ID   INT12_PONAB             Reviewed;         462 AA.
AC   Q5RCV7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Integrator complex subunit 12;
DE            Short=Int12;
DE   AltName: Full=PHD finger protein 22;
GN   Name=INTS12; Synonyms=PHF22;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR858161; CAH90400.1; -; mRNA.
DR   RefSeq; NP_001125197.1; NM_001131725.2.
DR   AlphaFoldDB; Q5RCV7; -.
DR   SMR; Q5RCV7; -.
DR   STRING; 9601.ENSPPYP00000016727; -.
DR   GeneID; 100172088; -.
DR   KEGG; pon:100172088; -.
DR   CTD; 57117; -.
DR   eggNOG; KOG4323; Eukaryota.
DR   InParanoid; Q5RCV7; -.
DR   OrthoDB; 1631937at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016180; P:snRNA processing; IEA:InterPro.
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_0000059315"
FT   ZN_FING         159..215
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          42..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..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..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..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;  48802 MW;  4ED0953F4EF2E150 CRC64;
     MAATVNLELD PIFLKALGFL HSKSKDSAEK LKALLDESLA RGIDSSYRPS QKDVEPPKIS
     STKNISIKQE PKISSSLPSG NNNGKVLTTE KVKKEAEKRP ADKMKSDITE GVDIPKKPRL
     EKPETQSSPI TVQSSKDLPM ADLSSFEETS ADDFAMEMGL ACVVCRQMMV ASGNQLVECQ
     ECHNLYHRDC HKPQVTDKEA NDPRLVWYCA RCTRQMKRMA QKTQKPPQKP APAVVSVTPA
     VKDPLVKKPE TKLKQETTFL AFKRTEVKTS TVISGNSSSA SISSSVTSGL TGWAAFAAKT
     SSAGPSTAKL SSTTQNNTGK PATSSANQKP VGLTGLATSS KGGIGSKIGS NNSTTPTVPL
     KPPPPLTLGK TGLSRSVSCD NVSKVGLPSP SSLVPGSSSQ LSGNGNSGTP GPSGSTASKT
     TSESSSSPSA SLKGPTSQES QLNAMKRLQM VKKKAAQKKL KK