INT2_HUMAN
ID INT2_HUMAN Reviewed; 1204 AA.
AC Q9H0H0; Q9ULD3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Integrator complex subunit 2;
DE Short=Int2;
GN Name=INTS2; Synonyms=KIAA1287;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-768.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-768.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-768.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP IDENTIFICATION IN THE INTEGRATOR COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND VARIANT HIS-768.
RX PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA Shiekhattar R.;
RT "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT associates with the C-terminal repeat of RNA polymerase II.";
RL Cell 123:265-276(2005).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
RA Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
RA Reversade B., Wagner E.J., Lee L.A.;
RT "Nuclear-localized Asunder regulates cytoplasmic dynein localization via
RT its role in the integrator complex.";
RL Mol. Biol. Cell 24:2954-2965(2013).
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 (Probable).
CC Mediates recruitment of cytoplasmic dynein to the nuclear envelope,
CC probably as component of the INT complex (PubMed:23904267).
CC {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
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.
CC {ECO:0000269|PubMed:16239144}.
CC -!- INTERACTION:
CC Q9H0H0; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-8471507, EBI-10961624;
CC Q9H0H0; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-8471507, EBI-745369;
CC Q9H0H0; O43639: NCK2; NbExp=3; IntAct=EBI-8471507, EBI-713635;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:16239144};
CC Single-pass membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:23904267}.
CC -!- SIMILARITY: Belongs to the Integrator subunit 2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC Orthologous sequences (mouse and chicken) have shorter N-terminus.
CC {ECO:0000305}.
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DR EMBL; AB033113; BAA86601.1; -; mRNA.
DR EMBL; AL136800; CAB66734.1; -; mRNA.
DR EMBL; CR533582; CAG38656.1; -; mRNA.
DR EMBL; AC060798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK005721; DAA05721.1; -; mRNA.
DR CCDS; CCDS45750.1; -.
DR RefSeq; NP_001317346.1; NM_001330417.1.
DR RefSeq; NP_065799.1; NM_020748.2.
DR PDB; 7CUN; EM; 3.50 A; B=1-1204.
DR PDB; 7PKS; EM; 3.60 A; b=1-1204.
DR PDBsum; 7CUN; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q9H0H0; -.
DR SMR; Q9H0H0; -.
DR BioGRID; 121572; 112.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q9H0H0; -.
DR DIP; DIP-48477N; -.
DR IntAct; Q9H0H0; 25.
DR MINT; Q9H0H0; -.
DR STRING; 9606.ENSP00000414237; -.
DR iPTMnet; Q9H0H0; -.
DR PhosphoSitePlus; Q9H0H0; -.
DR BioMuta; INTS2; -.
DR DMDM; 296434542; -.
DR EPD; Q9H0H0; -.
DR jPOST; Q9H0H0; -.
DR MassIVE; Q9H0H0; -.
DR MaxQB; Q9H0H0; -.
DR PaxDb; Q9H0H0; -.
DR PeptideAtlas; Q9H0H0; -.
DR PRIDE; Q9H0H0; -.
DR ProteomicsDB; 80277; -.
DR Antibodypedia; 57004; 73 antibodies from 19 providers.
DR DNASU; 57508; -.
DR Ensembl; ENST00000444766.7; ENSP00000414237.3; ENSG00000108506.13.
DR Ensembl; ENST00000617492.4; ENSP00000482710.1; ENSG00000108506.13.
DR GeneID; 57508; -.
DR KEGG; hsa:57508; -.
DR UCSC; uc002izn.4; human.
DR CTD; 57508; -.
DR DisGeNET; 57508; -.
DR GeneCards; INTS2; -.
DR HGNC; HGNC:29241; INTS2.
DR HPA; ENSG00000108506; Low tissue specificity.
DR MIM; 611346; gene.
DR neXtProt; NX_Q9H0H0; -.
DR OpenTargets; ENSG00000108506; -.
DR PharmGKB; PA142671605; -.
DR VEuPathDB; HostDB:ENSG00000108506; -.
DR eggNOG; ENOG502QSP2; Eukaryota.
DR GeneTree; ENSGT00390000011888; -.
DR InParanoid; Q9H0H0; -.
DR OrthoDB; 173270at2759; -.
DR PhylomeDB; Q9H0H0; -.
DR TreeFam; TF324737; -.
DR PathwayCommons; Q9H0H0; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q9H0H0; -.
DR SIGNOR; Q9H0H0; -.
DR BioGRID-ORCS; 57508; 651 hits in 1076 CRISPR screens.
DR ChiTaRS; INTS2; human.
DR GenomeRNAi; 57508; -.
DR Pharos; Q9H0H0; Tdark.
DR PRO; PR:Q9H0H0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H0H0; protein.
DR Bgee; ENSG00000108506; Expressed in oviduct epithelium and 179 other tissues.
DR ExpressionAtlas; Q9H0H0; baseline and differential.
DR Genevisible; Q9H0H0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL.
DR InterPro; IPR026236; Int2_metazoa.
DR InterPro; IPR029321; INTS2.
DR PANTHER; PTHR28608; PTHR28608; 1.
DR Pfam; PF14750; INTS2; 1.
DR PRINTS; PR02105; INTSUBUNIT2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1204
FT /note="Integrator complex subunit 2"
FT /id="PRO_0000236099"
FT TRANSMEM 428..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 768
FT /note="N -> H (in dbSNP:rs606072)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:16239144,
FT ECO:0000269|Ref.3"
FT /id="VAR_049628"
FT CONFLICT 1
FT /note="M -> GWRVDL (in Ref. 1; BAA86601)"
FT /evidence="ECO:0000305"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 166..185
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 265..279
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 351..365
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 405..414
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 423..438
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 441..444
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 446..469
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 516..522
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 531..536
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 553..563
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 574..580
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 592..601
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 616..621
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 645..664
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 689..697
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 704..717
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 724..726
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 739..743
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 744..751
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 754..761
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 770..777
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 778..780
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 787..793
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 797..800
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 807..819
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 821..824
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 825..835
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 851..854
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 857..861
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 867..869
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 871..895
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 924..945
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 986..988
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 989..1007
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1009..1018
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1022..1024
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1025..1029
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1033..1041
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1042..1046
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1051..1067
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1071..1086
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 1088..1091
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1093..1100
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1101..1103
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1104..1113
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1115..1117
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1118..1136
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1147..1150
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 1181..1201
FT /evidence="ECO:0007829|PDB:7CUN"
SQ SEQUENCE 1204 AA; 134323 MW; E4E160F25E1ACB4B CRC64;
MKDQQTVIMT ECTSLQFVSP FAFEAMQKVD VVCLASLSDP ELRLLLPCLV RMALCAPADQ
SQSWAQDKKL ILRLLSGVEA VNSIVALLSV DFHALEQDAS KEQQLRHKLG GGSGESILVS
QLQHGLTLEF EHSDSPRRLR LVLSELLAIM NKVSESNGEF FFKSSELFES PVYLEEAADV
LCILQAELPS LLPIVDVAEA LLHVRNGAWF LCLLVANVPD SFNEVCRGLI KNGERQDEES
LGGRRRTDAL RFLCKMNPSQ ALKVRGMVVE ECHLPGLGVA LTLDHTKNEA CEDGVSDLVC
FVSGLLLGTN AKVRTWFGTF IRNGQQRKRE TSSSVLWQMR RQLLLELMGI LPTVRSTRIV
EEADVDMEPN VSVYSGLKEE HVVKASALLR LYCALMGIAG LKPTEEEAEQ LLQLMTSRPP
ATPAGVRFVS LSFCMLLAFS TLVSTPEQEQ LMVVWLSWMI KEEAYFESTS GVSASFGEML
LLVAMYFHSN QLSAIIDLVC STLGMKIVIK PSSLSRMKTI FTQEIFTEQV VTAHAVRVPV
TSNLSANITG FLPIHCIYQL LRSRSFTKHK VSIKDWIYRQ LCETSTPLHP QLLPLIDVYI
NSILTPASKS NPEATNQPVT EQEILNIFQG VIGGDNIRLN QRFSITAQLL VLYYILSYEE
ALLANTKTLA AMQRKPKSYS SSLMDQIPIK FLIRQAQGLQ QELGGLHSAL LRLLATNYPH
LCIVDDWICE EEITGTDALL RRMLLTNNAK NHSPKQLQEA FSAVPVNNTQ VMQIIEHLTL
LSASELIPYA EVLTSNMSQL LNSGVPRRIL QTVNKLWMVL NTVMPRRLWV MTVNALQPSI
KFVRQQKYTQ NDLMIDPLIV LRCDQRVHRC PPLMDITLHM LNGYLLASKA YLSAHLKETE
QDRPSQNNTI GLVGQTDAPE VTREELKNAL LAAQDSAAVQ ILLEICLPTE EEKANGVNPD
SLLRNVQSVI TTSAPNKGME EGEDNLLCNL REVQCLICCL LHQMYIADPN IAKLVHFQGY
PCELLPLTVA GIPSMHICLD FIPELIAQPE LEKQIFAIQL LSHLCIQYAL PKSLSVARLA
VNVMGTLLTV LTQAKRYAFF MPTLPSLVSF CRAFPPLYED IMSLLIQIGQ VCASDVATQT
RDIDPIITRL QQIKEKPSGW SQICKDSSYK NGSRDTGSMD PDVQLCHCIE RTVIEIINMS
VSGI
