INT1_MOUSE
ID INT1_MOUSE Reviewed; 2195 AA.
AC Q6P4S8; Q0KK58; Q80UQ7; Q91Z01; Q9CTF7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Integrator complex subunit 1;
DE Short=Int1;
GN Name=Ints1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RG The German cDNA consortium;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2034-2195.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320; SER-1328 AND SER-1329,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH ESRRB.
RX PubMed=26206133; DOI=10.1038/ncomms8776;
RA Latos P.A., Goncalves A., Oxley D., Mohammed H., Turro E., Hemberger M.;
RT "Fgf and Esrrb integrate epigenetic and transcriptional networks that
RT regulate self-renewal of trophoblast stem cells.";
RL Nat. Commun. 6:7776-7776(2015).
CC -!- FUNCTION: Component of the Integrator (INT) complex, a complex involved
CC in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their
CC 3'-box-dependent processing. The Integrator complex is associated with
CC the C-terminal domain (CTD) of RNA polymerase II largest subunit
CC (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates
CC recruitment of cytoplasmic dynein to the nuclear envelope, probably as
CC component of the INT complex. {ECO:0000250|UniProtKB:Q8N201}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12 (By similarity). Interacts
CC with ESRRB, ESRRB is probably not a core component of the multiprotein
CC complex Integrator and this association is a bridge for the interaction
CC with the multiprotein complex Integrator; attracts the transcriptional
CC machinery (PubMed:26206133). {ECO:0000250|UniProtKB:Q8N201,
CC ECO:0000269|PubMed:26206133}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63266.1; Type=Miscellaneous discrepancy; Note=Could be due to alternative splicing but with non canonical splice junction.; Evidence={ECO:0000305};
CC Sequence=BAF03197.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB257854; BAF03197.1; ALT_INIT; mRNA.
DR EMBL; BC010333; AAH10333.1; -; mRNA.
DR EMBL; BC063266; AAH63266.1; ALT_SEQ; mRNA.
DR EMBL; AK003728; BAB22963.1; -; mRNA.
DR CCDS; CCDS57399.1; -.
DR RefSeq; NP_081024.3; NM_026748.2.
DR AlphaFoldDB; Q6P4S8; -.
DR SMR; Q6P4S8; -.
DR BioGRID; 212895; 17.
DR DIP; DIP-59891N; -.
DR IntAct; Q6P4S8; 2.
DR MINT; Q6P4S8; -.
DR STRING; 10090.ENSMUSP00000072406; -.
DR iPTMnet; Q6P4S8; -.
DR PhosphoSitePlus; Q6P4S8; -.
DR EPD; Q6P4S8; -.
DR jPOST; Q6P4S8; -.
DR MaxQB; Q6P4S8; -.
DR PaxDb; Q6P4S8; -.
DR PRIDE; Q6P4S8; -.
DR ProteomicsDB; 269489; -.
DR DNASU; 68510; -.
DR Ensembl; ENSMUST00000200393; ENSMUSP00000143789; ENSMUSG00000029547.
DR GeneID; 68510; -.
DR KEGG; mmu:68510; -.
DR CTD; 26173; -.
DR MGI; MGI:1915760; Ints1.
DR eggNOG; KOG4596; Eukaryota.
DR GeneTree; ENSGT00390000015743; -.
DR InParanoid; Q6P4S8; -.
DR OrthoDB; 357673at2759; -.
DR PhylomeDB; Q6P4S8; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 68510; 19 hits in 74 CRISPR screens.
DR ChiTaRS; Ints1; mouse.
DR PRO; PR:Q6P4S8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6P4S8; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032039; C:integrator complex; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0016180; P:snRNA processing; ISO:MGI.
DR GO; GO:0034474; P:U2 snRNA 3'-end processing; IMP:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022145; DUF3677.
DR InterPro; IPR038902; INTS1.
DR PANTHER; PTHR21224; PTHR21224; 1.
DR Pfam; PF12432; DUF3677; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2195
FT /note="Integrator complex subunit 1"
FT /id="PRO_0000236045"
FT TRANSMEM 1165..1185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N201"
FT MOD_RES 47
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N201"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N201"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N201"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N201"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N201"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 1680
FT /note="C -> R (in Ref. 1; BAF03197 and 2; AAH10333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2195 AA; 245168 MW; 47C1DEA4609197BE CRC64;
MNRAKPTTVR RPSAAAKPSG HPPPGDFIAL GSKGQASESK TTSTLLKPAP SGLPSERKRD
ASASLSGTSA LTGLTKRPKL SSTPPLSALG RLAEAAVAEK RAISPSIKEP SVVPIEVLPT
VLLDEIEAAE LEGNDDRIEG VLCGAVKQLK VTRAKPDSTL YLSLMYLAKI KPNIFATEGV
IEALCSLLRR DASVNFKAKG NSLVSVLACN LLMAAYEEDE NWPEIFVKVY IEDSLGERIW
VDSPHCRTFV DNIQTAFNTK MPPKSVLLQG EGARSGGELG AGSSPHPSLT EEEDSQTELL
IAEEKLSPEQ EGQLMPRPRY DELTESVEEY VLDMLRDQLN RRQPIDNVSR NLLRLLTATC
GYKEVRLLAV QRLEMWLQNP KLTRPAQDLL MSVCMNCNSH GSEDMDVISH LIKIRLKPKV
LLNHYMLCIR ELLNAHKDNL GTTIKFVIFN ELSNARNPNN MQILYTVLQH SSELAPKFLA
MVFQDLLTNK DDYLRASRAL LREIIKQTKH EINFQAFCLG LMQERKEPQY LEMEFKERFV
VHITDVLAVS MMLGITAQVK EAGVAWDKGE KRNLEVLRTF QNQIAAIQRD AVWWLHTVVP
SVSKLAPKDY VHCLHKVLFT EQPETYYKWD NWPPESDRNF FLRLCSEVPI LEDTLMRVLV
IGLSRELPLG PADAMELADH LVKRAAAVQA DDVEVLKVER IQLIDAVLNL CTYHHPENIQ
LPPGYQPPNL AISTLYWKAW PLLLVVAAFN PENIGLAAWE EYPTLKMLME MVMTNNYSYP
PCTLTDEETR TEMINRELQI SQREKQEILA FEGHLAAAST KQTITESSSL LLSQLTSLDP
QGPPRRPPPH ILDQVKALNQ SLRLGHLLCR SRNPDFLLHI IQRQASSQSM PWLADLVQSS
EGSLDVLPVQ CLCEFLLHDA ADSTASGEED DEGESREQKA KKRQRQQKQR QLLGRLQDLL
LGPKADEQTT CEVLDYFLRR LGSSQVASRV LAMKGLSLVL SEGGLRDKEE KEPPMEEDIG
ETDALQGYQW LLRDLPRLPL FDSVRTTTAL ALQQAIHMET DPQTISAYLI YLSQHTPVEE
QGPHSDLALD VARLVVERST IMAHLFSKPS CSTASDAVLS ALLSVFSRYV RRMRKSKEGE
EVYSWSESQD QVFLRWSSGE TATMHILVVH AMVILLTLGP PRSGDSEFSE LLDIWFPEKK
PLPTAFLVDT SEEALLLPDW LKLRMIRSEV PRLVDAALQD LEPQQLLLFV QSFGIPVSSM
SKLLQYLDQA VAQDPQTLEQ NIMDKNYMAH LVEVQHERGA SGGQTFHSLL TASLPPRRDS
TEAPKPESSP EPPPGQGRTR AGTQVPVLGP EDDLAGIFLQ IFPLSPDPRW QSSSPRPLAL
ALQQALGQEL ARVRQGNPEV PGITVRLLQA MTTLLSSPHG GTLALAMHHS HFLSCPLMRQ
LYQYQRAVPQ DTGFSSLFLK VLMQILQWLD SPAVEDGPLQ AQLKLFATRY SARHRISDVR
SGLLHLADAL SFHGDLEVAN STARAVIATL RSGEKCPVEP ELISKVLRGL IEVRSPHLEE
LLTALFSATT ETSCPSPASG PIVVVSSLLL QEKEELLGPS KQEVEGASTE AMRLGPASGL
LVDWLETLDP EVVCSCPDLQ WKLLFSRRKG KGHISAQVLS FRPYLLALLT HQASWSTLHC
CIRVLLGKSR EQRLDPSASL DFLWACIHVP RIWQGRDQRT PQKRREELVL HVQGPELLSL
VELILSEAET RSQDGDSAAR TLIQTRLPLL LSCCRSNDES IGKVTEHLTS CIQQWGDSVL
GQRCRDLLLQ LYLQRPEVRV PVPEVLLQSE GATSSSICKL DGLVHRFITL LADTSDSRSS
ESRVADANMA CRKLAVAHPV LLLRHLPMIA ALLHGRTHLN FQEFRQQNHL AFFLHVLGIL
ELLQPRVFQS EHQGALWDCL RSFIRLLLNY RKSSRHLAPF ISKFVQFIHK YVGCSAPAAV
AFLQKHAEPL HDLSFDNSDL VMLKSLLAGL SLPSRDGRTD QGLDEEGEDE RSAGSLPLVS
VSLSTPLTVA DVAPHMKRLS RGRAVEDVLE TLSDIDEMSR RRPEVLGFFS TNLQRLMSSA
EESCRNLAFS LALRSIQNNP SIAADFLPTF MYCLGSRDFE VVQTALRNLP EYTLLCQEHA
AVLLHRAFLV GVYGQIDTSA QISEALKILH MEAVM
