BCLA3_HUMAN
ID BCLA3_HUMAN Reviewed; 711 AA.
AC A2AJT9; A1A4E8; Q5VSM7; Q5VSN1; Q6ZS60; Q8N1W7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=BCLAF1 and THRAP3 family member 3 {ECO:0000312|HGNC:HGNC:27413};
GN Name=BCLAF3 {ECO:0000312|HGNC:HGNC:27413};
GN Synonyms=CXorf23 {ECO:0000312|HGNC:HGNC:27413};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-711 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-711 (ISOFORM 3).
RC TISSUE=Amygdala, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 290-711 (ISOFORM 2).
RC TISSUE=Colon;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-400, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AJT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJT9-2; Sequence=VSP_025459;
CC Name=3;
CC IsoId=A2AJT9-3; Sequence=VSP_025458;
CC -!- SIMILARITY: Belongs to the BCLAF1/THRAP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC87094.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL772197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK094661; BAC04399.1; ALT_INIT; mRNA.
DR EMBL; AK127709; BAC87094.1; ALT_INIT; mRNA.
DR EMBL; BC126172; AAI26173.1; -; mRNA.
DR CCDS; CCDS14194.2; -. [A2AJT9-2]
DR RefSeq; NP_938020.2; NM_198279.3. [A2AJT9-2]
DR RefSeq; XP_005274530.1; XM_005274473.3. [A2AJT9-1]
DR RefSeq; XP_011543777.1; XM_011545475.2. [A2AJT9-1]
DR RefSeq; XP_011543778.1; XM_011545476.2. [A2AJT9-1]
DR RefSeq; XP_011543779.1; XM_011545477.2. [A2AJT9-2]
DR AlphaFoldDB; A2AJT9; -.
DR BioGRID; 129173; 3.
DR IntAct; A2AJT9; 3.
DR STRING; 9606.ENSP00000369009; -.
DR iPTMnet; A2AJT9; -.
DR PhosphoSitePlus; A2AJT9; -.
DR BioMuta; BCLAF3; -.
DR EPD; A2AJT9; -.
DR jPOST; A2AJT9; -.
DR MassIVE; A2AJT9; -.
DR MaxQB; A2AJT9; -.
DR PaxDb; A2AJT9; -.
DR PeptideAtlas; A2AJT9; -.
DR PRIDE; A2AJT9; -.
DR ProteomicsDB; 405; -. [A2AJT9-1]
DR ProteomicsDB; 406; -. [A2AJT9-2]
DR ProteomicsDB; 407; -. [A2AJT9-3]
DR Antibodypedia; 9758; 34 antibodies from 11 providers.
DR DNASU; 256643; -.
DR Ensembl; ENST00000379682.9; ENSP00000369004.4; ENSG00000173681.17. [A2AJT9-1]
DR Ensembl; ENST00000379687.8; ENSP00000369009.3; ENSG00000173681.17. [A2AJT9-2]
DR GeneID; 256643; -.
DR KEGG; hsa:256643; -.
DR MANE-Select; ENST00000379682.9; ENSP00000369004.4; NM_001367774.2; NP_001354703.1.
DR UCSC; uc004czp.4; human. [A2AJT9-1]
DR CTD; 256643; -.
DR GeneCards; BCLAF3; -.
DR HGNC; HGNC:27413; BCLAF3.
DR HPA; ENSG00000173681; Low tissue specificity.
DR neXtProt; NX_A2AJT9; -.
DR OpenTargets; ENSG00000173681; -.
DR PharmGKB; PA134885371; -.
DR VEuPathDB; HostDB:ENSG00000173681; -.
DR eggNOG; ENOG502S4TN; Eukaryota.
DR GeneTree; ENSGT00950000183163; -.
DR HOGENOM; CLU_024256_0_0_1; -.
DR InParanoid; A2AJT9; -.
DR OMA; KWHEDEF; -.
DR OrthoDB; 442192at2759; -.
DR PhylomeDB; A2AJT9; -.
DR TreeFam; TF335939; -.
DR PathwayCommons; A2AJT9; -.
DR SignaLink; A2AJT9; -.
DR BioGRID-ORCS; 256643; 12 hits in 694 CRISPR screens.
DR ChiTaRS; CXorf23; human.
DR GenomeRNAi; 256643; -.
DR Pharos; A2AJT9; Tdark.
DR PRO; PR:A2AJT9; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; A2AJT9; protein.
DR Bgee; ENSG00000173681; Expressed in secondary oocyte and 124 other tissues.
DR ExpressionAtlas; A2AJT9; baseline and differential.
DR Genevisible; A2AJT9; HS.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR029199; THRAP3_BCLAF1.
DR PANTHER; PTHR15268; PTHR15268; 1.
DR Pfam; PF15440; THRAP3_BCLAF1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Mitochondrion; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..711
FT /note="BCLAF1 and THRAP3 family member 3"
FT /id="PRO_0000287434"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AG58"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AG58"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 592..711
FT /note="VKNVHTDGFQKPTHFIKSNFRKCIEKPYMNYTTQRKDIITHKPFEVEGNHRN
FT TRVRPFKSNFRGGRCQPNYKSGLVQKSLYIQAKYQRLRFTGPRGFITHKFRERLMRKKK
FT EYTDVATGI -> GLALSPRLECGVTITAYCSLYLQDSSYLPPQPPE (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025458"
FT VAR_SEQ 592..620
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025459"
FT CONFLICT A2AJT9-3:617
FT /note="S -> G (in Ref. 2; BAC04399)"
FT /evidence="ECO:0000305"
FT CONFLICT A2AJT9-3:622
FT /note="Q -> R (in Ref. 2; BAC04399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 83871 MW; ED389DC27B6C2D1B CRC64;
MARSRSRSPR WKHRSLSPVP RNAEHYKQRH SHGHYGCEYR KDPKRPVAWR MDSEKHGQSK
PRIPSRGNIY YQSYEHRSPS PNIRNSLENV YMYKPHRGYS PGRGDSNRRA QYMPKYSEGI
PYKEHERNSY PQKVQGGHSP DDHRVRGSGK GGKPPQRSIA DSFRFEGKWH EDELRHQRIQ
EEKYSQSTRR GSEDFETRSS FQKRYPEDRD FRKYGHTSKR PKDVERYESR EPARNPKWKP
EHSLPPYQED TDQWNLGPQT YRHAEREHPE TSSATKVSYD YRHKRPKLLD GDQDFSDGRT
QKYCKEEDRK YSFQKGPLNR ELDCFNTGRG RETQDGQVKE PFKPSKKDSI ACTYSNKNDV
DLRSSNDKWK EKIKKEGDCR KESNSSSNQL DKSQKLPDVK PSPINLRKKS LTVKVDVKKT
VDTFRVASSY STERQMSHDL VAVGRKSENF HPVFEHLDST QNTENKPTGE FAQEIITIIH
QVKANYFPSP GITLHERFST MQDIHKADVN EIPLNSDPEI HRRIDMSLAE LQSKQAVIYE
SEQTLIKIID PNDLRHDIER RRKERLQNED EHIFHIASAA ERDDQNSSFS KVKNVHTDGF
QKPTHFIKSN FRKCIEKPYM NYTTQRKDII THKPFEVEGN HRNTRVRPFK SNFRGGRCQP
NYKSGLVQKS LYIQAKYQRL RFTGPRGFIT HKFRERLMRK KKEYTDVATG I
