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INT12_BOVIN
ID   INT12_BOVIN             Reviewed;         462 AA.
AC   Q32LL5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Integrator complex subunit 12;
DE            Short=Int12;
DE   AltName: Full=PHD finger protein 22;
GN   Name=INTS12; Synonyms=PHF22;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; BC109520; AAI09521.1; -; mRNA.
DR   RefSeq; NP_001069221.1; NM_001075753.2.
DR   RefSeq; XP_005207666.1; XM_005207609.3.
DR   AlphaFoldDB; Q32LL5; -.
DR   SMR; Q32LL5; -.
DR   STRING; 9913.ENSBTAP00000044968; -.
DR   PaxDb; Q32LL5; -.
DR   PRIDE; Q32LL5; -.
DR   Ensembl; ENSBTAT00000047799; ENSBTAP00000044968; ENSBTAG00000033648.
DR   GeneID; 517489; -.
DR   KEGG; bta:517489; -.
DR   CTD; 57117; -.
DR   VEuPathDB; HostDB:ENSBTAG00000033648; -.
DR   VGNC; VGNC:30225; INTS12.
DR   eggNOG; KOG4323; Eukaryota.
DR   GeneTree; ENSGT00390000005218; -.
DR   HOGENOM; CLU_033336_0_0_1; -.
DR   InParanoid; Q32LL5; -.
DR   OMA; AKQDKRN; -.
DR   OrthoDB; 1631937at2759; -.
DR   TreeFam; TF106418; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000033648; Expressed in semen and 107 other tissues.
DR   GO; GO:0032039; C:integrator complex; IBA:GO_Central.
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   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   2: Evidence at transcript level;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..462
FT                   /note="Integrator complex subunit 12"
FT                   /id="PRO_0000259569"
FT   ZN_FING         159..215
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          39..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         128
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        254
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96CB8"
SQ   SEQUENCE   462 AA;  48557 MW;  0D0FB156EB92FD29 CRC64;
     MAAAVNLELD PIFLKALGFL HSKSKDSAEK LKTLLDESLA RGIDSSYRPS QKDVEPPKIS
     STKTVSVKQE PKTSSSLPSG NNNGKVLTTE KVKKEGEKRP ADKMKSDITE GADVPKKPRL
     EKPETRSSPI TVQTSKDLAM ADLSSFEETS ADDFAMEMGL ACVVCRQMTV ASGNQLVECQ
     ECHNLYHQDC HKPQVTDKEV TDPRLVWYCA RCTRQMKRMA QKTQKPPQKP APTVVSVAPA
     VKDPLVKKPE TKLKPETTFL AFKRSEVKAS TVVSGNSSST NVSSSATSGL IGWAAFAAKT
     TSAGPSTAKL SSAAQNNSGK PATSSANQKP VGLTGLATTS KGGIGSKIGS SNSTSPTVPL
     KPPPPLTLGK TGLSRSVSCD NVSKVGLPSP SSLVPGSSSQ LSGNGNSGTS GPSGSTTNKT
     ASEPSTSPSA SLKGPTSQES QLNAMKRLQM VKKKAAQKKL KK
 
 
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