ID   INT12_MOUSE             Reviewed;         461 AA.
AC   Q9D168; Q3U2Q5; Q921U2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Integrator complex subunit 12;
DE            Short=Int12;
DE   AltName: Full=PHD finger protein 22;
GN   Name=Ints12; Synonyms=Phf22;
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=C57BL/6J, and NOD; TISSUE=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, Mammary gland, and Mammary tumor;
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   STRUCTURE BY NMR OF 150-224.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of PHD domain in protein NP_082203.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Component of the Integrator complex, a complex involved in
CC       the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-
CC       box-dependent processing. The Integrator complex is associated with the
CC       C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A)
CC       and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of
CC       cytoplasmic dynein to the nuclear envelope, probably as component of
CC       the INT complex. {ECO:0000250|UniProtKB:Q96CB8}.
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:0000250|UniProtKB:Q96CB8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96CB8}.
CC   -!- SIMILARITY: Belongs to the Integrator subunit 12 family. {ECO:0000305}.
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DR   EMBL; AK003874; BAB23052.1; -; mRNA.
DR   EMBL; AK155162; BAE33085.1; -; mRNA.
DR   EMBL; BC010657; AAH10657.1; -; mRNA.
DR   EMBL; BC023801; AAH23801.1; -; mRNA.
DR   EMBL; BC046996; AAH46996.1; -; mRNA.
DR   CCDS; CCDS17848.1; -.
DR   RefSeq; NP_082203.1; NM_027927.4.
DR   PDB; 1WEV; NMR; -; A=150-224.
DR   PDBsum; 1WEV; -.
DR   AlphaFoldDB; Q9D168; -.
DR   SMR; Q9D168; -.
DR   STRING; 10090.ENSMUSP00000029650; -.
DR   iPTMnet; Q9D168; -.
DR   PhosphoSitePlus; Q9D168; -.
DR   SwissPalm; Q9D168; -.
DR   EPD; Q9D168; -.
DR   jPOST; Q9D168; -.
DR   MaxQB; Q9D168; -.
DR   PaxDb; 10090-ENSMUSP00000029650; -.
DR   PeptideAtlas; Q9D168; -.
DR   ProteomicsDB; 268974; -.
DR   Pumba; Q9D168; -.
DR   Antibodypedia; 26162; 84 antibodies from 22 providers.
DR   Ensembl; ENSMUST00000029650.9; ENSMUSP00000029650.9; ENSMUSG00000028016.10.
DR   GeneID; 71793; -.
DR   KEGG; mmu:71793; -.
DR   UCSC; uc008rkj.1; mouse.
DR   AGR; MGI:1919043; -.
DR   CTD; 57117; -.
DR   MGI; MGI:1919043; Ints12.
DR   VEuPathDB; HostDB:ENSMUSG00000028016; -.
DR   eggNOG; KOG4323; Eukaryota.
DR   GeneTree; ENSGT00390000005218; -.
DR   HOGENOM; CLU_033336_0_0_1; -.
DR   InParanoid; Q9D168; -.
DR   OMA; QPMATDE; -.
DR   OrthoDB; 2882290at2759; -.
DR   PhylomeDB; Q9D168; -.
DR   TreeFam; TF106418; -.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   BioGRID-ORCS; 71793; 8 hits in 66 CRISPR screens.
DR   ChiTaRS; Ints12; mouse.
DR   EvolutionaryTrace; Q9D168; -.
DR   PRO; PR:Q9D168; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9D168; Protein.
DR   Bgee; ENSMUSG00000028016; Expressed in secondary oocyte and 250 other cell types or tissues.
DR   GO; GO:0032039; C:integrator complex; ISS:HGNC-UCL.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0016180; P:snRNA processing; ISS:HGNC-UCL.
DR   CDD; cd15501; PHD_Int12; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039054; Int12_PHD.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13415:SF2; INTEGRATOR COMPLEX SUBUNIT 12; 1.
DR   PANTHER; PTHR13415; NUCLEAR FACTOR-RELATED; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   Genevisible; Q9D168; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..461
FT                   /note="Integrator complex subunit 12"
FT                   /id="PRO_0000059314"
FT   ZN_FING         158..214
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          42..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96CB8"
FT   CROSSLNK        68
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96CB8"
FT   CROSSLNK        253
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96CB8"
FT   HELIX           154..157
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   TURN            187..189
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   HELIX           196..200
FT                   /evidence="ECO:0007829|PDB:1WEV"
FT   HELIX           209..215
FT                   /evidence="ECO:0007829|PDB:1WEV"
SQ   SEQUENCE   461 AA;  48568 MW;  9230385FBD4A9425 CRC64;
     MAATVNLELD PIFLKALGFL HSKSKDSAEK LKALLDESLA RGIDSSYRPT QKDVEPPKIS
     STKSLSIKQE PKTSSSLPSG SSNGKVLTAE KIKKEAEKRP ADKMKDVTEG IDVPKKPRLE
     KPETRSSPIT VQTSKDLSMA DLSSFEETSA DDFAMEMGLA CVVCRQMTVA SGNQLVECQE
     CHNLYHQDCH KPQVTDKEVN DPRLVWYCAR CTRQMKRMAQ KTQKPPQKPA PTVVSVTPTV
     KDPLVKKPET KLKQETTFLA FKRTEVKPST VISGNSSSNN VSSSVTSGLT GWAAFAAKTS
     SAGPSTAKLN SAAQNSSGKP AASSSNQKPV GLTGLATSSK GGIGSKIGSG NSTSPSVPLK
     PLPPLTLGKT GLSRSVSCDN VSKVGLPSPS SLVPGGSSQL SGNGNSATTG PSGSTTSKAT
     SETSSSTSAS LKGPTSQESQ LNAMKRLQMV KKKAAQKKLK K
//