ID A0A2K5HAJ3_COLAP Unreviewed; 840 AA.
AC A0A2K5HAJ3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=SP140 nuclear body protein {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000001356.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000001356.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_011807362.1; XM_011951972.1.
DR AlphaFoldDB; A0A2K5HAJ3; -.
DR Ensembl; ENSCANT00000005542.1; ENSCANP00000001356.1; ENSCANG00000004704.1.
DR GeneID; 105518824; -.
DR CTD; 11262; -.
DR OrthoDB; 38708at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05501; Bromo_SP100C_like; 1.
DR CDD; cd15626; PHD_SP110_140; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.10.390.10; SAND domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR004865; HSR_dom.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR043563; Sp110/Sp140/Sp140L-like.
DR InterPro; IPR030411; Sp140_Bromo.
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; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1.
DR PANTHER; PTHR46386:SF8; NUCLEAR BODY PROTEIN SP140; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63763; SAND domain-like; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 22..138
FT /note="HSR"
FT /evidence="ECO:0000259|PROSITE:PS51414"
FT DOMAIN 553..634
FT /note="SAND"
FT /evidence="ECO:0000259|PROSITE:PS50864"
FT DOMAIN 663..709
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 768..802
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 179..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 95362 MW; E057F7BA465EDA42 CRC64;
MAQRGQQGQM ASGDSNLNFR MVTDIQNAED QNLQEQVFPE PIFRFFREHK VEIASAITRP
FPFLMGLRDR SFISEQMYEH FQEAFRNLVP VTRVMYCVLS ELEKTFGWSH LEALFSRINL
MAYPDLNEIY RSFQNVCYEH PPLQMNNVIE SEERPRLLPD GKQENSNASH EMGDVAVPQE
ALSSSPKCEP GFSSESCEQL ALPNADGGDT EDAPSLLPGG GVSCELAIQT DEGELDEMPT
LLPYDTEVLE SNRMTDAART YSTAPGKKEG DEEGRNSPGK RNQDKEKYQE SPAARDRETF
DLKTSQITNE GEPEKGLCLL PDEGEEGSDG CSQTCDGEEP QEASSSLARC GSVPCFSAEN
LDLKTPQITN EGEPEKGLCL LPDEGEVSSE LEDHPMNEEG ESEELACSLP HDDVSGAEQS
AYENEKCSCV MCFSEEVPGG PEVKMESDQA CGTMDTVDSG NNSTLGKPKR KKRKKRGHCW
TRVRRRMQKN IQQHENSKAD GQVISNEKKA NVNLKGLSKI RGRKRGKPRT HFTQSDRAPQ
KRVQSRASRK HKDETVDFKA PLLPVTCGGV KGILHKKKLK QGISVKCIQS EDGNWFTPRE
FETKGGHARS KNWKLSVRCG GWPLRWLIEN GFLPNPPRIY YRKKKRILKS HNNTSVDPCM
RNLDECEVCR DGGELFCCDT CSRVFHEDCH IAPVETERTP WSCIFCRMKQ SSGSQQCCQE
SEVLERQMCQ QEQLKCELLL LKVYCCSESS FFAKIPYYYY IREACQGLKE PMWLDKIKKR
LNEHSYPQVE GFVRDMRLIF QNHRASYKYK DFGQMGLRLE AEFEKNFKEV FAIQETNGNN
//
