVKGRNYEVR HHHHCCCCCCCCCCC	50.30	27667366
410	Acetylation	KVISGFVKGRNYEVR HHHHCCCCCCCCCCC	50.30	26051181
422	Acetylation	EVRPEMLKTFLCLRI CCCHHHHHHHHHHHC	35.60	26051181
430	Acetylation	TFLCLRIKEVEVKKD HHHHHHCCEEEECCC	49.64	26051181
443	Acetylation	KDTEDINKPKKFMTF CCCCCCCCCCCCCCH	59.56	26051181
445	2-Hydroxyisobutyrylation	TEDINKPKKFMTFKE CCCCCCCCCCCCHHH	61.32	-
449	Phosphorylation	NKPKKFMTFKEKRKS CCCCCCCCHHHHHHH	34.39	28555341
456	Phosphorylation	TFKEKRKSLSRMQRK CHHHHHHHHHHHHHH	35.29	24719451
481	Phosphorylation	ELREAEASESTEKKL HHHHHHHCHHHHHHH	24.48	20068231
483	Phosphorylation	REAEASESTEKKLKL HHHHHCHHHHHHHHH	39.09	20068231
484	Phosphorylation	EAEASESTEKKLKLH HHHHCHHHHHHHHHH	48.01	20068231
492	Phosphorylation	EKKLKLHTETLNIVF HHHHHHHHHHHHHHH	40.89	-
494	Phosphorylation	KLKLHTETLNIVFVT HHHHHHHHHHHHHHH	26.68	-
567	Phosphorylation	QTAFHILSGQGDVLN HHHHHHHCCCCCCCC	28.59	24719451
628	Sumoylation	QRALAFIKRLCTLAL HHHHHHHHHHHHHHH	32.63	-
628	2-Hydroxyisobutyrylation	QRALAFIKRLCTLAL HHHHHHHHHHHHHHH	32.63	-
628	Sumoylation	QRALAFIKRLCTLAL HHHHHHHHHHHHHHH	32.63	-
717	Phosphorylation	HLIAGAPSEGSGALK HHHHCCCCCCCCCCC	54.80	20068231
720	Phosphorylation	AGAPSEGSGALKPEL HCCCCCCCCCCCHHH	19.48	20068231
724	Acetylation	SEGSGALKPELSRRS CCCCCCCCHHHHHHC	35.59	26051181
728	Phosphorylation	GALKPELSRRSATEL CCCCHHHHHHCHHHH	24.80	20068231
760	Acetylation	SNPKIKGKFLQGDSF CCCCCCCCCCCCCCC	37.59	25953088
760	Ubiquitination	SNPKIKGKFLQGDSF CCCCCCCCCCCCCCC	37.59	29967540
777	Ubiquitination	EDLNQLIKRYSSEVA HHHHHHHHHHCHHCC	54.60	29967540
779	Phosphorylation	LNQLIKRYSSEVATE HHHHHHHHCHHCCCC	16.14	23663014
780	Phosphorylation	NQLIKRYSSEVATES HHHHHHHCHHCCCCC	24.85	23663014
781	Phosphorylation	QLIKRYSSEVATESP HHHHHHCHHCCCCCC	27.44	23663014
785	Phosphorylation	RYSSEVATESPLDFT HHCHHCCCCCCCHHH	42.02	30266825
787	Phosphorylation	SSEVATESPLDFTKY CHHCCCCCCCHHHHH	26.80	23927012
792	Phosphorylation	TESPLDFTKYLKTSL CCCCCHHHHHHHHCC	20.60	23663014
793	Ubiquitination	ESPLDFTKYLKTSLH CCCCHHHHHHHHCCC	48.88	29967540
793	Acetylation	ESPLDFTKYLKTSLH CCCCHHHHHHHHCCC	48.88	26051181
794	Phosphorylation	SPLDFTKYLKTSLH- CCCHHHHHHHHCCC-	15.46	23663014
796	Ubiquitination	LDFTKYLKTSLH--- CHHHHHHHHCCC---	32.74	-

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 NOC3L_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NOC3L_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 NOC3L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DDX24_HUMAN	DDX24	physical	26344197
PESC_HUMAN	PES1	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RLA0_HUMAN	RPLP0	physical	26344197
RRP12_HUMAN	RRP12	physical	26344197
SRP72_HUMAN	SRP72	physical	26344197
TBL3_HUMAN	TBL3	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 NOC3L_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-787, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 SER-787, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-117, ANDMASS SPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND MASSSPECTROMETRY.	16565220 [Abstract]