OTU6A_HUMAN
ID OTU6A_HUMAN Reviewed; 288 AA.
AC Q7L8S5; B2RPB7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=OTU domain-containing protein 6A;
DE EC=3.4.19.12;
DE AltName: Full=DUBA-2;
GN Name=OTUD6A; Synonyms=DUBA2;
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 MRNA].
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M.,
RA Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and enable
RT ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
CC -!- FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-27'-, 'Lys-
CC 29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze
CC 'Lys-11'-linked ubiquitin chains. {ECO:0000269|PubMed:23827681}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:23827681};
CC -!- INTERACTION:
CC Q7L8S5; Q14195-2: DPYSL3; NbExp=3; IntAct=EBI-11960139, EBI-10232496;
CC Q7L8S5; P63167: DYNLL1; NbExp=5; IntAct=EBI-11960139, EBI-349105;
CC Q7L8S5; Q96FJ2: DYNLL2; NbExp=3; IntAct=EBI-11960139, EBI-742371;
CC Q7L8S5; Q04743: EMX2; NbExp=3; IntAct=EBI-11960139, EBI-399831;
CC Q7L8S5; P12524-2: MYCL; NbExp=3; IntAct=EBI-11960139, EBI-18936665;
CC Q7L8S5; P37198: NUP62; NbExp=3; IntAct=EBI-11960139, EBI-347978;
CC Q7L8S5; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-11960139, EBI-350517;
CC Q7L8S5; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-11960139, EBI-11956563;
CC Q7L8S5; Q04837: SSBP1; NbExp=3; IntAct=EBI-11960139, EBI-353460;
CC Q7L8S5; Q9C029: TRIM7; NbExp=3; IntAct=EBI-11960139, EBI-2813981;
CC Q7L8S5; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-11960139, EBI-2799833;
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DR EMBL; AK098697; BAC05384.1; -; mRNA.
DR EMBL; CH471132; EAX05357.1; -; Genomic_DNA.
DR EMBL; BC137355; AAI37356.1; -; mRNA.
DR EMBL; BC137356; AAI37357.1; -; mRNA.
DR CCDS; CCDS14395.1; -.
DR RefSeq; NP_997203.1; NM_207320.2.
DR AlphaFoldDB; Q7L8S5; -.
DR SMR; Q7L8S5; -.
DR BioGRID; 126574; 23.
DR IntAct; Q7L8S5; 12.
DR STRING; 9606.ENSP00000339389; -.
DR BindingDB; Q7L8S5; -.
DR ChEMBL; CHEMBL4630842; -.
DR MEROPS; C85.008; -.
DR iPTMnet; Q7L8S5; -.
DR PhosphoSitePlus; Q7L8S5; -.
DR BioMuta; OTUD6A; -.
DR DMDM; 74713135; -.
DR MassIVE; Q7L8S5; -.
DR PaxDb; Q7L8S5; -.
DR PeptideAtlas; Q7L8S5; -.
DR PRIDE; Q7L8S5; -.
DR ProteomicsDB; 68839; -.
DR Antibodypedia; 43771; 118 antibodies from 24 providers.
DR DNASU; 139562; -.
DR Ensembl; ENST00000338352.3; ENSP00000339389.2; ENSG00000189401.3.
DR GeneID; 139562; -.
DR KEGG; hsa:139562; -.
DR MANE-Select; ENST00000338352.3; ENSP00000339389.2; NM_207320.3; NP_997203.1.
DR UCSC; uc004dxu.1; human.
DR CTD; 139562; -.
DR DisGeNET; 139562; -.
DR GeneCards; OTUD6A; -.
DR HGNC; HGNC:32312; OTUD6A.
DR HPA; ENSG00000189401; Tissue enriched (testis).
DR MIM; 300714; gene.
DR neXtProt; NX_Q7L8S5; -.
DR OpenTargets; ENSG00000189401; -.
DR PharmGKB; PA142671218; -.
DR VEuPathDB; HostDB:ENSG00000189401; -.
DR eggNOG; KOG2606; Eukaryota.
DR GeneTree; ENSGT00940000163556; -.
DR HOGENOM; CLU_034963_0_0_1; -.
DR InParanoid; Q7L8S5; -.
DR OMA; QDQLVFS; -.
DR OrthoDB; 1541668at2759; -.
DR PhylomeDB; Q7L8S5; -.
DR TreeFam; TF315010; -.
DR PathwayCommons; Q7L8S5; -.
DR SignaLink; Q7L8S5; -.
DR BioGRID-ORCS; 139562; 10 hits in 727 CRISPR screens.
DR GenomeRNAi; 139562; -.
DR Pharos; Q7L8S5; Tbio.
DR PRO; PR:Q7L8S5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q7L8S5; protein.
DR Bgee; ENSG00000189401; Expressed in right testis and 6 other tissues.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990167; P:protein K27-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0035523; P:protein K29-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990168; P:protein K33-linked deubiquitination; IDA:UniProtKB.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..288
FT /note="OTU domain-containing protein 6A"
FT /id="PRO_0000076277"
FT DOMAIN 141..275
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..152
FT /note="Cys-loop"
FT /evidence="ECO:0000250"
FT REGION 210..220
FT /note="Variable-loop"
FT /evidence="ECO:0000250"
FT REGION 258..268
FT /note="His-loop"
FT /evidence="ECO:0000250"
FT COMPBIAS 88..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /evidence="ECO:0000250"
SQ SEQUENCE 288 AA; 33300 MW; 78DCB2729A729C31 CRC64;
MDDPKSEQQR ILRRHQRERQ ELQAQIRSLK NSVPKTDKTK RKQLLQDVAR MEAEMAQKHR
QELEKFQDDS SIESVVEDLA KMNLENRPPR SSKAHRKRER MESEERERQE SIFQAEMSEH
LAGFKREEEE KLAAILGARG LEMKAIPADG HCMYRAIQDQ LVFSVSVEML RCRTASYMKK
HVDEFLPFFS NPETSDSFGY DDFMIYCDNI VRTTAWGGQL ELRALSHVLK TPIEVIQADS
PTLIIGEEYV KKPIILVYLR YAYSLGEHYN SVTPLEAGAA GGVLPRLL
