INT12_RAT
ID INT12_RAT Reviewed; 461 AA.
AC Q68FR3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Integrator complex subunit 12;
DE Short=Int12;
DE AltName: Full=PHD finger protein 22;
GN Name=Ints12; Synonyms=Phf22;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC079404; AAH79404.1; -; mRNA.
DR RefSeq; NP_001007641.1; NM_001007640.1.
DR RefSeq; XP_006233383.1; XM_006233321.3.
DR AlphaFoldDB; Q68FR3; -.
DR SMR; Q68FR3; -.
DR STRING; 10116.ENSRNOP00000016066; -.
DR iPTMnet; Q68FR3; -.
DR PhosphoSitePlus; Q68FR3; -.
DR PaxDb; Q68FR3; -.
DR PRIDE; Q68FR3; -.
DR Ensembl; ENSRNOT00000016066; ENSRNOP00000016066; ENSRNOG00000011844.
DR GeneID; 295448; -.
DR KEGG; rno:295448; -.
DR CTD; 57117; -.
DR RGD; 1359136; Ints12.
DR eggNOG; KOG4323; Eukaryota.
DR GeneTree; ENSGT00390000005218; -.
DR HOGENOM; CLU_033336_0_0_1; -.
DR InParanoid; Q68FR3; -.
DR PhylomeDB; Q68FR3; -.
DR TreeFam; TF106418; -.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:Q68FR3; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0032039; C:integrator complex; ISO:RGD.
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; ISO:RGD.
DR CDD; cd15501; PHD_Int12; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039053; Int12.
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:SF4; PTHR13415:SF4; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 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_0000059316"
FT ZN_FING 158..214
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 45..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..83
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 300..356
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"
SQ SEQUENCE 461 AA; 48477 MW; 085B5CED148624BE CRC64;
MAATVNLELD PIFLKALGFL HSKSKDSAEK LKTLLDESLA RGIDASYRPA QKDVEPPKIS
STKSLSIKQE PKTSSSLPSG SSNGKVLAAE KLKKEAEKRP ADKMKDATEG VDVPKKPRLE
KPETRSSPIT VQTSKDLAMA DLSSFEETSA DDFAMEMGLA CVVCRQMTVA SGNQLVECQE
CHNLYHQDCH KPQVTDKEVN DPRLVWYCAR CTRQMKRMAQ KTQKPPQKPA PTVVSVAPTV
KDPLVKKPET KLKQETTFLA FKRTEVKPST VISGNSSSNN VSSSVTSGLT GWAAFAAKTS
SAGPSTAKLN STAQNSSGKP AASSASQKPV GLTGLATSSK GGIGSKIGSS NSTSPSVPLK
PLPPLTLGKT GLSRSVSCDN VSKVGLPSPS SLVPGGSSQL SGNGNSATAG PTGSITSKTT
SETSSSTSAS LKGPTSQESQ LNAMKRLQMV KKKAAQKKLK K
