dbPTM

INT12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	INT12_HUMAN
UniProt AC	Q96CB8
Protein Name	Integrator complex subunit 12
Gene Name	INTS12
Organism	Homo sapiens (Human).
Sequence Length	462
Subcellular Localization	Nucleus .
Protein Description	Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. [PubMed: 16239144 Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex]
Protein Sequence	MAATVNLELDPIFLKALGFLHSKSKDSAEKLKALLDESLARGIDSSYRPSQKDVEPPKISSTKNISIKQEPKISSSLPSGNNNGKVLTTEKVKKEAEKRPADKMKSDITEGVDIPKKPRLEKPETQSSPITVQSSKDLPMADLSSFEETSADDFAMEMGLACVVCRQMMVASGNQLVECQECHNLYHRDCHKPQVTDKEANDPRLVWYCARCTRQMKRMAQKTQKPPQKPAPAVVSVTPAVKDPLVKKPETKLKQETTFLAFKRTEVKTSTVISGNSSSASVSSSVTSGLTGWAAFAAKTSSAGPSTAKLSSTTQNNTGKPATSSANQKPVGLTGLATSSKGGIGSKIGSNNSTTPTVPLKPPPPLTLGKTGLSRSVSCDNVSKVGLPSPSSLVPGSSSQLSGNGNSGTSGPSGSTTSKTTSESSSSPSASLKGPTSQESQLNAMKRLQMVKKKAAQKKLKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
45	Phosphorylation	SLARGIDSSYRPSQK HHHCCCCCCCCCCCC	27.61	28787133
46	Phosphorylation	LARGIDSSYRPSQKD HHCCCCCCCCCCCCC	22.78	28348404
50	Phosphorylation	IDSSYRPSQKDVEPP CCCCCCCCCCCCCCC	40.64	28348404
60	Phosphorylation	DVEPPKISSTKNISI CCCCCCCCCCCCCCC	37.77	24719451
61	Phosphorylation	VEPPKISSTKNISIK CCCCCCCCCCCCCCC	47.04	28348404
63	Acetylation	PPKISSTKNISIKQE CCCCCCCCCCCCCCC	54.99	25953088
66	Phosphorylation	ISSTKNISIKQEPKI CCCCCCCCCCCCCCC	32.88	23186163
68	Acetylation	STKNISIKQEPKISS CCCCCCCCCCCCCCC	41.64	23749302
68	Sumoylation	STKNISIKQEPKISS CCCCCCCCCCCCCCC	41.64	28112733
68	Sumoylation	STKNISIKQEPKISS CCCCCCCCCCCCCCC	41.64	-
79	Phosphorylation	KISSSLPSGNNNGKV CCCCCCCCCCCCCCE	60.49	26714015
85	Acetylation	PSGNNNGKVLTTEKV CCCCCCCCEEEHHHH	35.87	23236377
91	Acetylation	GKVLTTEKVKKEAEK CCEEEHHHHHHHHHH	58.21	25953088
94	Acetylation	LTTEKVKKEAEKRPA EEHHHHHHHHHHCCH	66.21	7299073
105	Sumoylation	KRPADKMKSDITEGV HCCHHHHCCCCCCCC	51.20	-
105	Sumoylation	KRPADKMKSDITEGV HCCHHHHCCCCCCCC	51.20	-
106	Phosphorylation	RPADKMKSDITEGVD CCHHHHCCCCCCCCC	30.65	20068231
109	Phosphorylation	DKMKSDITEGVDIPK HHHCCCCCCCCCCCC	31.51	20068231
122	Methylation	PKKPRLEKPETQSSP CCCCCCCCCCCCCCC	53.39	-
122	Acetylation	PKKPRLEKPETQSSP CCCCCCCCCCCCCCC	53.39	25953088
125	Phosphorylation	PRLEKPETQSSPITV CCCCCCCCCCCCEEE	42.13	30266825
127	Phosphorylation	LEKPETQSSPITVQS CCCCCCCCCCEEECC	45.56	29255136
128	Phosphorylation	EKPETQSSPITVQSS CCCCCCCCCEEECCC	15.54	29255136
131	Phosphorylation	ETQSSPITVQSSKDL CCCCCCEEECCCCCC	18.84	30266825
134	Phosphorylation	SSPITVQSSKDLPMA CCCEEECCCCCCCCC	34.71	23927012
135	Phosphorylation	SPITVQSSKDLPMAD CCEEECCCCCCCCCC	17.07	23927012
192	Ubiquitination	LYHRDCHKPQVTDKE CCCCCCCCCCCCCCC	43.40	-
198	Ubiquitination	HKPQVTDKEANDPRL CCCCCCCCCCCCHHH	49.73	-
222	Acetylation	QMKRMAQKTQKPPQK HHHHHHHHHCCCCCC	43.30	19822337
229	Acetylation	KTQKPPQKPAPAVVS HHCCCCCCCCCCEEE	49.25	19822345
247	Ubiquitination	AVKDPLVKKPETKLK HHCCCCCCCCCCCCC	71.00	-
254	Sumoylation	KKPETKLKQETTFLA CCCCCCCCCCEEEEE	47.87	28112733
254	Sumoylation	KKPETKLKQETTFLA CCCCCCCCCCEEEEE	47.87	-
257	Phosphorylation	ETKLKQETTFLAFKR CCCCCCCEEEEEEEE	21.98	23403867
258	Phosphorylation	TKLKQETTFLAFKRT CCCCCCEEEEEEEEC	18.85	23403867
263	Acetylation	ETTFLAFKRTEVKTS CEEEEEEEECEEEEE	53.45	25953088
279	Phosphorylation	VISGNSSSASVSSSV EEECCCCCCCCCHHH	25.12	22210691
281	Phosphorylation	SGNSSSASVSSSVTS ECCCCCCCCCHHHHC	25.20	22210691
287	Phosphorylation	ASVSSSVTSGLTGWA CCCCHHHHCCCCHHH	21.01	22210691
311	O-linked_Glycosylation	GPSTAKLSSTTQNNT CCCCEECCCCCCCCC	25.57	30059200
314	O-linked_Glycosylation	TAKLSSTTQNNTGKP CEECCCCCCCCCCCC	31.11	30059200
318	O-linked_Glycosylation	SSTTQNNTGKPATSS CCCCCCCCCCCCCCC	54.88	30059200
320	Ubiquitination	TTQNNTGKPATSSAN CCCCCCCCCCCCCCC	29.46	-
320	Acetylation	TTQNNTGKPATSSAN CCCCCCCCCCCCCCC	29.46	26051181
323	O-linked_Glycosylation	NNTGKPATSSANQKP CCCCCCCCCCCCCCC	31.57	30059200
324	O-linked_Glycosylation	NTGKPATSSANQKPV CCCCCCCCCCCCCCC	29.56	30059200
325	O-linked_Glycosylation	TGKPATSSANQKPVG CCCCCCCCCCCCCCC	27.21	30059200
329	Ubiquitination	ATSSANQKPVGLTGL CCCCCCCCCCCEECE	41.29	-
329	Acetylation	ATSSANQKPVGLTGL CCCCCCCCCCCEECE	41.29	26051181
338	O-linked_Glycosylation	VGLTGLATSSKGGIG CCEECEECCCCCCCC	38.28	30059200
340	Phosphorylation	LTGLATSSKGGIGSK EECEECCCCCCCCCC	30.85	25627689
341	Acetylation	TGLATSSKGGIGSKI ECEECCCCCCCCCCC	62.01	26051181
347	Acetylation	SKGGIGSKIGSNNST CCCCCCCCCCCCCCC	45.96	25953088
350	Phosphorylation	GIGSKIGSNNSTTPT CCCCCCCCCCCCCCC	35.99	27251275
353	Phosphorylation	SKIGSNNSTTPTVPL CCCCCCCCCCCCCCC	37.60	27251275
354	Phosphorylation	KIGSNNSTTPTVPLK CCCCCCCCCCCCCCC	38.63	25159151
355	Phosphorylation	IGSNNSTTPTVPLKP CCCCCCCCCCCCCCC	19.45	25159151
357	Phosphorylation	SNNSTTPTVPLKPPP CCCCCCCCCCCCCCC	32.44	27251275
361	Acetylation	TTPTVPLKPPPPLTL CCCCCCCCCCCCCCC	49.78	25953088
367	Phosphorylation	LKPPPPLTLGKTGLS CCCCCCCCCCCCCCC	38.96	27251275
370	Acetylation	PPPLTLGKTGLSRSV CCCCCCCCCCCCCCC	42.40	25953088
371	Phosphorylation	PPLTLGKTGLSRSVS CCCCCCCCCCCCCCC	41.37	29514088
374	Phosphorylation	TLGKTGLSRSVSCDN CCCCCCCCCCCCCCC	24.69	29514088
376	Phosphorylation	GKTGLSRSVSCDNVS CCCCCCCCCCCCCCH	18.27	30266825
378	Phosphorylation	TGLSRSVSCDNVSKV CCCCCCCCCCCCHHC	19.59	23401153
383	Phosphorylation	SVSCDNVSKVGLPSP CCCCCCCHHCCCCCH	28.07	29396449
389	Phosphorylation	VSKVGLPSPSSLVPG CHHCCCCCHHHCCCC	42.32	25159151
391	Phosphorylation	KVGLPSPSSLVPGSS HCCCCCHHHCCCCCC	40.41	25159151
392	Phosphorylation	VGLPSPSSLVPGSSS CCCCCHHHCCCCCCC	36.45	25627689
397	Phosphorylation	PSSLVPGSSSQLSGN HHHCCCCCCCCCCCC	22.27	29978859
398	Phosphorylation	SSLVPGSSSQLSGNG HHCCCCCCCCCCCCC	28.19	29978859
399	Phosphorylation	SLVPGSSSQLSGNGN HCCCCCCCCCCCCCC	36.52	29978859
402	Phosphorylation	PGSSSQLSGNGNSGT CCCCCCCCCCCCCCC	23.68	29978859
407	Phosphorylation	QLSGNGNSGTSGPSG CCCCCCCCCCCCCCC	44.86	23186163
419	Methylation	PSGSTTSKTTSESSS CCCCCCCCCCCCCCC	54.45	-
420	Phosphorylation	SGSTTSKTTSESSSS CCCCCCCCCCCCCCC	35.01	27251275
421	Phosphorylation	GSTTSKTTSESSSSP CCCCCCCCCCCCCCC	33.94	27251275
422	Phosphorylation	STTSKTTSESSSSPS CCCCCCCCCCCCCCC	40.49	25627689
424	Phosphorylation	TSKTTSESSSSPSAS CCCCCCCCCCCCCCC	34.97	29396449
425	Phosphorylation	SKTTSESSSSPSASL CCCCCCCCCCCCCCC	30.68	25262027
426	Phosphorylation	KTTSESSSSPSASLK CCCCCCCCCCCCCCC	56.39	25262027
427	Phosphorylation	TTSESSSSPSASLKG CCCCCCCCCCCCCCC	25.48	25159151
429	Phosphorylation	SESSSSPSASLKGPT CCCCCCCCCCCCCCC	32.22	22199227
431	Phosphorylation	SSSSPSASLKGPTSQ CCCCCCCCCCCCCCH	34.64	22199227
433	Methylation	SSPSASLKGPTSQES CCCCCCCCCCCCHHH	61.42	115974929
436	Phosphorylation	SASLKGPTSQESQLN CCCCCCCCCHHHHHH	52.27	27174698
437	Phosphorylation	ASLKGPTSQESQLNA CCCCCCCCHHHHHHH	34.77	25159151
440	Phosphorylation	KGPTSQESQLNAMKR CCCCCHHHHHHHHHH	32.12	27174698
446	Acetylation	ESQLNAMKRLQMVKK HHHHHHHHHHHHHHH	47.77	25953088
446	Ubiquitination	ESQLNAMKRLQMVKK HHHHHHHHHHHHHHH	47.77	-

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 INT12_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of INT12_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 INT12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
INT1_HUMAN	INTS1	physical	26344197
INT1_HUMAN	INTS1	physical	28514442
GT2D1_HUMAN	GTF2IRD1	physical	26275350

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 INT12_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-128 ANDSER-427, 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-128, AND MASSSPECTROMETRY.	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-128 AND SER-427, ANDMASS SPECTROMETRY.	18691976 [Abstract]