dbPTM

INT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	INT1_HUMAN
UniProt AC	Q8N201
Protein Name	Integrator complex subunit 1
Gene Name	INTS1
Organism	Homo sapiens (Human).
Sequence Length	2190
Subcellular Localization	Nucleus membrane Single-pass membrane protein .
Protein Description	Component of the Integrator (INT) 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 (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. [PubMed: 23904267]
Protein Sequence	MNRAKPTTVRRPSAAAKPSGHPPPGDFIALGSKGQANESKTASTLLKPAPSGLPSERKRDAAAALSSASALTGLTKRPKLSSTPPLSALGRLAEAAVAEKRAISPSIKEPSVVPIEVLPTVLLDEIEAAELEGNDDRIEGVLCGAVKQLKVTRAKPDSTLYLSLMYLAKIKPNIFATEGVIEALCSLLRRDASINFKAKGNSLVSVLACNLLMAAYEEDENWPEIFVKVYIEDSLGERIWVDSPHCKTFVDNIQTAFNTRMPPRSVLLQGEAGRVAGDLGAGSSPHPSLTEEEDSQTELLIAEEKLSPEQEGQLMPRYEELAESVEEYVLDMLRDQLNRRQPIDNVSRNLLRLLTSTCGYKEVRLLAVQKLEMWLQNPKLTRPAQDLLMSVCMNCNTHGSEDMDVISHLIKIRLKPKVLLNHFMLCIRELLSAHKDNLGTTIKLVIFNELSSARNPNNMQVLYTALQHSSELAPKFLAMVFQDLLTNKDDYLRASRALLREIIKQTKHEINFQAFCLGLMQERKEPQYLEMEFKERFVVHITDVLAVSMMLGITAQVKEAGIAWDKGEKRNLEVLRSFQNQIAAIQRDAVWWLHTVVPSISKLAPKDYVHCLHKVLFTEQPETYYKWDNWPPESDRNFFLRLCSEVPILEDTLMRILVIGLSRELPLGPADAMELADHLVKRAAAVQADDVEVLKVGRTQLIDAVLNLCTYHHPENIQLPPGYQPPNLAISTLYWKAWPLLLVVAAFNPENIGLAAWEEYPTLKMLMEMVMTNNYSYPPCTLTDEETRTEMLNRELQTAQREKQEILAFEGHLAAASTKQTITESSSLLLSQLTSLDPQGPPRRPPPHILDQVKSLNQSLRLGHLLCRSRNPDFLLHIIQRQASSQSMPWLADLVQSSEGSLDVLPVQCLCEFLLHDAVDDAASGEEDDEGESKEQKAKKRQRQQKQRQLLGRLQDLLLGPKADEQTTCEVLDYFLRRLGSSQVASRVLAMKGLSLVLSEGSLRDGEEKEPPMEEDVGDTDVLQGYQWLLRDLPRLPLFDSVRSTTALALQQAIHMETDPQTISAYLIYLSQHTPVEEQAQHSDLALDVARLVVERSTIMSHLFSKLSPSAASDAVLSALLSIFSRYVRRMRQSKEGEEVYSWSESQDQVFLRWSSGETATMHILVVHAMVILLTLGPPRADDSEFQALLDIWFPEEKPLPTAFLVDTSEEALLLPDWLKLRMIRSEVLRLVDAALQDLEPQQLLLFVQSFGIPVSSMSKLLQFLDQAVAHDPQTLEQNIMDKNYMAHLVEVQHERGASGGQTFHSLLTASLPPRRDSTEAPKPKSSPEQPIGQGRIRVGTQLRVLGPEDDLAGMFLQIFPLSPDPRWQSSSPRPVALALQQALGQELARVVQGSPEVPGITVRVLQALATLLSSPHGGALVMSMHRSHFLACPLLRQLCQYQRCVPQDTGFSSLFLKVLLQMLQWLDSPGVEGGPLRAQLRMLASQASAGRRLSDVRGGLLRLAEALAFRQDLEVVSSTVRAVIATLRSGEQCSVEPDLISKVLQGLIEVRSPHLEELLTAFFSATADAASPFPACKPVVVVSSLLLQEEEPLAGGKPGADGGSLEAVRLGPSSGLLVDWLEMLDPEVVSSCPDLQLRLLFSRRKGKGQAQVPSFRPYLLTLFTHQSSWPTLHQCIRVLLGKSREQRFDPSASLDFLWACIHVPRIWQGRDQRTPQKRREELVLRVQGPELISLVELILAEAETRSQDGDTAACSLIQARLPLLLSCCCGDDESVRKVTEHLSGCIQQWGDSVLGRRCRDLLLQLYLQRPELRVPVPEVLLHSEGAASSSVCKLDGLIHRFITLLADTSDSRALENRGADASMACRKLAVAHPLLLLRHLPMIAALLHGRTHLNFQEFRQQNHLSCFLHVLGLLELLQPHVFRSEHQGALWDCLLSFIRLLLNYRKSSRHLAAFINKFVQFIHKYITYNAPAAISFLQKHADPLHDLSFDNSDLVMLKSLLAGLSLPSRDDRTDRGLDEEGEEESSAGSLPLVSVSLFTPLTAAEMAPYMKRLSRGQTVEDLLEVLSDIDEMSRRRPEILSFFSTNLQRLMSSAEECCRNLAFSLALRSMQNSPSIAAAFLPTFMYCLGSQDFEVVQTALRNLPEYALLCQEHAAVLLHRAFLVGMYGQMDPSAQISEALRILHMEAVM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	PTTVRRPSAAAKPSG CCCCCCCCCCCCCCC	28.82	27273156
17	Acetylation	RRPSAAAKPSGHPPP CCCCCCCCCCCCCCC	34.68	21743961
19	Phosphorylation	PSAAAKPSGHPPPGD CCCCCCCCCCCCCCC	49.37	28152594
32	Phosphorylation	GDFIALGSKGQANES CCEEEECCCCCCCCC	34.17	20873877
41	Phosphorylation	GQANESKTASTLLKP CCCCCCCCHHHHCCC	34.81	17929957
44	Phosphorylation	NESKTASTLLKPAPS CCCCCHHHHCCCCCC	33.38	17929957
47	Acetylation	KTASTLLKPAPSGLP CCHHHHCCCCCCCCC	42.10	19608861
51	Phosphorylation	TLLKPAPSGLPSERK HHCCCCCCCCCCHHH	55.88	27732954
55	Phosphorylation	PAPSGLPSERKRDAA CCCCCCCCHHHHHHH	55.89	24719451
66	Phosphorylation	RDAAAALSSASALTG HHHHHHHHHHHHHHC	21.09	22210691
67	Phosphorylation	DAAAALSSASALTGL HHHHHHHHHHHHHCC	27.39	22210691
69	Phosphorylation	AAALSSASALTGLTK HHHHHHHHHHHCCCC	26.26	20068231
72	Phosphorylation	LSSASALTGLTKRPK HHHHHHHHCCCCCCC	29.84	20068231
75	Phosphorylation	ASALTGLTKRPKLSS HHHHHCCCCCCCCCC	26.76	20068231
76	Acetylation	SALTGLTKRPKLSST HHHHCCCCCCCCCCC	72.28	25953088
76	Ubiquitination	SALTGLTKRPKLSST HHHHCCCCCCCCCCC	72.28	-
79	Ubiquitination	TGLTKRPKLSSTPPL HCCCCCCCCCCCCCH	66.10	-
81	Phosphorylation	LTKRPKLSSTPPLSA CCCCCCCCCCCCHHH	37.99	25159151
82	Phosphorylation	TKRPKLSSTPPLSAL CCCCCCCCCCCHHHH	56.20	23401153
83	Phosphorylation	KRPKLSSTPPLSALG CCCCCCCCCCHHHHH	26.08	29255136
87	Phosphorylation	LSSTPPLSALGRLAE CCCCCCHHHHHHHHH	27.50	23927012
100	2-Hydroxyisobutyrylation	AEAAVAEKRAISPSI HHHHHHHHHCCCCCC	37.07	-
100	Acetylation	AEAAVAEKRAISPSI HHHHHHHHHCCCCCC	37.07	23954790
100	Ubiquitination	AEAAVAEKRAISPSI HHHHHHHHHCCCCCC	37.07	24816145
104	Phosphorylation	VAEKRAISPSIKEPS HHHHHCCCCCCCCCC	16.17	23401153
106	Phosphorylation	EKRAISPSIKEPSVV HHHCCCCCCCCCCCE	39.23	30266825
111	Phosphorylation	SPSIKEPSVVPIEVL CCCCCCCCCEEEEEE	36.52	29496963
120	Phosphorylation	VPIEVLPTVLLDEIE EEEEEECEEHHHHHH	21.45	26074081
152	Phosphorylation	AVKQLKVTRAKPDST HHEECEEEECCCCCH	24.27	-
161	Phosphorylation	AKPDSTLYLSLMYLA CCCCCHHHHHHHHHH	8.37	-
193	Phosphorylation	SLLRRDASINFKAKG HHHCCCCCCCCCCCC	23.50	29396449
283	Phosphorylation	AGDLGAGSSPHPSLT CCCCCCCCCCCCCCC	39.91	23401153
284	Phosphorylation	GDLGAGSSPHPSLTE CCCCCCCCCCCCCCC	26.72	30278072
288	Phosphorylation	AGSSPHPSLTEEEDS CCCCCCCCCCCCCCH	44.91	30278072
290	Phosphorylation	SSPHPSLTEEEDSQT CCCCCCCCCCCCHHH	45.76	30278072
295	Phosphorylation	SLTEEEDSQTELLIA CCCCCCCHHHEEEEE	42.13	30278072
297	Phosphorylation	TEEEDSQTELLIAEE CCCCCHHHEEEEEHH	32.33	28450419
305	Ubiquitination	ELLIAEEKLSPEQEG EEEEEHHCCCHHHCC	45.85	21890473
307	Phosphorylation	LIAEEKLSPEQEGQL EEEHHCCCHHHCCCC	37.14	19664994
318	Phosphorylation	EGQLMPRYEELAESV CCCCCHHHHHHHHHH	14.11	26074081
361	Acetylation	LTSTCGYKEVRLLAV HHHCCCHHHHHHHHH	34.71	26051181
390	Phosphorylation	PAQDLLMSVCMNCNT CHHHHHHHHHHCCCC	16.48	20068231
397	Phosphorylation	SVCMNCNTHGSEDMD HHHHCCCCCCCCCHH	29.79	20068231
400	Phosphorylation	MNCNTHGSEDMDVIS HCCCCCCCCCHHHHH	23.87	20068231
407	Phosphorylation	SEDMDVISHLIKIRL CCCHHHHHHHHHHHC	16.46	20068231
440	Phosphorylation	AHKDNLGTTIKLVIF HCCCCCCCEEEEEEE	28.63	23403867
441	Phosphorylation	HKDNLGTTIKLVIFN CCCCCCCEEEEEEEH	17.83	23403867
491	Phosphorylation	LLTNKDDYLRASRAL HHCCHHHHHHHHHHH	14.28	-
495	Phosphorylation	KDDYLRASRALLREI HHHHHHHHHHHHHHH	16.20	24719451
528	Phosphorylation	QERKEPQYLEMEFKE HHCCCCCCCCCHHHH	18.49	29052541
534	Ubiquitination	QYLEMEFKERFVVHI CCCCCHHHHHHHHHH	34.37	24816145
569	Ubiquitination	IAWDKGEKRNLEVLR CCCCCCCCCCHHHHH	56.08	-
601	Phosphorylation	HTVVPSISKLAPKDY HHHHHHHHHHCCHHH	26.42	28787133
614	Ubiquitination	DYVHCLHKVLFTEQP HHHHHHHHHHHCCCC	27.90	29967540
623	Phosphorylation	LFTEQPETYYKWDNW HHCCCCCCCCCCCCC	38.54	18452278
624	Phosphorylation	FTEQPETYYKWDNWP HCCCCCCCCCCCCCC	11.03	18452278
681	Ubiquitination	ELADHLVKRAAAVQA HHHHHHHHHHHHCCC	42.55	21890473
695	Ubiquitination	ADDVEVLKVGRTQLI CCCCEEEEECHHHHH	48.06	21906983
803	Ubiquitination	LQTAQREKQEILAFE HHHHHHHHHHHHHHH	56.26	29967540
854	Ubiquitination	PHILDQVKSLNQSLR CCHHHHHHHHCHHHH	43.52	21890473
924	Phosphorylation	DAVDDAASGEEDDEG HHHCHHHCCCCCCCC	48.75	26657352
962	Ubiquitination	QDLLLGPKADEQTTC HHHHHCCCCCCHHHH	67.67	21987572
981	Phosphorylation	YFLRRLGSSQVASRV HHHHHHCCHHHHHHH	23.37	29449344
982	Phosphorylation	FLRRLGSSQVASRVL HHHHHCCHHHHHHHH	27.20	29449344
986	Phosphorylation	LGSSQVASRVLAMKG HCCHHHHHHHHHHHC	24.86	29449344
992	Ubiquitination	ASRVLAMKGLSLVLS HHHHHHHHCHHEEEC	51.60	21906983
995	Phosphorylation	VLAMKGLSLVLSEGS HHHHHCHHEEECCCC	25.71	20068231
999	Phosphorylation	KGLSLVLSEGSLRDG HCHHEEECCCCCCCC	32.22	20068231
1002	Phosphorylation	SLVLSEGSLRDGEEK HEEECCCCCCCCCCC	19.04	20068231
1009	Ubiquitination	SLRDGEEKEPPMEED CCCCCCCCCCCCCCC	71.82	21906983
1097	Phosphorylation	ARLVVERSTIMSHLF HHHHHHHHHHHHHHH	14.58	-
1101	Phosphorylation	VERSTIMSHLFSKLS HHHHHHHHHHHHHCC	17.12	-
1105	Phosphorylation	TIMSHLFSKLSPSAA HHHHHHHHHCCHHHH	38.76	24719451
1135	Ubiquitination	VRRMRQSKEGEEVYS HHHHHHCCCCCCCCC	62.49	21906983
1141	Phosphorylation	SKEGEEVYSWSESQD CCCCCCCCCCCCCCC	14.01	22210691
1142	Phosphorylation	KEGEEVYSWSESQDQ CCCCCCCCCCCCCCC	29.33	28348404
1144	Phosphorylation	GEEVYSWSESQDQVF CCCCCCCCCCCCCEE	22.79	28450419
1146	Phosphorylation	EVYSWSESQDQVFLR CCCCCCCCCCCEEEE	33.28	27251275
1299	Phosphorylation	VQHERGASGGQTFHS ECCCCCCCCCCHHHH	46.40	30624053
1303	Phosphorylation	RGASGGQTFHSLLTA CCCCCCCHHHHHHHC	26.96	30624053
1306	Phosphorylation	SGGQTFHSLLTASLP CCCCHHHHHHHCCCC	22.38	23312004
1309	Phosphorylation	QTFHSLLTASLPPRR CHHHHHHHCCCCCCC	21.35	30576142
1311	Phosphorylation	FHSLLTASLPPRRDS HHHHHHCCCCCCCCC	35.85	30576142
1318	Phosphorylation	SLPPRRDSTEAPKPK CCCCCCCCCCCCCCC	26.74	27273156
1319	Phosphorylation	LPPRRDSTEAPKPKS CCCCCCCCCCCCCCC	40.22	30278072
1323	Ubiquitination	RDSTEAPKPKSSPEQ CCCCCCCCCCCCCCC	72.61	24816145
1325	Ubiquitination	STEAPKPKSSPEQPI CCCCCCCCCCCCCCC	70.46	21906983
1326	Phosphorylation	TEAPKPKSSPEQPIG CCCCCCCCCCCCCCC	60.70	22167270
1327	Phosphorylation	EAPKPKSSPEQPIGQ CCCCCCCCCCCCCCC	38.28	22167270
1363	Phosphorylation	FLQIFPLSPDPRWQS HHEEEECCCCCCCCC	27.74	24719451
1395	Phosphorylation	LARVVQGSPEVPGIT HHHHHCCCCCCCCHH	10.78	29255136
1415	Phosphorylation	ALATLLSSPHGGALV HHHHHHCCCCCCCHH	22.38	-
1486	Phosphorylation	AQLRMLASQASAGRR HHHHHHHHHHHHCCC	23.47	24114839
1489	Phosphorylation	RMLASQASAGRRLSD HHHHHHHHHCCCHHH	24.50	24114839
1498	Methylation	GRRLSDVRGGLLRLA CCCHHHHHHHHHHHH	38.15	-
1543	Ubiquitination	VEPDLISKVLQGLIE CCHHHHHHHHHHHHH	39.71	21906983
1659	Phosphorylation	QVPSFRPYLLTLFTH CCCCCHHHHHHHHHC	15.30	22210691
1662	Phosphorylation	SFRPYLLTLFTHQSS CCHHHHHHHHHCCCC	19.75	22210691
1665	Phosphorylation	PYLLTLFTHQSSWPT HHHHHHHHCCCCCHH	23.32	22210691
1683	Ubiquitination	CIRVLLGKSREQRFD HHHHHHCCCHHHCCC	46.43	27667366
1747	Phosphorylation	LAEAETRSQDGDTAA HHHHHHCCCCCCHHH	39.79	25262027
1834	Ubiquitination	AASSSVCKLDGLIHR CCCCCCHHHHHHHHH	47.67	21963094
1868	Ubiquitination	DASMACRKLAVAHPL CHHHHHHHHHHHHHH	40.45	21906983
2006	Phosphorylation	KSLLAGLSLPSRDDR HHHHHCCCCCCCCCC	37.00	20068231
2043	Phosphorylation	VSLFTPLTAAEMAPY EECCCCCCHHHHHHH	25.65	-
2050	Phosphorylation	TAAEMAPYMKRLSRG CHHHHHHHHHHHCCC	13.01	-
2052	Ubiquitination	AEMAPYMKRLSRGQT HHHHHHHHHHCCCCC	44.32	23503661
2068	Phosphorylation	EDLLEVLSDIDEMSR HHHHHHHHCHHHHHH	37.38	-
2074	Phosphorylation	LSDIDEMSRRRPEIL HHCHHHHHHHCHHHH	22.16	-
2086	Phosphorylation	EILSFFSTNLQRLMS HHHHHHHHHHHHHHH	34.49	-

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 INT1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of INT1_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 INT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
INT2_HUMAN	INTS2	physical	20133760
INT3_HUMAN	INTS3	physical	20133760
INT4_HUMAN	INTS4	physical	20133760
INT5_HUMAN	INTS5	physical	20133760
INT6_HUMAN	INTS6	physical	20133760
INT6L_HUMAN	DDX26B	physical	20133760
INT7_HUMAN	INTS7	physical	20133760
INT8_HUMAN	INTS8	physical	20133760
INT9_HUMAN	INTS9	physical	20133760
INT10_HUMAN	INTS10	physical	20133760
INT11_HUMAN	CPSF3L	physical	20133760
INT12_HUMAN	INTS12	physical	20133760
RPB1_HUMAN	POLR2A	physical	20133760
RPB2_HUMAN	POLR2B	physical	20133760
RPAB3_HUMAN	POLR2H	physical	20133760
2AAA_HUMAN	PPP2R1A	physical	20133760
2AAB_HUMAN	PPP2R1B	physical	20133760
PP1B_HUMAN	PPP1CB	physical	20133760
PP2AA_HUMAN	PPP2CA	physical	20133760
PP2AB_HUMAN	PPP2CB	physical	20133760
INT13_HUMAN	ASUN	physical	20133760
INT14_HUMAN	VWA9	physical	20133760
CG026_HUMAN	C7orf26	physical	20133760
SOSB1_HUMAN	NABP2	physical	20133760
PKCB1_HUMAN	ZMYND8	physical	20133760
ZN687_HUMAN	ZNF687	physical	20133760
INT7_HUMAN	INTS7	physical	26344197

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 INT1_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-47, 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-1327 AND SER-1395, ANDMASS SPECTROMETRY.	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-1326, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-1327, ANDMASS SPECTROMETRY.	19413330 [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-1327, AND MASSSPECTROMETRY.	19007248 [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 THR-83, AND MASSSPECTROMETRY.	18691976 [Abstract]