dbPTM

SPT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPT2_HUMAN
UniProt AC	Q68D10
Protein Name	Protein SPT2 homolog
Gene Name	SPTY2D1
Organism	Homo sapiens (Human).
Sequence Length	685
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin. [PubMed: 26109053 Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription]
Protein Sequence	MDFREILMIASKGQGVNNVPKRYSLAVGPPKKDPKVKGVQSAAVQAFLKRKEEELRRKALEEKRRKEELVKKRIELKHDKKARAMAKRTKDNFHGYNGIPIEEKSKKRQATESHTSQGTDREYEMEEENEFLEYNHAESEQEYEEEQEPPKVESKPKVPLKSAPPPMNFTDLLRLAEKKQFEPVEIKVVKKSEERPMTAEELREREFLERKHRRKKLETDGKLPPTVSKKAPSQKESVGTKLSKGSGDRHPSSKGMPLPHAEKKSRPSMANEKHLALSSSKSMPGERIKAGSGNSSQPSLREGHDKPVFNGAGKPHSSTSSPSVPKTSASRTQKSAVEHKAKKSLSHPSHSRPGPMVTPHNKAKSPGVRQPGSSSSSAPGQPSTGVARPTVSSGPVPRRQNGSSSSGPERSISGSKKPTNDSNPSRRTVSGTCGPGQPASSSGGPGRPISGSVSSARPLGSSRGPGRPVSSPHELRRPVSGLGPPGRSVSGPGRSISGSIPAGRTVSNSVPGRPVSSLGPGQTVSSSGPTIKPKCTVVSETISSKNIISRSSNGQMNGMKPPLSGYRAAQGPQRLPFPTGYKRQREYEEEDDDDDEYDSEMEDFIEDEGEPQEEISKHIREIFGYDRKKYKDESDYALRYMESSWKEQQKEEAKSLRLGMQEDLEEMRREEEEMQRRRAKKLKRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Sulfoxidation	MDFREILMIASKGQG CCHHHHHHHHCCCCC	2.71	21406390
11	Phosphorylation	REILMIASKGQGVNN HHHHHHHCCCCCCCC	26.79	-
12	Acetylation	EILMIASKGQGVNNV HHHHHHCCCCCCCCC	46.35	25953088
23	Phosphorylation	VNNVPKRYSLAVGPP CCCCCCCEEECCCCC	17.73	22985185
24	Phosphorylation	NNVPKRYSLAVGPPK CCCCCCEEECCCCCC	17.56	20860994
37	Sumoylation	PKKDPKVKGVQSAAV CCCCCCCCHHHHHHH	60.53	28112733
41	Phosphorylation	PKVKGVQSAAVQAFL CCCCHHHHHHHHHHH	18.78	-
58	Methylation	KEEELRRKALEEKRR HHHHHHHHHHHHHHH	51.38	116252913
72	Ubiquitination	RKEELVKKRIELKHD HHHHHHHHHHHHHHH	51.64	24816145
81	Ubiquitination	IELKHDKKARAMAKR HHHHHHHHHHHHHHH	49.51	24816145
123	Phosphorylation	SQGTDREYEMEEENE CCCCCCCCCHHHHHH	22.82	28985074
134	Phosphorylation	EENEFLEYNHAESEQ HHHHHHCCCCHHHHH	17.88	26074081
139	Phosphorylation	LEYNHAESEQEYEEE HCCCCHHHHHHHHHH	45.42	26074081
143	Phosphorylation	HAESEQEYEEEQEPP CHHHHHHHHHHHCCC	28.47	26074081
154	Phosphorylation	QEPPKVESKPKVPLK HCCCCCCCCCCCCCC	58.19	26074081
187	Sumoylation	QFEPVEIKVVKKSEE CCCCCEEEEEECCCC	27.72	28112733
192	Phosphorylation	EIKVVKKSEERPMTA EEEEEECCCCCCCCH	38.68	26074081
197	Sulfoxidation	KKSEERPMTAEELRE ECCCCCCCCHHHHHH	7.50	21406390
198	Phosphorylation	KSEERPMTAEELRER CCCCCCCCHHHHHHH	33.33	26074081
226	Phosphorylation	TDGKLPPTVSKKAPS CCCCCCCCCCCCCCC	35.16	22964224
241	Acetylation	QKESVGTKLSKGSGD CCCCCCCCCCCCCCC	44.85	25953088
243	Phosphorylation	ESVGTKLSKGSGDRH CCCCCCCCCCCCCCC	36.20	25627689
273	Acetylation	RPSMANEKHLALSSS CCCHHCHHHHHHHCC	43.66	25953088
273	Ubiquitination	RPSMANEKHLALSSS CCCHHCHHHHHHHCC	43.66	29967540
278	Phosphorylation	NEKHLALSSSKSMPG CHHHHHHHCCCCCCC	27.27	20068231
279	Phosphorylation	EKHLALSSSKSMPGE HHHHHHHCCCCCCCC	42.51	26699800
280	Phosphorylation	KHLALSSSKSMPGER HHHHHHCCCCCCCCC	25.93	26699800
281	Acetylation	HLALSSSKSMPGERI HHHHHCCCCCCCCCC	53.36	25953088
281	Ubiquitination	HLALSSSKSMPGERI HHHHHCCCCCCCCCC	53.36	-
289	Ubiquitination	SMPGERIKAGSGNSS CCCCCCCCCCCCCCC	53.57	29967540
299	Phosphorylation	SGNSSQPSLREGHDK CCCCCCCCHHCCCCC	32.21	21955146
306	Acetylation	SLREGHDKPVFNGAG CHHCCCCCCCCCCCC	37.09	26051181
317	Phosphorylation	NGAGKPHSSTSSPSV CCCCCCCCCCCCCCC	43.78	25159151
318	Phosphorylation	GAGKPHSSTSSPSVP CCCCCCCCCCCCCCC	29.31	25159151
319	Phosphorylation	AGKPHSSTSSPSVPK CCCCCCCCCCCCCCC	35.92	25159151
320	Phosphorylation	GKPHSSTSSPSVPKT CCCCCCCCCCCCCCC	42.05	25849741
321	Phosphorylation	KPHSSTSSPSVPKTS CCCCCCCCCCCCCCC	22.68	25849741
323	Phosphorylation	HSSTSSPSVPKTSAS CCCCCCCCCCCCCCC	53.66	30576142
333	Ubiquitination	KTSASRTQKSAVEHK CCCCCCHHHHHHHHH	36.27	24816145
344	Phosphorylation	VEHKAKKSLSHPSHS HHHHHHHCCCCCCCC	34.10	22210691
346	Phosphorylation	HKAKKSLSHPSHSRP HHHHHCCCCCCCCCC	40.21	29449344
349	Phosphorylation	KKSLSHPSHSRPGPM HHCCCCCCCCCCCCC	28.77	29449344
351	Phosphorylation	SLSHPSHSRPGPMVT CCCCCCCCCCCCCCC	44.50	28555341
358	Phosphorylation	SRPGPMVTPHNKAKS CCCCCCCCCCCCCCC	16.75	25159151
365	Phosphorylation	TPHNKAKSPGVRQPG CCCCCCCCCCCCCCC	31.57	29214152
373	Phosphorylation	PGVRQPGSSSSSAPG CCCCCCCCCCCCCCC	33.46	28555341
374	Phosphorylation	GVRQPGSSSSSAPGQ CCCCCCCCCCCCCCC	39.91	28857561
375	Phosphorylation	VRQPGSSSSSAPGQP CCCCCCCCCCCCCCC	29.97	28857561
390	Phosphorylation	STGVARPTVSSGPVP CCCCCCCCCCCCCCC	27.71	27732954
392	Phosphorylation	GVARPTVSSGPVPRR CCCCCCCCCCCCCCC	31.86	20860994
393	Phosphorylation	VARPTVSSGPVPRRQ CCCCCCCCCCCCCCC	42.66	20860994
416	Acetylation	ERSISGSKKPTNDSN CCCCCCCCCCCCCCC	67.32	25953088
417	Ubiquitination	RSISGSKKPTNDSNP CCCCCCCCCCCCCCC	59.79	24816145
452	Phosphorylation	PGRPISGSVSSARPL CCCCCCCCCCCCCCC	16.43	24719451
462	Phosphorylation	SARPLGSSRGPGRPV CCCCCCCCCCCCCCC	39.18	24719451
470	Phosphorylation	RGPGRPVSSPHELRR CCCCCCCCCHHHHCC	40.61	30266825
471	Phosphorylation	GPGRPVSSPHELRRP CCCCCCCCHHHHCCC	30.43	30266825
480	Phosphorylation	HELRRPVSGLGPPGR HHHCCCCCCCCCCCC	30.86	26270265
488	Phosphorylation	GLGPPGRSVSGPGRS CCCCCCCCCCCCCCC	26.92	23917254
490	Phosphorylation	GPPGRSVSGPGRSIS CCCCCCCCCCCCCCC	40.28	28555341
495	Phosphorylation	SVSGPGRSISGSIPA CCCCCCCCCCCCCCC	27.33	28555341
497	Phosphorylation	SGPGRSISGSIPAGR CCCCCCCCCCCCCCC	27.95	28555341
499	Phosphorylation	PGRSISGSIPAGRTV CCCCCCCCCCCCCCC	20.71	29978859
505	Phosphorylation	GSIPAGRTVSNSVPG CCCCCCCCCCCCCCC	27.63	27067055
507	Phosphorylation	IPAGRTVSNSVPGRP CCCCCCCCCCCCCCC	23.83	25159151
516	Phosphorylation	SVPGRPVSSLGPGQT CCCCCCCHHCCCCCE	23.64	20860994
532	Acetylation	SSSGPTIKPKCTVVS CCCCCCCCCCEEEEE	40.68	25953088
543	Phosphorylation	TVVSETISSKNIISR EEEECEECCCCCCCC	42.55	-
544	Phosphorylation	VVSETISSKNIISRS EEECEECCCCCCCCC	26.35	-
545	Acetylation	VSETISSKNIISRSS EECEECCCCCCCCCC	45.43	25953088
547	Ubiquitination	ETISSKNIISRSSNG CEECCCCCCCCCCCC	3.30	24816145
549	Phosphorylation	ISSKNIISRSSNGQM ECCCCCCCCCCCCCC	23.47	-
551	Phosphorylation	SKNIISRSSNGQMNG CCCCCCCCCCCCCCC	22.74	29214152
552	Phosphorylation	KNIISRSSNGQMNGM CCCCCCCCCCCCCCC	43.82	28555341
579	Phosphorylation	PQRLPFPTGYKRQRE CCCCCCCCCCHHHHH	54.22	27174698
581	Phosphorylation	RLPFPTGYKRQREYE CCCCCCCCHHHHHCC	12.89	27174698
582	Acetylation	LPFPTGYKRQREYEE CCCCCCCHHHHHCCC	43.32	19608861
587	Phosphorylation	GYKRQREYEEEDDDD CCHHHHHCCCCCCCC	30.72	20873877
597	Phosphorylation	EDDDDDEYDSEMEDF CCCCCCCCHHHHHHH	31.59	30576142
599	Phosphorylation	DDDDEYDSEMEDFIE CCCCCCHHHHHHHHH	37.63	20067319
616	Phosphorylation	GEPQEEISKHIREIF CCCHHHHHHHHHHHH	22.82	20873877
630	Phosphorylation	FGYDRKKYKDESDYA HCCCHHHCCCHHHHH	27.06	25262027
631	Sumoylation	GYDRKKYKDESDYAL CCCHHHCCCHHHHHH	64.99	-
631	Ubiquitination	GYDRKKYKDESDYAL CCCHHHCCCHHHHHH	64.99	24816145
631	Sumoylation	GYDRKKYKDESDYAL CCCHHHCCCHHHHHH	64.99	-
634	Phosphorylation	RKKYKDESDYALRYM HHHCCCHHHHHHHHH	46.16	25262027
636	Phosphorylation	KYKDESDYALRYMES HCCCHHHHHHHHHHH	19.47	25262027
640	Phosphorylation	ESDYALRYMESSWKE HHHHHHHHHHHHHHH	13.19	19658100

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 SPT2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPT2_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 SPT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SPT2_HUMAN !!

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 SPT2_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-582, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-599, AND MASSSPECTROMETRY.	18669648 [Abstract]