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Protein

Integrator complex subunit 1

Gene

Ints1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

  • blastocyst growth Source: MGI
  • inner cell mass cell proliferation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • snRNA processing Source: MGI
  • U2 snRNA 3'-end processing Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Integrator complex subunit 1
Short name:
Int1
Gene namesi
Name:Ints1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1915760. Ints1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1165 – 118521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • integrator complex Source: MGI
  • membrane Source: MGI
  • nuclear membrane Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21952195Integrator complex subunit 1PRO_0000236045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471N6-acetyllysineBy similarity
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei926 – 9261PhosphoserineBy similarity
Modified residuei1320 – 13201PhosphoserineCombined sources
Modified residuei1328 – 13281PhosphoserineCombined sources
Modified residuei1329 – 13291PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6P4S8.
MaxQBiQ6P4S8.
PaxDbiQ6P4S8.
PRIDEiQ6P4S8.

PTM databases

iPTMnetiQ6P4S8.
PhosphoSiteiQ6P4S8.

Expressioni

Gene expression databases

BgeeiQ6P4S8.
CleanExiMM_INTS1.

Interactioni

Subunit structurei

Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, CPSF3L/INTS11 and INTS12.By similarity

Protein-protein interaction databases

BioGridi212895. 2 interactions.
DIPiDIP-59891N.
IntActiQ6P4S8. 2 interactions.
MINTiMINT-4122126.
STRINGi10090.ENSMUSP00000072406.

Structurei

3D structure databases

ProteinModelPortaliQ6P4S8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4596. Eukaryota.
ENOG410XTAB. LUCA.
HOGENOMiHOG000008530.
HOVERGENiHBG081799.
InParanoidiQ6P4S8.
KOiK13138.
PhylomeDBiQ6P4S8.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR022145. DUF3677.
[Graphical view]
PfamiPF12432. DUF3677. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.

Sequencei

Sequence statusi: Complete.

Q6P4S8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRAKPTTVR RPSAAAKPSG HPPPGDFIAL GSKGQASESK TTSTLLKPAP
60 70 80 90 100
SGLPSERKRD ASASLSGTSA LTGLTKRPKL SSTPPLSALG RLAEAAVAEK
110 120 130 140 150
RAISPSIKEP SVVPIEVLPT VLLDEIEAAE LEGNDDRIEG VLCGAVKQLK
160 170 180 190 200
VTRAKPDSTL YLSLMYLAKI KPNIFATEGV IEALCSLLRR DASVNFKAKG
210 220 230 240 250
NSLVSVLACN LLMAAYEEDE NWPEIFVKVY IEDSLGERIW VDSPHCRTFV
260 270 280 290 300
DNIQTAFNTK MPPKSVLLQG EGARSGGELG AGSSPHPSLT EEEDSQTELL
310 320 330 340 350
IAEEKLSPEQ EGQLMPRPRY DELTESVEEY VLDMLRDQLN RRQPIDNVSR
360 370 380 390 400
NLLRLLTATC GYKEVRLLAV QRLEMWLQNP KLTRPAQDLL MSVCMNCNSH
410 420 430 440 450
GSEDMDVISH LIKIRLKPKV LLNHYMLCIR ELLNAHKDNL GTTIKFVIFN
460 470 480 490 500
ELSNARNPNN MQILYTVLQH SSELAPKFLA MVFQDLLTNK DDYLRASRAL
510 520 530 540 550
LREIIKQTKH EINFQAFCLG LMQERKEPQY LEMEFKERFV VHITDVLAVS
560 570 580 590 600
MMLGITAQVK EAGVAWDKGE KRNLEVLRTF QNQIAAIQRD AVWWLHTVVP
610 620 630 640 650
SVSKLAPKDY VHCLHKVLFT EQPETYYKWD NWPPESDRNF FLRLCSEVPI
660 670 680 690 700
LEDTLMRVLV IGLSRELPLG PADAMELADH LVKRAAAVQA DDVEVLKVER
710 720 730 740 750
IQLIDAVLNL CTYHHPENIQ LPPGYQPPNL AISTLYWKAW PLLLVVAAFN
760 770 780 790 800
PENIGLAAWE EYPTLKMLME MVMTNNYSYP PCTLTDEETR TEMINRELQI
810 820 830 840 850
SQREKQEILA FEGHLAAAST KQTITESSSL LLSQLTSLDP QGPPRRPPPH
860 870 880 890 900
ILDQVKALNQ SLRLGHLLCR SRNPDFLLHI IQRQASSQSM PWLADLVQSS
910 920 930 940 950
EGSLDVLPVQ CLCEFLLHDA ADSTASGEED DEGESREQKA KKRQRQQKQR
960 970 980 990 1000
QLLGRLQDLL LGPKADEQTT CEVLDYFLRR LGSSQVASRV LAMKGLSLVL
1010 1020 1030 1040 1050
SEGGLRDKEE KEPPMEEDIG ETDALQGYQW LLRDLPRLPL FDSVRTTTAL
1060 1070 1080 1090 1100
ALQQAIHMET DPQTISAYLI YLSQHTPVEE QGPHSDLALD VARLVVERST
1110 1120 1130 1140 1150
IMAHLFSKPS CSTASDAVLS ALLSVFSRYV RRMRKSKEGE EVYSWSESQD
1160 1170 1180 1190 1200
QVFLRWSSGE TATMHILVVH AMVILLTLGP PRSGDSEFSE LLDIWFPEKK
1210 1220 1230 1240 1250
PLPTAFLVDT SEEALLLPDW LKLRMIRSEV PRLVDAALQD LEPQQLLLFV
1260 1270 1280 1290 1300
QSFGIPVSSM SKLLQYLDQA VAQDPQTLEQ NIMDKNYMAH LVEVQHERGA
1310 1320 1330 1340 1350
SGGQTFHSLL TASLPPRRDS TEAPKPESSP EPPPGQGRTR AGTQVPVLGP
1360 1370 1380 1390 1400
EDDLAGIFLQ IFPLSPDPRW QSSSPRPLAL ALQQALGQEL ARVRQGNPEV
1410 1420 1430 1440 1450
PGITVRLLQA MTTLLSSPHG GTLALAMHHS HFLSCPLMRQ LYQYQRAVPQ
1460 1470 1480 1490 1500
DTGFSSLFLK VLMQILQWLD SPAVEDGPLQ AQLKLFATRY SARHRISDVR
1510 1520 1530 1540 1550
SGLLHLADAL SFHGDLEVAN STARAVIATL RSGEKCPVEP ELISKVLRGL
1560 1570 1580 1590 1600
IEVRSPHLEE LLTALFSATT ETSCPSPASG PIVVVSSLLL QEKEELLGPS
1610 1620 1630 1640 1650
KQEVEGASTE AMRLGPASGL LVDWLETLDP EVVCSCPDLQ WKLLFSRRKG
1660 1670 1680 1690 1700
KGHISAQVLS FRPYLLALLT HQASWSTLHC CIRVLLGKSR EQRLDPSASL
1710 1720 1730 1740 1750
DFLWACIHVP RIWQGRDQRT PQKRREELVL HVQGPELLSL VELILSEAET
1760 1770 1780 1790 1800
RSQDGDSAAR TLIQTRLPLL LSCCRSNDES IGKVTEHLTS CIQQWGDSVL
1810 1820 1830 1840 1850
GQRCRDLLLQ LYLQRPEVRV PVPEVLLQSE GATSSSICKL DGLVHRFITL
1860 1870 1880 1890 1900
LADTSDSRSS ESRVADANMA CRKLAVAHPV LLLRHLPMIA ALLHGRTHLN
1910 1920 1930 1940 1950
FQEFRQQNHL AFFLHVLGIL ELLQPRVFQS EHQGALWDCL RSFIRLLLNY
1960 1970 1980 1990 2000
RKSSRHLAPF ISKFVQFIHK YVGCSAPAAV AFLQKHAEPL HDLSFDNSDL
2010 2020 2030 2040 2050
VMLKSLLAGL SLPSRDGRTD QGLDEEGEDE RSAGSLPLVS VSLSTPLTVA
2060 2070 2080 2090 2100
DVAPHMKRLS RGRAVEDVLE TLSDIDEMSR RRPEVLGFFS TNLQRLMSSA
2110 2120 2130 2140 2150
EESCRNLAFS LALRSIQNNP SIAADFLPTF MYCLGSRDFE VVQTALRNLP
2160 2170 2180 2190
EYTLLCQEHA AVLLHRAFLV GVYGQIDTSA QISEALKILH MEAVM
Length:2,195
Mass (Da):245,168
Last modified:January 15, 2008 - v2
Checksum:i47C1DEA4609197BE
GO

Sequence cautioni

The sequence AAH63266.1 differs from that shown.Could be due to alternative splicing but with non canonical splice junction.Curated
The sequence BAF03197.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1680 – 16801C → R in BAF03197 (Ref. 1) Curated
Sequence conflicti1680 – 16801C → R in AAH10333 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB257854 mRNA. Translation: BAF03197.1. Different initiation.
BC010333 mRNA. Translation: AAH10333.1.
BC063266 mRNA. Translation: AAH63266.1. Sequence problems.
AK003728 mRNA. Translation: BAB22963.1.
RefSeqiNP_081024.3. NM_026748.2.
UniGeneiMm.292942.

Genome annotation databases

GeneIDi68510.
KEGGimmu:68510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB257854 mRNA. Translation: BAF03197.1. Different initiation.
BC010333 mRNA. Translation: AAH10333.1.
BC063266 mRNA. Translation: AAH63266.1. Sequence problems.
AK003728 mRNA. Translation: BAB22963.1.
RefSeqiNP_081024.3. NM_026748.2.
UniGeneiMm.292942.

3D structure databases

ProteinModelPortaliQ6P4S8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212895. 2 interactions.
DIPiDIP-59891N.
IntActiQ6P4S8. 2 interactions.
MINTiMINT-4122126.
STRINGi10090.ENSMUSP00000072406.

PTM databases

iPTMnetiQ6P4S8.
PhosphoSiteiQ6P4S8.

Proteomic databases

EPDiQ6P4S8.
MaxQBiQ6P4S8.
PaxDbiQ6P4S8.
PRIDEiQ6P4S8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi68510.
KEGGimmu:68510.

Organism-specific databases

CTDi26173.
MGIiMGI:1915760. Ints1.

Phylogenomic databases

eggNOGiKOG4596. Eukaryota.
ENOG410XTAB. LUCA.
HOGENOMiHOG000008530.
HOVERGENiHBG081799.
InParanoidiQ6P4S8.
KOiK13138.
PhylomeDBiQ6P4S8.

Miscellaneous databases

ChiTaRSiInts1. mouse.
NextBioi327330.
PROiQ6P4S8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P4S8.
CleanExiMM_INTS1.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR022145. DUF3677.
[Graphical view]
PfamiPF12432. DUF3677. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
ProtoNetiSearch...

Publicationsi

  1. The German cDNA consortium
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Mammary gland.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2034-2195.
    Strain: C57BL/6J.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320; SER-1328 AND SER-1329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiINT1_MOUSE
AccessioniPrimary (citable) accession number: Q6P4S8
Secondary accession number(s): Q0KK58
, Q80UQ7, Q91Z01, Q9CTF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 15, 2008
Last modified: March 16, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.