INT5_HUMAN
ID INT5_HUMAN Reviewed; 1019 AA.
AC Q6P9B9; Q8N6W5; Q9C0G5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Integrator complex subunit 5;
DE Short=Int5;
GN Name=INTS5; Synonyms=KIAA1698;
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].
RC TISSUE=Brain, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-1019.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE INTEGRATOR
RP COMPLEX.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
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 Q6P9B9; Q75QN2: INTS8; NbExp=3; IntAct=EBI-7600112, EBI-2340089;
CC Q6P9B9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-7600112, EBI-10171774;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:23904267}.
CC Cytoplasm {ECO:0000269|PubMed:23904267}.
CC -!- SIMILARITY: Belongs to the Integrator subunit 5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28025.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC028025; AAH28025.1; ALT_INIT; mRNA.
DR EMBL; BC060841; AAH60841.1; -; mRNA.
DR EMBL; AB051485; BAB21789.1; -; mRNA.
DR EMBL; BK005724; DAA05724.1; -; mRNA.
DR CCDS; CCDS8027.1; -.
DR RefSeq; NP_085131.1; NM_030628.1.
DR PDB; 7CUN; EM; 3.50 A; E=1-1019.
DR PDB; 7PKS; EM; 3.60 A; e=1-1019.
DR PDBsum; 7CUN; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q6P9B9; -.
DR SMR; Q6P9B9; -.
DR BioGRID; 123312; 178.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q6P9B9; -.
DR IntAct; Q6P9B9; 32.
DR MINT; Q6P9B9; -.
DR STRING; 9606.ENSP00000327889; -.
DR iPTMnet; Q6P9B9; -.
DR PhosphoSitePlus; Q6P9B9; -.
DR BioMuta; INTS5; -.
DR DMDM; 74737528; -.
DR EPD; Q6P9B9; -.
DR jPOST; Q6P9B9; -.
DR MassIVE; Q6P9B9; -.
DR MaxQB; Q6P9B9; -.
DR PaxDb; Q6P9B9; -.
DR PeptideAtlas; Q6P9B9; -.
DR PRIDE; Q6P9B9; -.
DR ProteomicsDB; 67036; -.
DR Antibodypedia; 28628; 100 antibodies from 21 providers.
DR DNASU; 80789; -.
DR Ensembl; ENST00000330574.2; ENSP00000327889.2; ENSG00000185085.2.
DR GeneID; 80789; -.
DR KEGG; hsa:80789; -.
DR MANE-Select; ENST00000330574.2; ENSP00000327889.2; NM_030628.2; NP_085131.1.
DR UCSC; uc001nud.3; human.
DR CTD; 80789; -.
DR DisGeNET; 80789; -.
DR GeneCards; INTS5; -.
DR HGNC; HGNC:29352; INTS5.
DR HPA; ENSG00000185085; Low tissue specificity.
DR MIM; 611349; gene.
DR neXtProt; NX_Q6P9B9; -.
DR OpenTargets; ENSG00000185085; -.
DR PharmGKB; PA142671596; -.
DR VEuPathDB; HostDB:ENSG00000185085; -.
DR eggNOG; ENOG502QPVK; Eukaryota.
DR GeneTree; ENSGT00390000008374; -.
DR HOGENOM; CLU_013732_0_0_1; -.
DR InParanoid; Q6P9B9; -.
DR OMA; KDFCVHS; -.
DR OrthoDB; 108880at2759; -.
DR PhylomeDB; Q6P9B9; -.
DR TreeFam; TF323720; -.
DR PathwayCommons; Q6P9B9; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q6P9B9; -.
DR SIGNOR; Q6P9B9; -.
DR BioGRID-ORCS; 80789; 578 hits in 1083 CRISPR screens.
DR ChiTaRS; INTS5; human.
DR GenomeRNAi; 80789; -.
DR Pharos; Q6P9B9; Tbio.
DR PRO; PR:Q6P9B9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6P9B9; protein.
DR Bgee; ENSG00000185085; Expressed in stromal cell of endometrium and 109 other tissues.
DR Genevisible; Q6P9B9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; IDA:HPA.
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; IPR040316; INTS5.
DR InterPro; IPR029444; INTS5_C.
DR InterPro; IPR029445; INTS5_N.
DR PANTHER; PTHR31697; PTHR31697; 1.
DR Pfam; PF14838; INTS5_C; 1.
DR Pfam; PF14837; INTS5_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1019
FT /note="Integrator complex subunit 5"
FT /id="PRO_0000259541"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 294..314
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 384..392
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 440..458
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 472..477
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 495..509
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 515..524
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 529..542
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 550..562
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 568..586
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 591..594
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 599..603
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 607..610
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 619..629
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 641..661
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 668..678
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 682..695
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 698..701
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 703..706
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 733..737
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 773..787
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 806..820
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 835..838
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 841..853
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 856..864
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 868..870
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 871..873
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 875..890
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 897..899
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 901..916
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 917..919
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 922..930
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 936..952
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 964..967
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 982..994
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 996..999
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 1001..1005
FT /evidence="ECO:0007829|PDB:7CUN"
SQ SEQUENCE 1019 AA; 107995 MW; DD4E3B0E2A60F9E7 CRC64;
MSALCDPPGA PGPPGPAPAT HGPAPLSAQE LSQEIKAFLT GVDPILGHQL SAREHARCGL
LLLRSLPPAR AAVLDHLRGV FDESVRAHLA ALDETPVAGP PHLRPPPPSH VPAGGPGLED
VVQEVQQVLS EFIRANPKAW APVISAWSID LMGQLSSTYS GQHQRVPHAT GALNELLQLW
MGCRATRTLM DIYVQCLSAL IGSCPDACVD ALLDTSVQHS PHFDWVVAHI GSSFPGTIIS
RVLSCGLKDF CVHGGAGGGA GSSGGSSSQT PSTDPFPGSP AIPAEKRVPK IASVVGILGH
LASRHGDSIR RELLRMFHDS LAGGSGGRSG DPSLQATVPF LLQLAVMSPA LLGTVSGELV
DCLKPPAVLS QLQQHLQGFP REELDNMLNL AVHLVSQASG AGAYRLLQFL VDTAMPASVI
TTQGLAVPDT VREACDRLIQ LLLLHLQKLV HHRGGSPGEG VLGPPPPPRL VPFLDALKNH
VGELCGETLR LERKRFLWQH QLLGLLSVYT RPSCGPEALG HLLSRARSPE ELSLATQLYA
GLVVSLSGLL PLAFRSCLAR VHAGTLQPPF TARFLRNLAL LVGWEQQGGE GPAALGAHFG
ESASAHLSDL APLLLHPEEE VAEAAASLLA ICPFPSEALS PSQLLGLVRA GVHRFFASLR
LHGPPGVASA CQLLTRLSQT SPAGLKAVLQ LLVEGALHRG NTELFGGQVD GDNETLSVVS
ASLASASLLD TNRRHTAAVP GPGGIWSVFH AGVIGRGLKP PKFVQSRNQQ EVIYNTQSLL
SLLVHCCSAP GGTECGECWG APILSPEAAK AVAVTLVESV CPDAAGAELA WPPEEHARAT
VERDLRIGRR FREQPLLFEL LKLVAAAPPA LCYCSVLLRG LLAALLGHWE ASRHPDTTHS
PWHLEASCTL VAVMAEGSLL PPALGNMHEV FSQLAPFEVR LLLLSVWGFL REHGPLPQKF
IFQSERGRFI RDFSREGGGE GGPHLAVLHS VLHRNIDRLG LFSGRFQAPS PSTLLRQGT
