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INT12_MACFA
ID   INT12_MACFA             Reviewed;         462 AA.
AC   Q8WNV2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-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; ORFNames=QtsA-10963;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
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; AB064993; BAB83535.1; -; mRNA.
DR   RefSeq; NP_001274215.1; NM_001287286.1.
DR   RefSeq; XP_005555674.1; XM_005555617.2.
DR   RefSeq; XP_015306042.1; XM_015450556.1.
DR   RefSeq; XP_015306043.1; XM_015450557.1.
DR   AlphaFoldDB; Q8WNV2; -.
DR   SMR; Q8WNV2; -.
DR   STRING; 9541.XP_005555672.1; -.
DR   GeneID; 102130496; -.
DR   KEGG; mcf:102130496; -.
DR   CTD; 57117; -.
DR   VEuPathDB; HostDB:ENSMFAG00000042815; -.
DR   eggNOG; KOG4323; Eukaryota.
DR   OMA; AKQDKRN; -.
DR   Proteomes; UP000233100; Chromosome 5.
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_0000059313"
FT   ZN_FING         159..215
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          42..129
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;  48810 MW;  0ACFFA3FF5AA93C7 CRC64;
     MAATVNLELD PIFLKALGFL HSKSKDSAEK LKALLDESLA RGIDSSYRPS QKDVEPPKIS
     STKNISIKQE PKISSSLPSG NNNGKVLTTE KVKKEAEKRP ADKMKSDITE GVDIPKKPRL
     EKPETQSSPI TVQTSKDLAM ADLSSFEETS ADDFAMEMGL ACVVCRQMMV ASGNQLVECQ
     ECHNLYHRDC HKPQVTDKEA NDPRLVWYCA RCTRQMKRMA QKTQKPPQKP APAVVSVTPA
     VKDPLVKKPE TKLKQETTFL AFKRTEVKTS TVISGNSSSA SVSSSVTSGL TGWAAFAAKT
     SSAGPSTAKL SSTTQNSTGK PATSSANQKP VGLTGLATSS KGGIGSKIGS NNSTTPTVPL
     KPPPPLTLGK TGLSRSVSCD NVSKVGLPSP SSLVPGNSSQ LSGNGNTGTS GPSGSTTSKT
     TSESSSSPSA SLKGPTSQES QLNAMKRLQM VKKKAAQKKL KK
 
 
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