dbPTM

SYMPK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYMPK_HUMAN
UniProt AC	Q92797
Protein Name	Symplekin
Gene Name	SYMPK
Organism	Homo sapiens (Human).
Sequence Length	1274
Subcellular Localization	Cytoplasm, cytoskeleton. Cell junction, tight junction. Cell membrane Peripheral membrane protein Cytoplasmic side. Cell junction. Nucleus, nucleoplasm. Cytoplasmic face of adhesion plaques (major) and nucleoplasm (minor) (in cells with TJ). Nucleo
Protein Description	Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity..
Protein Sequence	MASGSGDSVTRRSVASQFFTQEEGPGIDGMTTSERVVDLLNQAALITNDSKITVLKQVQELIINKDPTLLDNFLDEIIAFQADKSIEVRKFVIGFIEEACKRDIELLLKLIANLNMLLRDENVNVVKKAILTMTQLYKVALQWMVKSRVISELQEACWDMVSAMAGDIILLLDSDNDGIRTHAIKFVEGLIVTLSPRMADSEIPRRQEHDISLDRIPRDHPYIQYNVLWEEGKAALEQLLKFMVHPAISSINLTTALGSLANIARQRPMFMSEVIQAYETLHANLPPTLAKSQVSSVRKNLKLHLLSVLKHPASLEFQAQITTLLVDLGTPQAEIARNMPSSKDTRKRPRDDSDSTLKKMKLEPNLGEDDEDKDLEPGPSGTSKASAQISGQSDTDITAEFLQPLLTPDNVANLVLISMVYLPEAMPASFQAIYTPVESAGTEAQIKHLARLMATQMTAAGLGPGVEQTKQCKEEPKEEKVVKTESVLIKRRLSAQGQAISVVGSLSSMSPLEEEAPQAKRRPEPIIPVTQPRLAGAGGRKKIFRLSDVLKPLTDAQVEAMKLGAVKRILRAEKAVACSGAAQVRIKILASLVTQFNSGLKAEVLSFILEDVRARLDLAFAWLYQEYNAYLAAGASGSLDKYEDCLIRLLSGLQEKPDQKDGIFTKVVLEAPLITESALEVVRKYCEDESRTYLGMSTLRDLIFKRPSRQFQYLHVLLDLSSHEKDKVRSQALLFIKRMYEKEQLREYVEKFALNYLQLLVHPNPPSVLFGADKDTEVAAPWTEETVKQCLYLYLALLPQNHKLIHELAAVYTEAIADIKRTVLRVIEQPIRGMGMNSPELLLLVENCPKGAETLVTRCLHSLTDKVPPSPELVKRVRDLYHKRLPDVRFLIPVLNGLEKKEVIQALPKLIKLNPIVVKEVFNRLLGTQHGEGNSALSPLNPGELLIALHNIDSVKCDMKSIIKATNLCFAERNVYTSEVLAVVMQQLMEQSPLPMLLMRTVIQSLTMYPRLGGFVMNILSRLIMKQVWKYPKVWEGFIKCCQRTKPQSFQVILQLPPQQLGAVFDKCPELREPLLAHVRSFTPHQQAHIPNSIMTILEASGKQEPEAKEAPAGPLEEDDLEPLTLAPAPAPRPPQDLIGLRLAQEKALKRQLEEEQKLKPGGVGAPSSSSPSPSPSARPGPPPSEEAMDFREEGPECETPGIFISMDDDSGLTEAALLDSSLEGPLPKETAAGGLTLKEERSPQTLAPVGEDAMKTPSPAAEDAREPEAKGNS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGSGDSV ------CCCCCCCCC	33.62	-
3	O-linked_Glycosylation	-----MASGSGDSVT -----CCCCCCCCCC	45.40	30379171
3	Phosphorylation	-----MASGSGDSVT -----CCCCCCCCCC	45.40	23403867
5	Phosphorylation	---MASGSGDSVTRR ---CCCCCCCCCCHH	36.61	23403867
8	Phosphorylation	MASGSGDSVTRRSVA CCCCCCCCCCHHHHH	28.99	23403867
13	Phosphorylation	GDSVTRRSVASQFFT CCCCCHHHHHHHHCC	20.81	26434776
16	Phosphorylation	VTRRSVASQFFTQEE CCHHHHHHHHCCCCC	25.93	26434776
20	Phosphorylation	SVASQFFTQEEGPGI HHHHHHCCCCCCCCC	36.04	23186163
132	Phosphorylation	VVKKAILTMTQLYKV HHHHHHHHHHHHHHH	16.44	20068231
134	Phosphorylation	KKAILTMTQLYKVAL HHHHHHHHHHHHHHH	15.36	21406692
137	Phosphorylation	ILTMTQLYKVALQWM HHHHHHHHHHHHHHH	8.13	20068231
147	Phosphorylation	ALQWMVKSRVISELQ HHHHHHHHHHHHHHH	21.99	-
193	Phosphorylation	FVEGLIVTLSPRMAD HEECEEEECCHHHCC	17.96	28842319
195	Phosphorylation	EGLIVTLSPRMADSE ECEEEECCHHHCCCC	10.90	28842319
198	Sulfoxidation	IVTLSPRMADSEIPR EEECCHHHCCCCCCC	5.73	21406390
201	Phosphorylation	LSPRMADSEIPRRQE CCHHHCCCCCCCHHC	28.08	-
215	Methylation	EHDISLDRIPRDHPY CCCCCHHCCCCCCCC	46.21	115918069
353	Phosphorylation	RKRPRDDSDSTLKKM CCCCCCCCCHHHHHH	37.44	26074081
355	Phosphorylation	RPRDDSDSTLKKMKL CCCCCCCHHHHHHCC	39.32	26074081
356	Phosphorylation	PRDDSDSTLKKMKLE CCCCCCHHHHHHCCC	47.81	26074081
358	Acetylation	DDSDSTLKKMKLEPN CCCCHHHHHHCCCCC	51.41	23954790
361	Sumoylation	DSTLKKMKLEPNLGE CHHHHHHCCCCCCCC	59.59	-
361	Sumoylation	DSTLKKMKLEPNLGE CHHHHHHCCCCCCCC	59.59	25114211
361	Ubiquitination	DSTLKKMKLEPNLGE CHHHHHHCCCCCCCC	59.59	-
361	Acetylation	DSTLKKMKLEPNLGE CHHHHHHCCCCCCCC	59.59	23236377
373	Acetylation	LGEDDEDKDLEPGPS CCCCCCCCCCCCCCC	63.26	26051181
455	Phosphorylation	HLARLMATQMTAAGL HHHHHHHHHHHHCCC	12.61	20068231
458	Phosphorylation	RLMATQMTAAGLGPG HHHHHHHHHCCCCCC	11.98	27050516
469	Phosphorylation	LGPGVEQTKQCKEEP CCCCHHHHHHHCCCC	15.02	20068231
483	Sumoylation	PKEEKVVKTESVLIK CCCCCEEEHHHHHHH	49.95	-
483	Sumoylation	PKEEKVVKTESVLIK CCCCCEEEHHHHHHH	49.95	28112733
483	Ubiquitination	PKEEKVVKTESVLIK CCCCCEEEHHHHHHH	49.95	-
484	Phosphorylation	KEEKVVKTESVLIKR CCCCEEEHHHHHHHH	23.14	20068231
486	Phosphorylation	EKVVKTESVLIKRRL CCEEEHHHHHHHHHH	27.70	20068231
490	Ubiquitination	KTESVLIKRRLSAQG EHHHHHHHHHHHHCC	27.57	-
490	2-Hydroxyisobutyrylation	KTESVLIKRRLSAQG EHHHHHHHHHHHHCC	27.57	-
494	Phosphorylation	VLIKRRLSAQGQAIS HHHHHHHHHCCCEEE	19.41	29255136
501	Phosphorylation	SAQGQAISVVGSLSS HHCCCEEEEEECHHH	17.48	30278072
505	Phosphorylation	QAISVVGSLSSMSPL CEEEEEECHHHCCCC	17.30	30278072
507	Phosphorylation	ISVVGSLSSMSPLEE EEEEECHHHCCCCHH	26.20	23927012
508	Phosphorylation	SVVGSLSSMSPLEEE EEEECHHHCCCCHHH	28.68	30278072
510	Phosphorylation	VGSLSSMSPLEEEAP EECHHHCCCCHHHCC	28.42	30278072
520	Ubiquitination	EEEAPQAKRRPEPII HHHCCHHHCCCCCCC	43.63	21906983
520 (in isoform 1)	Ubiquitination	-	43.63	21890473
520 (in isoform 2)	Ubiquitination	-	43.63	21890473
530	Phosphorylation	PEPIIPVTQPRLAGA CCCCCCCCCCCCCCC	27.74	28555341
547	Phosphorylation	RKKIFRLSDVLKPLT CCCEEEHHHCHHCCC	22.78	25159151
551	Ubiquitination	FRLSDVLKPLTDAQV EEHHHCHHCCCHHHH	37.52	21890473
551	Acetylation	FRLSDVLKPLTDAQV EEHHHCHHCCCHHHH	37.52	26051181
551 (in isoform 1)	Ubiquitination	-	37.52	21890473
551 (in isoform 2)	Ubiquitination	-	37.52	21890473
554	Phosphorylation	SDVLKPLTDAQVEAM HHCHHCCCHHHHHHH	37.50	20068231
562	Ubiquitination	DAQVEAMKLGAVKRI HHHHHHHHHHHHHHH	51.31	-
574	Ubiquitination	KRILRAEKAVACSGA HHHHHHHHHHHCCCC	47.37	-
624	Phosphorylation	DLAFAWLYQEYNAYL HHHHHHHHHHHHHHH	6.65	22817900
627	Phosphorylation	FAWLYQEYNAYLAAG HHHHHHHHHHHHHCC	6.92	22817900
642	Phosphorylation	ASGSLDKYEDCLIRL CCCCHHHHHHHHHHH	19.37	22817900
651	Phosphorylation	DCLIRLLSGLQEKPD HHHHHHHHCCCCCCC	41.89	-
656	Ubiquitination	LLSGLQEKPDQKDGI HHHCCCCCCCCCCCC	40.72	21906983
656	Acetylation	LLSGLQEKPDQKDGI HHHCCCCCCCCCCCC	40.72	26051181
656 (in isoform 1)	Ubiquitination	-	40.72	21890473
666	Ubiquitination	QKDGIFTKVVLEAPL CCCCCEEEEHEECCC	21.43	-
693	Phosphorylation	CEDESRTYLGMSTLR CCCCCCCCCCHHHHH	10.51	21712546
697	Phosphorylation	SRTYLGMSTLRDLIF CCCCCCHHHHHHHHH	23.61	21712546
698	Phosphorylation	RTYLGMSTLRDLIFK CCCCCHHHHHHHHHC	19.54	21712546
705	Ubiquitination	TLRDLIFKRPSRQFQ HHHHHHHCCCCHHHH	57.30	-
737	Acetylation	SQALLFIKRMYEKEQ HHHHHHHHHHHCHHH	24.63	26051181
742	Ubiquitination	FIKRMYEKEQLREYV HHHHHHCHHHHHHHH	33.02	-
742	2-Hydroxyisobutyrylation	FIKRMYEKEQLREYV HHHHHHCHHHHHHHH	33.02	-
742	Acetylation	FIKRMYEKEQLREYV HHHHHHCHHHHHHHH	33.02	26822725
848	Glutathionylation	LLLLVENCPKGAETL HHHEEECCCCCHHHH	2.03	22555962
866	Ubiquitination	CLHSLTDKVPPSPEL HHHHHCCCCCCCHHH	51.94	-
870	Phosphorylation	LTDKVPPSPELVKRV HCCCCCCCHHHHHHH	25.57	25850435
875	Ubiquitination	PPSPELVKRVRDLYH CCCHHHHHHHHHHHH	58.77	-
900	2-Hydroxyisobutyrylation	PVLNGLEKKEVIQAL HCCCCCCHHHHHHHH	60.31	-
901	Ubiquitination	VLNGLEKKEVIQALP CCCCCCHHHHHHHHH	48.08	-
909	Ubiquitination	EVIQALPKLIKLNPI HHHHHHHHHHHCCHH	64.79	21890473
909	Acetylation	EVIQALPKLIKLNPI HHHHHHHHHHHCCHH	64.79	26051181
909 (in isoform 1)	Ubiquitination	-	64.79	21890473
912	Ubiquitination	QALPKLIKLNPIVVK HHHHHHHHCCHHHHH	53.28	-
912	Malonylation	QALPKLIKLNPIVVK HHHHHHHHCCHHHHH	53.28	26320211
912	Acetylation	QALPKLIKLNPIVVK HHHHHHHHCCHHHHH	53.28	25953088
919	Ubiquitination	KLNPIVVKEVFNRLL HCCHHHHHHHHHHHH	36.95	21890473
919	Acetylation	KLNPIVVKEVFNRLL HCCHHHHHHHHHHHH	36.95	26051181
919 (in isoform 1)	Ubiquitination	-	36.95	21890473
935	Phosphorylation	TQHGEGNSALSPLNP CCCCCCCCCCCCCCH	41.25	29523821
938	Phosphorylation	GEGNSALSPLNPGEL CCCCCCCCCCCHHHH	27.36	25159151
960	Ubiquitination	DSVKCDMKSIIKATN CCCCCCHHHHHHHHC	25.83	-
961	Phosphorylation	SVKCDMKSIIKATNL CCCCCHHHHHHHHCC	23.94	24719451
964	Ubiquitination	CDMKSIIKATNLCFA CCHHHHHHHHCCCHH	47.70	-
964	Malonylation	CDMKSIIKATNLCFA CCHHHHHHHHCCCHH	47.70	26320211
978	Phosphorylation	AERNVYTSEVLAVVM HCCCCCHHHHHHHHH	14.18	22210691
1001	Phosphorylation	LPMLLMRTVIQSLTM HHHHHHHHHHHHHHC	14.16	21406692
1005	Phosphorylation	LMRTVIQSLTMYPRL HHHHHHHHHHCCHHH	18.06	21406692
1007	Phosphorylation	RTVIQSLTMYPRLGG HHHHHHHHCCHHHHH	21.65	21406692
1009	Phosphorylation	VIQSLTMYPRLGGFV HHHHHHCCHHHHHHH	4.67	22210691
1021	Phosphorylation	GFVMNILSRLIMKQV HHHHHHHHHHHHHHH	22.65	20068231
1031	Phosphorylation	IMKQVWKYPKVWEGF HHHHHHCCHHHHHHH	7.80	22817900
1040	Ubiquitination	KVWEGFIKCCQRTKP HHHHHHHHHHHHCCC	27.05	21890473
1040	Malonylation	KVWEGFIKCCQRTKP HHHHHHHHHHHHCCC	27.05	26320211
1040	Acetylation	KVWEGFIKCCQRTKP HHHHHHHHHHHHCCC	27.05	26051181
1040 (in isoform 1)	Ubiquitination	-	27.05	21890473
1081	Phosphorylation	PLLAHVRSFTPHQQA HHHHHHHHCCHHHHC	32.17	30576142
1083	Phosphorylation	LAHVRSFTPHQQAHI HHHHHHCCHHHHCCC	22.55	25159151
1103	Ubiquitination	TILEASGKQEPEAKE HHHHHCCCCCCCHHC	49.33	-
1147	Ubiquitination	GLRLAQEKALKRQLE HHHHHHHHHHHHHHH	47.11	-
1147	Acetylation	GLRLAQEKALKRQLE HHHHHHHHHHHHHHH	47.11	25953088
1150	Methylation	LAQEKALKRQLEEEQ HHHHHHHHHHHHHHH	42.85	116253337
1160	Ubiquitination	LEEEQKLKPGGVGAP HHHHHCCCCCCCCCC	48.96	-
1168	Phosphorylation	PGGVGAPSSSSPSPS CCCCCCCCCCCCCCC	42.17	23401153
1169	Phosphorylation	GGVGAPSSSSPSPSP CCCCCCCCCCCCCCC	33.50	30266825
1170	Phosphorylation	GVGAPSSSSPSPSPS CCCCCCCCCCCCCCC	51.08	30266825
1171	Phosphorylation	VGAPSSSSPSPSPSA CCCCCCCCCCCCCCC	31.20	29255136
1173	Phosphorylation	APSSSSPSPSPSARP CCCCCCCCCCCCCCC	39.70	29255136
1175	Phosphorylation	SSSSPSPSPSARPGP CCCCCCCCCCCCCCC	35.51	19664994
1177	Phosphorylation	SSPSPSPSARPGPPP CCCCCCCCCCCCCCC	41.05	30266825
1185	Phosphorylation	ARPGPPPSEEAMDFR CCCCCCCCHHHCCHH	54.57	30175587
1221	Phosphorylation	TEAALLDSSLEGPLP CHHHHHCCCCCCCCC	36.47	26074081
1222	Phosphorylation	EAALLDSSLEGPLPK HHHHHCCCCCCCCCC	30.06	26074081
1231	Phosphorylation	EGPLPKETAAGGLTL CCCCCCCCCCCCCEE	28.12	23927012
1231	O-linked_Glycosylation	EGPLPKETAAGGLTL CCCCCCCCCCCCCEE	28.12	30379171
1237	Phosphorylation	ETAAGGLTLKEERSP CCCCCCCEECCCCCC	38.77	23401153
1239	Acetylation	AAGGLTLKEERSPQT CCCCCEECCCCCCCC	52.90	25953088
1239	Sumoylation	AAGGLTLKEERSPQT CCCCCEECCCCCCCC	52.90	25114211
1243	Phosphorylation	LTLKEERSPQTLAPV CEECCCCCCCCCCCC	25.33	19664994
1246	Phosphorylation	KEERSPQTLAPVGED CCCCCCCCCCCCCCC	28.42	29255136
1255	Sulfoxidation	APVGEDAMKTPSPAA CCCCCCCCCCCCCHH	8.42	21406390
1257	Phosphorylation	VGEDAMKTPSPAAED CCCCCCCCCCCHHHH	18.86	29255136
1259	Phosphorylation	EDAMKTPSPAAEDAR CCCCCCCCCHHHHHC	32.19	29255136
1274	Phosphorylation	EPEAKGNS------- CCHHCCCC-------	50.71	26074081

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
1257	T	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSU72_HUMAN	SSU72	physical	20861839
KAT6A_HUMAN	KAT6A	physical	23994619
KMT2A_HUMAN	KMT2A	physical	23994619
CPSF3_HUMAN	CPSF3	physical	26344197
CPSF4_HUMAN	CPSF4	physical	26344197
UBP24_HUMAN	USP24	physical	26344197
WDR33_HUMAN	WDR33	physical	26344197
CLK1_HUMAN	CLK1	physical	26496610
CSTF2_HUMAN	CSTF2	physical	26496610
CSTF3_HUMAN	CSTF3	physical	26496610
FINC_HUMAN	FN1	physical	26496610
PDIA1_HUMAN	P4HB	physical	26496610
CPSF4_HUMAN	CPSF4	physical	26496610
CPSF1_HUMAN	CPSF1	physical	26496610
CPSF3_HUMAN	CPSF3	physical	26496610
CPSF2_HUMAN	CPSF2	physical	26496610
WDR33_HUMAN	WDR33	physical	26496610
ELMO3_HUMAN	ELMO3	physical	26496610
FIP1_HUMAN	FIP1L1	physical	26496610

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 SYMPK_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 THR-1257, AND MASS SPECTROMETRY.	19413330 [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-494 AND SER-1243, ANDMASS SPECTROMETRY.	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-1171; SER-1175;SER-1243; THR-1257 AND SER-1259, AND MASS SPECTROMETRY.	18669648 [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-1243, AND MASSSPECTROMETRY.	15302935 [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 THR-1257, AND MASS SPECTROMETRY.	19413330 [Abstract]