dbPTM

SSRP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SSRP1_HUMAN
UniProt AC	Q08945
Protein Name	FACT complex subunit SSRP1
Gene Name	SSRP1
Organism	Homo sapiens (Human).
Sequence Length	709
Subcellular Localization	Nucleus . Nucleus, nucleolus . Chromosome . Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Protein Description	Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63..
Protein Sequence	MAETLEFNDVYQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGMNPSYDEYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDRDEKKRKQLKKAKMAKDRKSRKKPVEVKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARRDYEKAMKEYEGGRGESSKRDKSKKKKKVKVKMEKKSTPSRGSSSKSSSRQLSESFKSKEFVSSDESSSGENKSKKKRRRSEDSEEEELASTPPSSEDSASGSDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAETLEFND ------CCCEEECHH	20.62	19413330
4	Phosphorylation	----MAETLEFNDVY ----CCCEEECHHHH	23.27	28464451
11	Phosphorylation	TLEFNDVYQEVKGSM EEECHHHHHHHHCCC	11.21	25147952
15	Ubiquitination	NDVYQEVKGSMNDGR HHHHHHHHCCCCCCC	44.51	21890473
17	Phosphorylation	VYQEVKGSMNDGRLR HHHHHHCCCCCCCEE	14.54	20068231
22	Methylation	KGSMNDGRLRLSRQG HCCCCCCCEEEEEEE	21.35	115917893
33	Acetylation	SRQGIIFKNSKTGKV EEEEEEEECCCCCCC	50.32	19608861
33	Ubiquitination	SRQGIIFKNSKTGKV EEEEEEEECCCCCCC	50.32	19608861
36	Ubiquitination	GIIFKNSKTGKVDNI EEEEECCCCCCCCCE	71.35	-
39	Acetylation	FKNSKTGKVDNIQAG EECCCCCCCCCEECC	52.20	26051181
39	Ubiquitination	FKNSKTGKVDNIQAG EECCCCCCCCCEECC	52.20	21890473
49	Phosphorylation	NIQAGELTEGIWRRV CEECCCCCCCHHHHH	28.06	-
63	Acetylation	VALGHGLKLLTKNGH HHHHCCEEEEECCCE	46.15	25953088
63	Ubiquitination	VALGHGLKLLTKNGH HHHHCCEEEEECCCE	46.15	21890473
67	Ubiquitination	HGLKLLTKNGHVYKY CCEEEEECCCEEEEE	61.98	-
73	Ubiquitination	TKNGHVYKYDGFRES ECCCEEEEECCCCHH	35.46	-
84	Acetylation	FRESEFEKLSDFFKT CCHHHHHHHHHHHHH	59.62	26822725
84	Ubiquitination	FRESEFEKLSDFFKT CCHHHHHHHHHHHHH	59.62	21890473
90	2-Hydroxyisobutyrylation	EKLSDFFKTHYRLEL HHHHHHHHHHHHHHH	34.09	-
90	Acetylation	EKLSDFFKTHYRLEL HHHHHHHHHHHHHHH	34.09	25825284
90	Methylation	EKLSDFFKTHYRLEL HHHHHHHHHHHHHHH	34.09	22633901
90	Sumoylation	EKLSDFFKTHYRLEL HHHHHHHHHHHHHHH	34.09	28112733
90	Ubiquitination	EKLSDFFKTHYRLEL HHHHHHHHHHHHHHH	34.09	21906983
100	2-Hydroxyisobutyrylation	YRLELMEKDLCVKGW HHHHHHHHCEEECCC	41.87	-
100	Acetylation	YRLELMEKDLCVKGW HHHHHHHHCEEECCC	41.87	25825284
100	Ubiquitination	YRLELMEKDLCVKGW HHHHHHHHCEEECCC	41.87	-
103	Glutathionylation	ELMEKDLCVKGWNWG HHHHHCEEECCCCCE	4.22	22555962
105	Acetylation	MEKDLCVKGWNWGTV HHHCEEECCCCCEEE	58.15	25953088
105	Sumoylation	MEKDLCVKGWNWGTV HHHCEEECCCCCEEE	58.15	-
105	Ubiquitination	MEKDLCVKGWNWGTV HHHCEEECCCCCEEE	58.15	-
111	Phosphorylation	VKGWNWGTVKFGGQL ECCCCCEEEEECCEE	16.49	30576142
120	Phosphorylation	KFGGQLLSFDIGDQP EECCEEEEEECCCCE	29.48	29496963
143	Methylation	VSQCTTGKNEVTLEF CCCCCCCCCEEEEEE	48.09	23583077
166	Phosphorylation	SLMEVRFYVPPTQED EEEEEEEECCCCCCC	11.07	28122231
170	Phosphorylation	VRFYVPPTQEDGVDP EEEECCCCCCCCCCH	38.22	21082442
200	Glutathionylation	QATGDAICIFRELQC HHCCCEEEEEEEEEE	2.29	22555962
207	Glutathionylation	CIFRELQCLTPRGRY EEEEEEEECCCCCCC	7.75	22555962
209	Phosphorylation	FRELQCLTPRGRYDI EEEEEECCCCCCCEE	20.68	25850435
219	Phosphorylation	GRYDIRIYPTFLHLH CCCEEEEEEEEEEEC	6.08	28152594
221	Phosphorylation	YDIRIYPTFLHLHGK CEEEEEEEEEEECCC	23.12	28152594
228	Acetylation	TFLHLHGKTFDYKIP EEEEECCCCCCCCCC	34.96	25825284
228	Ubiquitination	TFLHLHGKTFDYKIP EEEEECCCCCCCCCC	34.96	21890473
229	Phosphorylation	FLHLHGKTFDYKIPY EEEECCCCCCCCCCC	26.74	21406692
232	Phosphorylation	LHGKTFDYKIPYTTV ECCCCCCCCCCCHHH	13.46	21406692
233	Acetylation	HGKTFDYKIPYTTVL CCCCCCCCCCCHHHE	38.76	19608861
233	Ubiquitination	HGKTFDYKIPYTTVL CCCCCCCCCCCHHHE	38.76	21906983
236	Phosphorylation	TFDYKIPYTTVLRLF CCCCCCCCHHHEEEE	20.65	21406692
237	Phosphorylation	FDYKIPYTTVLRLFL CCCCCCCHHHEEEEE	12.69	21406692
238	Phosphorylation	DYKIPYTTVLRLFLL CCCCCCHHHEEEEEC	16.23	21406692
248	Acetylation	RLFLLPHKDQRQMFF EEEECCCCCCCEEEE	54.33	25953088
253	Sulfoxidation	PHKDQRQMFFVISLD CCCCCCEEEEEEEEC	2.83	28183972
258	Phosphorylation	RQMFFVISLDPPIKQ CEEEEEEEECCCCCC	22.78	22817900
270	Phosphorylation	IKQGQTRYHFLILLF CCCCCCEEEEEEEEE	10.58	20068231
278	Phosphorylation	HFLILLFSKDEDISL EEEEEEEECCCCEEE	38.88	20068231
296	Sumoylation	MNEEEVEKRFEGRLT CCHHHHHHHHCCCCC	68.51	28112733
304	Ubiquitination	RFEGRLTKNMSGSLY HHCCCCCCCCCCHHH	56.07	21890473
306	Sulfoxidation	EGRLTKNMSGSLYEM CCCCCCCCCCHHHHH	5.24	28183972
307	Phosphorylation	GRLTKNMSGSLYEMV CCCCCCCCCHHHHHH	34.32	20068231
309	Phosphorylation	LTKNMSGSLYEMVSR CCCCCCCHHHHHHHH	22.07	20068231
311	Phosphorylation	KNMSGSLYEMVSRVM CCCCCHHHHHHHHHH	12.04	20068231
315	Phosphorylation	GSLYEMVSRVMKALV CHHHHHHHHHHHHHH	20.18	20068231
319	Acetylation	EMVSRVMKALVNRKI HHHHHHHHHHHCCCE	35.39	25825284
319	Malonylation	EMVSRVMKALVNRKI HHHHHHHHHHHCCCE	35.39	26320211
319	Ubiquitination	EMVSRVMKALVNRKI HHHHHHHHHHHCCCE	35.39	21890473
325	Malonylation	MKALVNRKITVPGNF HHHHHCCCEECCCCC	37.21	30639696
325	Ubiquitination	MKALVNRKITVPGNF HHHHHCCCEECCCCC	37.21	-
327	Phosphorylation	ALVNRKITVPGNFQG HHHCCCEECCCCCCC	24.55	28348404
336	Phosphorylation	PGNFQGHSGAQCITC CCCCCCCCCCEEEEE	42.52	28348404
346	Acetylation	QCITCSYKASSGLLY EEEEEEEECCCCCEE	26.04	25953088
348	Phosphorylation	ITCSYKASSGLLYPL EEEEEECCCCCEEEE	22.31	27050516
349	Phosphorylation	TCSYKASSGLLYPLE EEEEECCCCCEEEEC	38.02	27050516
353	Phosphorylation	KASSGLLYPLERGFI ECCCCCEEEECCCEE	15.71	28152594
361	Phosphorylation	PLERGFIYVHKPPVH EECCCEEEEECCCEE	8.34	28152594
364	Acetylation	RGFIYVHKPPVHIRF CCEEEEECCCEEEEE	40.76	25825284
364	Sumoylation	RGFIYVHKPPVHIRF CCEEEEECCCEEEEE	40.76	28112733
364	Ubiquitination	RGFIYVHKPPVHIRF CCEEEEECCCEEEEE	40.76	-
375	Phosphorylation	HIRFDEISFVNFARG EEEECEEEEEEECCC	22.54	25850435
381	Methylation	ISFVNFARGTTTTRS EEEEEECCCCEEEEE	38.56	115917897
399	Phosphorylation	EIETKQGTQYTFSSI EEEECCCCEEEEEEE	18.86	21406692
401	Phosphorylation	ETKQGTQYTFSSIER EECCCCEEEEEEEEH	15.02	21406692
402	Phosphorylation	TKQGTQYTFSSIERE ECCCCEEEEEEEEHH	13.76	21406692
404	Phosphorylation	QGTQYTFSSIEREEY CCCEEEEEEEEHHHH	23.70	21406692
405	Phosphorylation	GTQYTFSSIEREEYG CCEEEEEEEEHHHHH	25.03	25849741
408	Methylation	YTFSSIEREEYGKLF EEEEEEEHHHHHHHH	40.14	115917901
413	Acetylation	IEREEYGKLFDFVNA EEHHHHHHHHHHHCH	45.11	19608861
413	Ubiquitination	IEREEYGKLFDFVNA EEHHHHHHHHHHHCH	45.11	19608861
421	Acetylation	LFDFVNAKKLNIKNR HHHHHCHHHCCCCCC	53.22	25953088
421	Ubiquitination	LFDFVNAKKLNIKNR HHHHHCHHHCCCCCC	53.22	-
437	Phosphorylation	LKEGMNPSYDEYADS CCCCCCCCHHHCCCC	39.96	22167270
438	Phosphorylation	KEGMNPSYDEYADSD CCCCCCCHHHCCCCC	17.66	22167270
441	Phosphorylation	MNPSYDEYADSDEDQ CCCCHHHCCCCCHHH	16.89	22167270
444	Phosphorylation	SYDEYADSDEDQHDA CHHHCCCCCHHHHHH	34.43	19664994
452	Phosphorylation	DEDQHDAYLERMKEE CHHHHHHHHHHHHHH	18.36	27273156
471	Phosphorylation	EENANDSSDDSGEET CCCCCCCCCCCCCCC	48.58	24275569
503	Phosphorylation	DSNASASSSSNEGDS HCCCCCCCCCCCCCC	37.19	24275569
510	Phosphorylation	SSSNEGDSDRDEKKR CCCCCCCCCHHHHHH	45.46	22817900
539	2-Hydroxyisobutyrylation	RKKPVEVKKGKDPNA CCCCCCCCCCCCCCC	42.16	-
542	Acetylation	PVEVKKGKDPNAPKR CCCCCCCCCCCCCCC	78.04	23749302
548	Acetylation	GKDPNAPKRPMSAYM CCCCCCCCCCCCHHH	67.72	19608861
551	Sulfoxidation	PNAPKRPMSAYMLWL CCCCCCCCCHHHHHH	4.09	28183972
554	Phosphorylation	PKRPMSAYMLWLNAS CCCCCCHHHHHHHHC	5.85	22817900
555	Sulfoxidation	KRPMSAYMLWLNASR CCCCCHHHHHHHHCH	1.85	28183972
561	Phosphorylation	YMLWLNASREKIKSD HHHHHHHCHHHHHCC	39.64	22817900
566	Ubiquitination	NASREKIKSDHPGIS HHCHHHHHCCCCCCC	61.98	21890473
567	Phosphorylation	ASREKIKSDHPGISI HCHHHHHCCCCCCCH	44.62	20068231
573	Phosphorylation	KSDHPGISITDLSKK HCCCCCCCHHHHHHH	25.92	30108239
575	Phosphorylation	DHPGISITDLSKKAG CCCCCCHHHHHHHHH	24.89	30108239
578	Phosphorylation	GISITDLSKKAGEIW CCCHHHHHHHHHHHH	34.61	30108239
579	2-Hydroxyisobutyrylation	ISITDLSKKAGEIWK CCHHHHHHHHHHHHC	54.67	-
579	Ubiquitination	ISITDLSKKAGEIWK CCHHHHHHHHHHHHC	54.67	-
580	Ubiquitination	SITDLSKKAGEIWKG CHHHHHHHHHHHHCC	59.24	-
586	Acetylation	KKAGEIWKGMSKEKK HHHHHHHCCCCHHHH	50.85	25953088
586	Ubiquitination	KKAGEIWKGMSKEKK HHHHHHHCCCCHHHH	50.85	-
609	2-Hydroxyisobutyrylation	DARRDYEKAMKEYEG HHHHHHHHHHHHHCC	47.77	-
612	2-Hydroxyisobutyrylation	RDYEKAMKEYEGGRG HHHHHHHHHHCCCCC	63.10	-
612	Acetylation	RDYEKAMKEYEGGRG HHHHHHHHHHCCCCC	63.10	30592673
612	Ubiquitination	RDYEKAMKEYEGGRG HHHHHHHHHHCCCCC	63.10	-
614	Phosphorylation	YEKAMKEYEGGRGES HHHHHHHHCCCCCCC	17.85	24275569
621	Phosphorylation	YEGGRGESSKRDKSK HCCCCCCCCCCCCCC	43.94	20068231
622	Phosphorylation	EGGRGESSKRDKSKK CCCCCCCCCCCCCCC	27.66	20068231
623	Acetylation	GGRGESSKRDKSKKK CCCCCCCCCCCCCCC	74.11	7495599
641	Phosphorylation	KVKMEKKSTPSRGSS CCCCCCCCCCCCCCC	57.53	23403867
642	Phosphorylation	VKMEKKSTPSRGSSS CCCCCCCCCCCCCCC	33.88	23403867
644	Phosphorylation	MEKKSTPSRGSSSKS CCCCCCCCCCCCCHH	49.73	23403867
645	Methylation	EKKSTPSRGSSSKSS CCCCCCCCCCCCHHH	50.66	54559697
647	Phosphorylation	KSTPSRGSSSKSSSR CCCCCCCCCCHHHHH	30.26	23403867
648	Phosphorylation	STPSRGSSSKSSSRQ CCCCCCCCCHHHHHH	44.61	26546556
649	Phosphorylation	TPSRGSSSKSSSRQL CCCCCCCCHHHHHHH	37.95	23403867
651	Phosphorylation	SRGSSSKSSSRQLSE CCCCCCHHHHHHHHH	35.18	20068231
652	Phosphorylation	RGSSSKSSSRQLSES CCCCCHHHHHHHHHH	33.02	20068231
653	Phosphorylation	GSSSKSSSRQLSESF CCCCHHHHHHHHHHH	31.01	25159151
657	Phosphorylation	KSSSRQLSESFKSKE HHHHHHHHHHHHCCH	23.90	23401153
659	Phosphorylation	SSRQLSESFKSKEFV HHHHHHHHHHCCHHH	34.30	29255136
661	Acetylation	RQLSESFKSKEFVSS HHHHHHHHCCHHHCC	70.65	23749302
661	Ubiquitination	RQLSESFKSKEFVSS HHHHHHHHCCHHHCC	70.65	-
662	Phosphorylation	QLSESFKSKEFVSSD HHHHHHHCCHHHCCC	35.09	25159151
667	Phosphorylation	FKSKEFVSSDESSSG HHCCHHHCCCCCCCC	37.08	29255136
668	Phosphorylation	KSKEFVSSDESSSGE HCCHHHCCCCCCCCC	39.84	29255136
671	Phosphorylation	EFVSSDESSSGENKS HHHCCCCCCCCCCHH	34.49	29255136
672	Phosphorylation	FVSSDESSSGENKSK HHCCCCCCCCCCHHH	40.07	29255136
673	Phosphorylation	VSSDESSSGENKSKK HCCCCCCCCCCHHHH	60.45	29255136
678	Phosphorylation	SSSGENKSKKKRRRS CCCCCCHHHHCCCCC	62.38	23401153
685	Phosphorylation	SKKKRRRSEDSEEEE HHHCCCCCCCCHHHH	43.90	30576142
688	Phosphorylation	KRRRSEDSEEEELAS CCCCCCCCHHHHHHC	42.74	16498457
695	Phosphorylation	SEEEELASTPPSSED CHHHHHHCCCCCCCC	54.81	24275569
696	Phosphorylation	EEEELASTPPSSEDS HHHHHHCCCCCCCCC	33.34	30177828
699	Phosphorylation	ELASTPPSSEDSASG HHHCCCCCCCCCCCC	47.79	30177828
700	Phosphorylation	LASTPPSSEDSASGS HHCCCCCCCCCCCCC	51.72	30177828
703	Phosphorylation	TPPSSEDSASGSDE- CCCCCCCCCCCCCC-	21.93	30177828
705	Phosphorylation	PSSEDSASGSDE--- CCCCCCCCCCCC---	42.66	30177828

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
510	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
510	S	Phosphorylation	Kinase	CK2	-	Uniprot
657	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
688	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
688	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SSRP1_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 SSRP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NEK9_HUMAN	NEK9	physical	14660563
AIRE_HUMAN	AIRE	physical	20085707
SP16H_HUMAN	SUPT16H	physical	19214185
RPC5_HUMAN	POLR3E	physical	19214185
RPB1_HUMAN	POLR2A	physical	19214185
RPA1_HUMAN	POLR1A	physical	19214185
MCM4_HUMAN	MCM4	physical	16902406
MCM6_HUMAN	MCM6	physical	16902406
MCM7_HUMAN	MCM7	physical	16902406
NEK9_HUMAN	NEK9	physical	16902406
SP16H_HUMAN	SUPT16H	physical	16902406
MCM2_HUMAN	MCM2	physical	16902406
MCM3_HUMAN	MCM3	physical	16902406
MCM5_HUMAN	MCM5	physical	16902406
SP16H_HUMAN	SUPT16H	physical	16713563
SP16H_HUMAN	SUPT16H	physical	16682447
TONSL_HUMAN	TONSL	physical	21055985
MMS22_HUMAN	MMS22L	physical	21055985
SP16H_HUMAN	SUPT16H	physical	21055985
MCM2_HUMAN	MCM2	physical	21055985
MCM3_HUMAN	MCM3	physical	21055985
MCM4_HUMAN	MCM4	physical	21055985
MCM5_HUMAN	MCM5	physical	21055985
MCM6_HUMAN	MCM6	physical	21055985
MCM7_HUMAN	MCM7	physical	21055985
H2A2C_HUMAN	HIST2H2AC	physical	21969370
H2B2E_HUMAN	HIST2H2BE	physical	21969370
H33_HUMAN	H3F3A	physical	21969370
VATB2_HUMAN	ATP6V1B2	physical	22863883
CUL1_HUMAN	CUL1	physical	22863883
DBLOH_HUMAN	DIABLO	physical	22863883
CSDE1_HUMAN	CSDE1	physical	22863883
SBNO1_HUMAN	SBNO1	physical	22863883
SP16H_HUMAN	SUPT16H	physical	22863883
TONSL_HUMAN	TONSL	physical	25184681
AN32A_HUMAN	ANP32A	physical	26344197
CHD1_HUMAN	CHD1	physical	26344197
CSK2B_HUMAN	CSNK2B	physical	26344197
HMGB1_HUMAN	HMGB1	physical	26344197
HMGB2_HUMAN	HMGB2	physical	26344197
NP1L1_HUMAN	NAP1L1	physical	26344197
PAF1_HUMAN	PAF1	physical	26344197
PSMD6_HUMAN	PSMD6	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RTF1_HUMAN	RTF1	physical	26344197
SAP18_HUMAN	SAP18	physical	26344197
ZCH18_HUMAN	ZC3H18	physical	26344197
TONSL_HUMAN	TONSL	physical	28514442
MMS22_HUMAN	MMS22L	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
XPC_HUMAN	XPC	physical	28514442
TIM_HUMAN	TIMELESS	physical	28514442
MCM2_HUMAN	MCM2	physical	28514442
MCM4_HUMAN	MCM4	physical	28514442
TPPC8_HUMAN	TRAPPC8	physical	28514442
E41L5_HUMAN	EPB41L5	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
SPT6H_HUMAN	SUPT6H	physical	28514442
MCM6_HUMAN	MCM6	physical	28514442
SLD5_HUMAN	GINS4	physical	28514442
MCM7_HUMAN	MCM7	physical	28514442
PARP1_HUMAN	PARP1	physical	28514442
CSK21_HUMAN	CSNK2A1	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 SSRP1_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-437 AND SER-444, 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-33; LYS-90; LYS-233 ANDLYS-413, 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-444, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.	19369195 [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-437 AND SER-444, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.	18318008 [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 THR-170; SER-437; SER-444;SER-667; SER-668; SER-671; SER-672 AND SER-673, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.	18691976 [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-444, 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-444, AND MASSSPECTROMETRY.	18220336 [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-444; SER-657 ANDSER-659, AND MASS SPECTROMETRY.	19007248 [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-657, AND MASSSPECTROMETRY.	17287340 [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 TYR-554; SER-561; SER-667;SER-668; SER-671; SER-672 AND SER-673, AND MASS SPECTROMETRY.	17081983 [Abstract]
"CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity."; Li Y., Keller D.M., Scott J.D., Lu H.; J. Biol. Chem. 280:11869-11875(2005). Cited for: PHOSPHORYLATION AT SER-510; SER-657 AND SER-688, AND MUTAGENESIS OFSER-510; SER-657 AND SER-688.	15659405 [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-444, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND MASSSPECTROMETRY.	15592455 [Abstract]