dbPTM

SAFB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SAFB2_HUMAN
UniProt AC	Q14151
Protein Name	Scaffold attachment factor B2
Gene Name	SAFB2
Organism	Homo sapiens (Human).
Sequence Length	953
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation..
Protein Sequence	MAETLPGSGDSGPGTASLGPGVAETGTRRLSELRVIDLRAELKKRNLDTGGNKSVLMERLKKAVKEEGQDPDEIGIELEATSKKSAKRCVKGLKMEEEGTEDNGLEDDSRDGQEDMEASLENLQNMGMMDMSVLDETEVANSSAPDFGEDGTDGLLDSFCDSKEYVAAQLRQLPAQPPEHAVDGEGFKNTLETSSLNFKVTPDIEESLLEPENEKILDILGETCKSEPVKEESSELEQPFAQDTSSVGPDRKLAEEEDLFDSAHPEEGDLDLASESTAHAQSSKADSLLAVVKREPAEQPGDGERTDCEPVGLEPAVEQSSAASELAEASSEELAEAPTEAPSPEARDSKEDGRKFDFDACNEVPPAPKESSTSEGADQKMSSFKEEKDIKPIIKDEKGRVGSGSGRNLWVSGLSSTTRATDLKNLFSKYGKVVGAKVVTNARSPGARCYGFVTMSTSDEATKCISHLHRTELHGRMISVEKAKNEPAGKKLSDRKECEVKKEKLSSVDRHHSVEIKIEKTVIKKEEKIEKKEEKKPEDIKKEEKDQDELKPGPTNRSRVTKSGSRGMERTVVMDKSKGEPVISVKTTSRSKERSSKSQDRKSESKEKRDILSFDKIKEQRERERQRQREREIRETERRREREQREREQRLEAFHERKEKARLQRERLQLECQRQRLERERMERERLERERMRVERERRKEQERIHREREELRRQQEQLRYEQERRPGRRPYDLDRRDDAYWPEGKRVAMEDRYRADFPRPDHRFHDFDHRDRGQYQDHAIDRREGSRPMMGDHRDGQHYGDDRHGHGGPPERHGRDSRDGWGGYGSDKRLSEGRGLPPPPRGGRDWGEHNQRLEEHQARAWQGAMDAGAASREHARWQGGERGLSGPSGPGHMASRGGVAGRGGFAQGGHSQGHVVPGGGLEGGGVASQDRGSRVPHPHPHPPPYPHFTRRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAETLPGSG ------CCCCCCCCC	20.62	22223895
4	Phosphorylation	----MAETLPGSGDS ----CCCCCCCCCCC	28.81	20068231
8	Phosphorylation	MAETLPGSGDSGPGT CCCCCCCCCCCCCCC	37.17	20068231
11	Phosphorylation	TLPGSGDSGPGTASL CCCCCCCCCCCCCCC	50.87	20068231
15	Phosphorylation	SGDSGPGTASLGPGV CCCCCCCCCCCCCCC	19.06	30387612
17	Phosphorylation	DSGPGTASLGPGVAE CCCCCCCCCCCCCCC	33.43	30387612
25	Phosphorylation	LGPGVAETGTRRLSE CCCCCCCCCCCCHHH	33.83	20068231
27	Phosphorylation	PGVAETGTRRLSELR CCCCCCCCCCHHHHE	21.75	20068231
31	Phosphorylation	ETGTRRLSELRVIDL CCCCCCHHHHEEEEH	32.54	29496963
49	Phosphorylation	LKKRNLDTGGNKSVL HHHCCCCCCCCHHHH	50.59	29214152
53	Acetylation	NLDTGGNKSVLMERL CCCCCCCHHHHHHHH	45.26	26051181
53	Ubiquitination	NLDTGGNKSVLMERL CCCCCCCHHHHHHHH	45.26	24816145
54	Phosphorylation	LDTGGNKSVLMERLK CCCCCCHHHHHHHHH	25.20	26055452
59	Methylation	NKSVLMERLKKAVKE CHHHHHHHHHHHHHH	37.53	-
65	Sumoylation	ERLKKAVKEEGQDPD HHHHHHHHHHCCCHH	55.71	-
65	Acetylation	ERLKKAVKEEGQDPD HHHHHHHHHHCCCHH	55.71	26051181
65	Sumoylation	ERLKKAVKEEGQDPD HHHHHHHHHHCCCHH	55.71	25114211
81	Phosphorylation	IGIELEATSKKSAKR HCEEEEECCHHHHHH	31.53	28555341
83	Acetylation	IELEATSKKSAKRCV EEEEECCHHHHHHHH	46.52	26051181
83	Ubiquitination	IELEATSKKSAKRCV EEEEECCHHHHHHHH	46.52	32015554
85	Phosphorylation	LEATSKKSAKRCVKG EEECCHHHHHHHHHC	42.64	-
94	Sumoylation	KRCVKGLKMEEEGTE HHHHHCCCCCCCCCC	53.59	-
94	Acetylation	KRCVKGLKMEEEGTE HHHHHCCCCCCCCCC	53.59	26051181
94	Sumoylation	KRCVKGLKMEEEGTE HHHHHCCCCCCCCCC	53.59	25218447
100	Phosphorylation	LKMEEEGTEDNGLED CCCCCCCCCCCCCCC	43.37	23927012
109	Phosphorylation	DNGLEDDSRDGQEDM CCCCCCCCCCCHHHH	44.59	23401153
132	Ubiquitination	NMGMMDMSVLDETEV HCCCCCHHHCCHHHH	18.44	21963094
158	Phosphorylation	GTDGLLDSFCDSKEY CCCCHHHHHCCCHHH	27.95	24275569
162	Ubiquitination	LLDSFCDSKEYVAAQ HHHHHCCCHHHHHHH	28.68	21890473
164	Ubiquitination	DSFCDSKEYVAAQLR HHHCCCHHHHHHHHH	49.55	22817900
165	Phosphorylation	SFCDSKEYVAAQLRQ HHCCCHHHHHHHHHC	10.10	28796482
188	Acetylation	AVDGEGFKNTLETSS CCCCCCCCCCHHCCC	60.94	26051181
188	Sumoylation	AVDGEGFKNTLETSS CCCCCCCCCCHHCCC	60.94	28112733
188	Ubiquitination	AVDGEGFKNTLETSS CCCCCCCCCCHHCCC	60.94	32015554
190	Phosphorylation	DGEGFKNTLETSSLN CCCCCCCCHHCCCCC	26.93	23403867
193	Phosphorylation	GFKNTLETSSLNFKV CCCCCHHCCCCCEEE	27.08	29255136
194	Phosphorylation	FKNTLETSSLNFKVT CCCCHHCCCCCEEEC	24.37	29255136
195	Phosphorylation	KNTLETSSLNFKVTP CCCHHCCCCCEEECC	34.45	23401153
199	Sumoylation	ETSSLNFKVTPDIEE HCCCCCEEECCCHHH	44.09	28112733
199	Ubiquitination	ETSSLNFKVTPDIEE HCCCCCEEECCCHHH	44.09	29967540
201	Phosphorylation	SSLNFKVTPDIEESL CCCCEEECCCHHHHH	18.81	29255136
207	Phosphorylation	VTPDIEESLLEPENE ECCCHHHHHCCCCCH	26.01	29255136
215	Ubiquitination	LLEPENEKILDILGE HCCCCCHHHHHHHHH	61.22	29967540
223	Phosphorylation	ILDILGETCKSEPVK HHHHHHHHHCCCCCC	24.36	28102081
224	Glutathionylation	LDILGETCKSEPVKE HHHHHHHHCCCCCCC	3.87	22555962
224	S-nitrosylation	LDILGETCKSEPVKE HHHHHHHHCCCCCCC	3.87	22178444
225	Sumoylation	DILGETCKSEPVKEE HHHHHHHCCCCCCCC	66.33	-
225	Acetylation	DILGETCKSEPVKEE HHHHHHHCCCCCCCC	66.33	26051181
225	Methylation	DILGETCKSEPVKEE HHHHHHHCCCCCCCC	66.33	23583077
225	Sumoylation	DILGETCKSEPVKEE HHHHHHHCCCCCCCC	66.33	-
225	Ubiquitination	DILGETCKSEPVKEE HHHHHHHCCCCCCCC	66.33	32015554
226	Phosphorylation	ILGETCKSEPVKEES HHHHHHCCCCCCCCC	49.64	29255136
230	Sumoylation	TCKSEPVKEESSELE HHCCCCCCCCCCCCC	67.49	-
230	Acetylation	TCKSEPVKEESSELE HHCCCCCCCCCCCCC	67.49	26051181
230	Sumoylation	TCKSEPVKEESSELE HHCCCCCCCCCCCCC	67.49	21527249
230	Ubiquitination	TCKSEPVKEESSELE HHCCCCCCCCCCCCC	67.49	21906983
233	Phosphorylation	SEPVKEESSELEQPF CCCCCCCCCCCCCCC	30.15	29255136
234	Phosphorylation	EPVKEESSELEQPFA CCCCCCCCCCCCCCC	49.86	29255136
244	Phosphorylation	EQPFAQDTSSVGPDR CCCCCCCCCCCCCCH	15.72	29255136
245	Phosphorylation	QPFAQDTSSVGPDRK CCCCCCCCCCCCCHH	31.17	29255136
246	Phosphorylation	PFAQDTSSVGPDRKL CCCCCCCCCCCCHHH	32.93	29255136
252	Sumoylation	SSVGPDRKLAEEEDL CCCCCCHHHHHHHHH	60.47	-
252	Acetylation	SSVGPDRKLAEEEDL CCCCCCHHHHHHHHH	60.47	26051181
252	Sumoylation	SSVGPDRKLAEEEDL CCCCCCHHHHHHHHH	60.47	-
262	Phosphorylation	EEEDLFDSAHPEEGD HHHHHHHCCCCCCCC	22.57	30266825
274	Phosphorylation	EGDLDLASESTAHAQ CCCCCCCCCCHHHHH	39.10	30266825
276	Phosphorylation	DLDLASESTAHAQSS CCCCCCCCHHHHHHC	28.53	30266825
277	Phosphorylation	LDLASESTAHAQSSK CCCCCCCHHHHHHCC	20.57	30266825
282	Phosphorylation	ESTAHAQSSKADSLL CCHHHHHHCCHHHEE	34.29	23401153
283	Phosphorylation	STAHAQSSKADSLLA CHHHHHHCCHHHEEE	21.56	30108239
284	Acetylation	TAHAQSSKADSLLAV HHHHHHCCHHHEEEE	62.55	26051181
284	Ubiquitination	TAHAQSSKADSLLAV HHHHHHCCHHHEEEE	62.55	21963094
287	Phosphorylation	AQSSKADSLLAVVKR HHHCCHHHEEEEEEC	30.09	19664994
293	Sumoylation	DSLLAVVKREPAEQP HHEEEEEECCCCCCC	44.43	-
293	Acetylation	DSLLAVVKREPAEQP HHEEEEEECCCCCCC	44.43	23954790
293	Sumoylation	DSLLAVVKREPAEQP HHEEEEEECCCCCCC	44.43	21527249
293	Ubiquitination	DSLLAVVKREPAEQP HHEEEEEECCCCCCC	44.43	33845483
306	Phosphorylation	QPGDGERTDCEPVGL CCCCCCCCCCEECCC	40.47	23927012
320	Phosphorylation	LEPAVEQSSAASELA CHHHHHCCHHHHHHH	14.40	25159151
321	Phosphorylation	EPAVEQSSAASELAE HHHHHCCHHHHHHHH	27.78	23927012
324	Phosphorylation	VEQSSAASELAEASS HHCCHHHHHHHHHCH	32.62	23927012
330	Phosphorylation	ASELAEASSEELAEA HHHHHHHCHHHHHHC	29.77	26503892
331	Phosphorylation	SELAEASSEELAEAP HHHHHHCHHHHHHCC	41.98	30278072
339	Phosphorylation	EELAEAPTEAPSPEA HHHHHCCCCCCCCCC	52.40	30278072
343	Phosphorylation	EAPTEAPSPEARDSK HCCCCCCCCCCCCCC	42.28	29255136
349	Phosphorylation	PSPEARDSKEDGRKF CCCCCCCCCCCCCCC	32.18	30576142
350	Ubiquitination	SPEARDSKEDGRKFD CCCCCCCCCCCCCCC	65.20	23000965
355	Acetylation	DSKEDGRKFDFDACN CCCCCCCCCCCCCCC	55.61	25825284
355	Ubiquitination	DSKEDGRKFDFDACN CCCCCCCCCCCCCCC	55.61	23000965
361	Glutathionylation	RKFDFDACNEVPPAP CCCCCCCCCCCCCCC	4.86	22555962
369	Ubiquitination	NEVPPAPKESSTSEG CCCCCCCCCCCCCCC	72.79	-
371	Phosphorylation	VPPAPKESSTSEGAD CCCCCCCCCCCCCCH	45.07	20873877
372	Phosphorylation	PPAPKESSTSEGADQ CCCCCCCCCCCCCHH	36.72	21082442
373	Phosphorylation	PAPKESSTSEGADQK CCCCCCCCCCCCHHH	39.82	20873877
374	Phosphorylation	APKESSTSEGADQKM CCCCCCCCCCCHHHH	35.66	20873877
380	Sumoylation	TSEGADQKMSSFKEE CCCCCHHHHHCCCCH	41.10	-
380	Sumoylation	TSEGADQKMSSFKEE CCCCCHHHHHCCCCH	41.10	28112733
380	Ubiquitination	TSEGADQKMSSFKEE CCCCCHHHHHCCCCH	41.10	32015554
382	Phosphorylation	EGADQKMSSFKEEKD CCCHHHHHCCCCHHC	39.39	29214152
385	Sumoylation	DQKMSSFKEEKDIKP HHHHHCCCCHHCCCC	67.90	-
385	Sumoylation	DQKMSSFKEEKDIKP HHHHHCCCCHHCCCC	67.90	28112733
388	Sumoylation	MSSFKEEKDIKPIIK HHCCCCHHCCCCCEE	66.88	-
388	Acetylation	MSSFKEEKDIKPIIK HHCCCCHHCCCCCEE	66.88	90449
388	Sumoylation	MSSFKEEKDIKPIIK HHCCCCHHCCCCCEE	66.88	28112733
391	Sumoylation	FKEEKDIKPIIKDEK CCCHHCCCCCEECCC	40.05	-
391	Acetylation	FKEEKDIKPIIKDEK CCCHHCCCCCEECCC	40.05	25953088
391	Sumoylation	FKEEKDIKPIIKDEK CCCHHCCCCCEECCC	40.05	28112733
395	Sumoylation	KDIKPIIKDEKGRVG HCCCCCEECCCCCCC	61.63	-
395	Sumoylation	KDIKPIIKDEKGRVG HCCCCCEECCCCCCC	61.63	28112733
398	Acetylation	KPIIKDEKGRVGSGS CCCEECCCCCCCCCC	63.25	26051181
415	Phosphorylation	NLWVSGLSSTTRATD CCEEECCCCCCCHHH	29.21	-
416	Phosphorylation	LWVSGLSSTTRATDL CEEECCCCCCCHHHH	38.55	28555341
417	Phosphorylation	WVSGLSSTTRATDLK EEECCCCCCCHHHHH	19.54	20068231
424	Acetylation	TTRATDLKNLFSKYG CCCHHHHHHHHHHHC	55.18	23749302
424	Malonylation	TTRATDLKNLFSKYG CCCHHHHHHHHHHHC	55.18	26320211
424	Ubiquitination	TTRATDLKNLFSKYG CCCHHHHHHHHHHHC	55.18	21890473
428	Phosphorylation	TDLKNLFSKYGKVVG HHHHHHHHHHCCCCC	28.30	24719451
429	Acetylation	DLKNLFSKYGKVVGA HHHHHHHHHCCCCCC	51.17	19608861
429	Ubiquitination	DLKNLFSKYGKVVGA HHHHHHHHHCCCCCC	51.17	23000965
432	2-Hydroxyisobutyrylation	NLFSKYGKVVGAKVV HHHHHHCCCCCCEEE	30.56	-
432	Acetylation	NLFSKYGKVVGAKVV HHHHHHCCCCCCEEE	30.56	25953088
432	Ubiquitination	NLFSKYGKVVGAKVV HHHHHHCCCCCCEEE	30.56	23000965
437	2-Hydroxyisobutyrylation	YGKVVGAKVVTNARS HCCCCCCEEEECCCC	31.17	-
437	Acetylation	YGKVVGAKVVTNARS HCCCCCCEEEECCCC	31.17	23749302
437	Malonylation	YGKVVGAKVVTNARS HCCCCCCEEEECCCC	31.17	26320211
437	Ubiquitination	YGKVVGAKVVTNARS HCCCCCCEEEECCCC	31.17	23000965
440	Phosphorylation	VVGAKVVTNARSPGA CCCCEEEECCCCCCC	26.58	25159151
444	Phosphorylation	KVVTNARSPGARCYG EEEECCCCCCCEEEE	25.85	28355574
463	Acetylation	STSDEATKCISHLHR CCCHHHHHHHHHHHH	36.30	7479789
471	Phosphorylation	CISHLHRTELHGRMI HHHHHHHHHHCCCEE	31.95	-
479	Phosphorylation	ELHGRMISVEKAKNE HHCCCEEEHHHHCCC	18.19	-
482	Acetylation	GRMISVEKAKNEPAG CCEEEHHHHCCCCCC	63.61	25953088
482	Malonylation	GRMISVEKAKNEPAG CCEEEHHHHCCCCCC	63.61	26320211
501	Sumoylation	DRKECEVKKEKLSSV CHHHHHHHHHHHCCC	32.68	-
501	Sumoylation	DRKECEVKKEKLSSV CHHHHHHHHHHHCCC	32.68	-
504	Acetylation	ECEVKKEKLSSVDRH HHHHHHHHHCCCCCC	63.65	25953088
506	Phosphorylation	EVKKEKLSSVDRHHS HHHHHHHCCCCCCCC	39.11	23403867
507	Phosphorylation	VKKEKLSSVDRHHSV HHHHHHCCCCCCCCE	38.17	25159151
513	Phosphorylation	SSVDRHHSVEIKIEK CCCCCCCCEEEEEEE	18.47	23401153
517	Sumoylation	RHHSVEIKIEKTVIK CCCCEEEEEEEEEEC	31.16	-
517	Acetylation	RHHSVEIKIEKTVIK CCCCEEEEEEEEEEC	31.16	26051181
517	Sumoylation	RHHSVEIKIEKTVIK CCCCEEEEEEEEEEC	31.16	28112733
524	Sumoylation	KIEKTVIKKEEKIEK EEEEEEECHHHHHCH	50.20	-
524	Sumoylation	KIEKTVIKKEEKIEK EEEEEEECHHHHHCH	50.20	28112733
525	Sumoylation	IEKTVIKKEEKIEKK EEEEEECHHHHHCHH	61.04	28112733
528	Acetylation	TVIKKEEKIEKKEEK EEECHHHHHCHHHHC	58.20	18585839
531	Ubiquitination	KKEEKIEKKEEKKPE CHHHHHCHHHHCCHH	69.80	-
532	Acetylation	KEEKIEKKEEKKPED HHHHHCHHHHCCHHH	59.31	18585847
532	Ubiquitination	KEEKIEKKEEKKPED HHHHHCHHHHCCHHH	59.31	-
541	Sumoylation	EKKPEDIKKEEKDQD HCCHHHHHHHHHCCC	67.46	-
541	2-Hydroxyisobutyrylation	EKKPEDIKKEEKDQD HCCHHHHHHHHHCCC	67.46	-
541	Sumoylation	EKKPEDIKKEEKDQD HCCHHHHHHHHHCCC	67.46	28112733
542	Sumoylation	KKPEDIKKEEKDQDE CCHHHHHHHHHCCCC	72.01	28112733
551	Sumoylation	EKDQDELKPGPTNRS HHCCCCCCCCCCCHH	45.97	-
551	Acetylation	EKDQDELKPGPTNRS HHCCCCCCCCCCCHH	45.97	26051181
551	Sumoylation	EKDQDELKPGPTNRS HHCCCCCCCCCCCHH	45.97	28112733
551	Ubiquitination	EKDQDELKPGPTNRS HHCCCCCCCCCCCHH	45.97	32015554
555	Phosphorylation	DELKPGPTNRSRVTK CCCCCCCCCHHHCCC	49.53	26074081
558	Phosphorylation	KPGPTNRSRVTKSGS CCCCCCHHHCCCCCC	32.92	26074081
561	Phosphorylation	PTNRSRVTKSGSRGM CCCHHHCCCCCCCCC	20.55	26074081
563	Phosphorylation	NRSRVTKSGSRGMER CHHHCCCCCCCCCEE	32.41	27422710
565	Phosphorylation	SRVTKSGSRGMERTV HHCCCCCCCCCEEEE	32.52	27422710
571	Phosphorylation	GSRGMERTVVMDKSK CCCCCEEEEEEECCC	12.26	26074081
576	Acetylation	ERTVVMDKSKGEPVI EEEEEEECCCCCEEE	35.65	25953088
577	O-linked_Glycosylation	RTVVMDKSKGEPVIS EEEEEECCCCCEEEE	41.45	30379171
577	Phosphorylation	RTVVMDKSKGEPVIS EEEEEECCCCCEEEE	41.45	29083192
578	Sumoylation	TVVMDKSKGEPVISV EEEEECCCCCEEEEE	73.38	28112733
578	Ubiquitination	TVVMDKSKGEPVISV EEEEECCCCCEEEEE	73.38	33845483
584	Phosphorylation	SKGEPVISVKTTSRS CCCCEEEEEEECCCC	20.14	26074081
586	Acetylation	GEPVISVKTTSRSKE CCEEEEEEECCCCHH	39.02	25953088
586	Sumoylation	GEPVISVKTTSRSKE CCEEEEEEECCCCHH	39.02	28112733
586	Ubiquitination	GEPVISVKTTSRSKE CCEEEEEEECCCCHH	39.02	21963094
587	Phosphorylation	EPVISVKTTSRSKER CEEEEEEECCCCHHC	28.04	26074081
588	Phosphorylation	PVISVKTTSRSKERS EEEEEEECCCCHHCC	19.20	26074081
589	Phosphorylation	VISVKTTSRSKERSS EEEEEECCCCHHCCC	39.53	22210691
591	Phosphorylation	SVKTTSRSKERSSKS EEEECCCCHHCCCCC	38.34	26074081
595	Phosphorylation	TSRSKERSSKSQDRK CCCCHHCCCCCCCCC	43.12	26074081
596	Phosphorylation	SRSKERSSKSQDRKS CCCHHCCCCCCCCCH	42.41	26074081
598	Phosphorylation	SKERSSKSQDRKSES CHHCCCCCCCCCHHH	38.98	26074081
608	Sumoylation	RKSESKEKRDILSFD CCHHHHHHHHHHCHH	60.14	28112733
613	Phosphorylation	KEKRDILSFDKIKEQ HHHHHHHCHHHHHHH	31.56	30266825
616	Acetylation	RDILSFDKIKEQRER HHHHCHHHHHHHHHH	54.38	19608861
616	Sumoylation	RDILSFDKIKEQRER HHHHCHHHHHHHHHH	54.38	28112733
616	Ubiquitination	RDILSFDKIKEQRER HHHHCHHHHHHHHHH	54.38	21906983
618	Ubiquitination	ILSFDKIKEQRERER HHCHHHHHHHHHHHH	54.24	22817900
730	Methylation	QERRPGRRPYDLDRR HHHCCCCCCCCCCCC	39.79	-
741	Phosphorylation	LDRRDDAYWPEGKRV CCCCCCCCCCCCCCC	28.61	17360941
746	2-Hydroxyisobutyrylation	DAYWPEGKRVAMEDR CCCCCCCCCCCCHHH	41.88	-
746	Acetylation	DAYWPEGKRVAMEDR CCCCCCCCCCCCHHH	41.88	26051181
753	Methylation	KRVAMEDRYRADFPR CCCCCHHHHCCCCCC	14.99	115493179
754	Phosphorylation	RVAMEDRYRADFPRP CCCCHHHHCCCCCCC	23.60	-
773	Methylation	HDFDHRDRGQYQDHA CCCCCCCCCCCCCCC	33.79	115493161
776	Phosphorylation	DHRDRGQYQDHAIDR CCCCCCCCCCCCCCC	20.80	29759185
787	Phosphorylation	AIDRREGSRPMMGDH CCCCCCCCCCCCCCC	28.58	23401153
818	Phosphorylation	PERHGRDSRDGWGGY CCCCCCCCCCCCCCC	30.80	30576142
825	Phosphorylation	SRDGWGGYGSDKRLS CCCCCCCCCCCCCCC	14.98	28152594
827	Phosphorylation	DGWGGYGSDKRLSEG CCCCCCCCCCCCCCC	31.32	23927012
829	Acetylation	WGGYGSDKRLSEGRG CCCCCCCCCCCCCCC	57.86	130161
829	Methylation	WGGYGSDKRLSEGRG CCCCCCCCCCCCCCC	57.86	130161
832	Phosphorylation	YGSDKRLSEGRGLPP CCCCCCCCCCCCCCC	41.88	28355574
835	Methylation	DKRLSEGRGLPPPPR CCCCCCCCCCCCCCC	39.15	54558987
842	Methylation	RGLPPPPRGGRDWGE CCCCCCCCCCCCCHH	67.00	80701719
845	Methylation	PPPPRGGRDWGEHNQ CCCCCCCCCCHHHHH	39.06	115386497
872	Phosphorylation	AMDAGAASREHARWQ HHHHCHHHHHHHHHC	37.35	28555341
883	Methylation	ARWQGGERGLSGPSG HHHCCCCCCCCCCCC	55.41	100494617
886	Phosphorylation	QGGERGLSGPSGPGH CCCCCCCCCCCCCCC	52.02	28348404
889	Phosphorylation	ERGLSGPSGPGHMAS CCCCCCCCCCCCCCC	62.23	27732954
896	Phosphorylation	SGPGHMASRGGVAGR CCCCCCCCCCCCCCC	24.71	20068231
897	Dimethylation	GPGHMASRGGVAGRG CCCCCCCCCCCCCCC	36.03	-
897	Methylation	GPGHMASRGGVAGRG CCCCCCCCCCCCCCC	36.03	24129315
903	Dimethylation	SRGGVAGRGGFAQGG CCCCCCCCCCCCCCC	32.12	-
903	Methylation	SRGGVAGRGGFAQGG CCCCCCCCCCCCCCC	32.12	24129315
912	Phosphorylation	GFAQGGHSQGHVVPG CCCCCCCCCCCCCCC	40.92	27251275
932	Methylation	GGVASQDRGSRVPHP CCCCCCCCCCCCCCC	37.03	115368081
935	Methylation	ASQDRGSRVPHPHPH CCCCCCCCCCCCCCC	49.13	115493167

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 SAFB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SAFB2_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 SAFB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR1_HUMAN	ESR1	physical	12660241
VINEX_HUMAN	SORBS3	physical	12660241
SCG1_HUMAN	CHGB	physical	16169070
NCOR1_HUMAN	NCOR1	physical	16195251
SRCAP_HUMAN	SRCAP	physical	22939629
ZSC18_HUMAN	ZSCAN18	physical	21988832
P53_HUMAN	TP53	physical	21130767
HNRL1_HUMAN	HNRNPUL1	physical	26344197
SAFB1_HUMAN	SAFB	physical	26344197
LA_HUMAN	SSB	physical	26344197
DHYS_HUMAN	DHPS	physical	28514442
TRIP6_HUMAN	TRIP6	physical	28514442
CIZ1_HUMAN	CIZ1	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 SAFB2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-195 AND THR-201, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-293; LYS-424; LYS-429 ANDLYS-616, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-195 AND SER-207, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-195 AND THR-201, AND MASS SPECTROMETRY.	19413330 [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-207; SER-287; SER-343AND SER-613, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASSSPECTROMETRY.	17287340 [Abstract]
"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 SER-31, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-343 ANDSER-513, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.	15302935 [Abstract]
Sumoylation
Reference	PubMed
"Co-repressor activity of scaffold attachment factor B1 requiressumoylation."; Garee J.P., Meyer R., Oesterreich S.; Biochem. Biophys. Res. Commun. 408:516-522(2011). Cited for: SUMOYLATION AT LYS-230 AND LYS-293.	21527249 [Abstract]