US6NL_HUMAN
ID US6NL_HUMAN Reviewed; 828 AA.
AC Q92738; A8KA79; Q15400; Q5VV10; Q7L0K9;
DT 30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=USP6 N-terminal-like protein;
DE AltName: Full=Related to the N-terminus of tre;
DE Short=RN-tre;
GN Name=USP6NL; Synonyms=KIAA0019;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH EPS8.
RX PubMed=8700515;
RA Wong W.T., Seki N., Nagase T., Nomura N., Robbins K.C., Di Fiore P.P.,
RA Matoskova B.;
RT "RN-tre identifies a family of tre-related proteins displaying a novel
RT potential protein binding domain.";
RL Oncogene 12:2563-2571(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-202 (ISOFORM 2).
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ARG-106; ASP-147 AND ARG-150.
RX PubMed=11099046; DOI=10.1038/35042605;
RA Lanzetti L., Rybin V., Malabarba M.G., Christoforidis S., Scita G.,
RA Zerial M., Di Fiore P.P.;
RT "The Eps8 protein coordinates EGF receptor signalling through Rac and
RT trafficking through Rab5.";
RL Nature 408:374-377(2000).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-582; SER-585 AND TYR-729, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-150.
RX PubMed=17562788; DOI=10.1083/jcb.200612068;
RA Fuchs E., Haas A.K., Spooner R.A., Yoshimura S., Lord J.M., Barr F.A.;
RT "Specific Rab GTPase-activating proteins define the Shiga toxin and
RT epidermal growth factor uptake pathways.";
RL J. Cell Biol. 177:1133-1143(2007).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17684057; DOI=10.1242/jcs.014225;
RA Haas A.K., Yoshimura S., Stephens D.J., Preisinger C., Fuchs E., Barr F.A.;
RT "Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs
RT required to maintain a functional Golgi complex in human cells.";
RL J. Cell Sci. 120:2997-3010(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-396 AND SER-716, 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-655; SER-659;
RP SER-680 AND SER-716, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, AND IDENTIFICATION BY
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-396; SER-400;
RP SER-585; SER-680 AND SER-716, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642 AND SER-716, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acts as a GTPase-activating protein for RAB5A and RAB43.
CC Involved in receptor trafficking. In complex with EPS8 inhibits
CC internalization of EGFR. Involved in retrograde transport from the
CC endocytic pathway to the Golgi apparatus. Involved in the transport of
CC Shiga toxin from early and recycling endosomes to the trans-Golgi
CC network. Required for structural integrity of the Golgi complex.
CC {ECO:0000269|PubMed:11099046, ECO:0000269|PubMed:17562788,
CC ECO:0000269|PubMed:17684057}.
CC -!- SUBUNIT: Interacts with EPS8. {ECO:0000269|PubMed:8700515}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92738-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92738-2; Sequence=VSP_040850;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8700515}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02807.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB449916; BAH16659.1; -; mRNA.
DR EMBL; D13644; BAA02807.2; ALT_INIT; mRNA.
DR EMBL; AK292944; BAF85633.1; -; mRNA.
DR EMBL; AL512631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86344.1; -; Genomic_DNA.
DR EMBL; BC042943; AAH42943.1; -; mRNA.
DR EMBL; CF121539; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS44357.1; -. [Q92738-2]
DR CCDS; CCDS53492.1; -. [Q92738-1]
DR RefSeq; NP_001073960.1; NM_001080491.3. [Q92738-2]
DR RefSeq; NP_055503.1; NM_014688.3. [Q92738-1]
DR AlphaFoldDB; Q92738; -.
DR SMR; Q92738; -.
DR BioGRID; 115063; 80.
DR ELM; Q92738; -.
DR IntAct; Q92738; 18.
DR MINT; Q92738; -.
DR STRING; 9606.ENSP00000277575; -.
DR iPTMnet; Q92738; -.
DR PhosphoSitePlus; Q92738; -.
DR BioMuta; USP6NL; -.
DR DMDM; 50897492; -.
DR EPD; Q92738; -.
DR jPOST; Q92738; -.
DR MassIVE; Q92738; -.
DR MaxQB; Q92738; -.
DR PaxDb; Q92738; -.
DR PeptideAtlas; Q92738; -.
DR PRIDE; Q92738; -.
DR ProteomicsDB; 75435; -. [Q92738-1]
DR ProteomicsDB; 75436; -. [Q92738-2]
DR Antibodypedia; 52457; 108 antibodies from 20 providers.
DR DNASU; 9712; -.
DR Ensembl; ENST00000277575.5; ENSP00000277575.5; ENSG00000148429.15. [Q92738-2]
DR Ensembl; ENST00000609104.6; ENSP00000476462.1; ENSG00000148429.15. [Q92738-1]
DR GeneID; 9712; -.
DR KEGG; hsa:9712; -.
DR MANE-Select; ENST00000609104.6; ENSP00000476462.1; NM_014688.5; NP_055503.1.
DR UCSC; uc001iks.1; human. [Q92738-1]
DR CTD; 9712; -.
DR DisGeNET; 9712; -.
DR GeneCards; USP6NL; -.
DR HGNC; HGNC:16858; USP6NL.
DR HPA; ENSG00000148429; Low tissue specificity.
DR MIM; 605405; gene.
DR neXtProt; NX_Q92738; -.
DR OpenTargets; ENSG00000148429; -.
DR PharmGKB; PA134955568; -.
DR VEuPathDB; HostDB:ENSG00000148429; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000156715; -.
DR HOGENOM; CLU_005350_10_3_1; -.
DR InParanoid; Q92738; -.
DR OMA; YNKLKHR; -.
DR OrthoDB; 976276at2759; -.
DR PhylomeDB; Q92738; -.
DR TreeFam; TF318099; -.
DR PathwayCommons; Q92738; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q92738; -.
DR BioGRID-ORCS; 9712; 12 hits in 1080 CRISPR screens.
DR ChiTaRS; USP6NL; human.
DR GeneWiki; USP6NL; -.
DR GenomeRNAi; 9712; -.
DR Pharos; Q92738; Tbio.
DR PRO; PR:Q92738; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q92738; protein.
DR Bgee; ENSG00000148429; Expressed in amniotic fluid and 189 other tissues.
DR ExpressionAtlas; Q92738; baseline and differential.
DR Genevisible; Q92738; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0048227; P:plasma membrane to endosome transport; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IMP:UniProtKB.
DR GO; GO:0035526; P:retrograde transport, plasma membrane to Golgi; IMP:UniProtKB.
DR GO; GO:0019068; P:virion assembly; IMP:UniProtKB.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasmic vesicle; Golgi apparatus;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..828
FT /note="USP6 N-terminal-like protein"
FT /id="PRO_0000208056"
FT DOMAIN 100..292
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 355..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XC3"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XC3"
FT MOD_RES 582
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XC3"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 729
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT VAR_SEQ 1..2
FT /note="MN -> MRTEAVVNSQGQTDYLTKD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8889548"
FT /id="VSP_040850"
FT MUTAGEN 106
FT /note="R->A: Loss of GAP activity on RAB5A."
FT /evidence="ECO:0000269|PubMed:11099046"
FT MUTAGEN 147
FT /note="D->A: Loss of GAP activity on RAB5A."
FT /evidence="ECO:0000269|PubMed:11099046"
FT MUTAGEN 150
FT /note="R->A: Loss of GAP activity on RAB5A."
FT /evidence="ECO:0000269|PubMed:11099046,
FT ECO:0000269|PubMed:17562788"
FT CONFLICT 622
FT /note="E -> D (in Ref. 4; BAF85633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 828 AA; 94104 MW; A5E3DBF0FEE04E78 CRC64;
MNSDQDVALK LAQERAEIVA KYDRGREGAE IEPWEDADYL VYKVTDRFGF LHEEELPDHN
VAVERQKHLE IERTTKWLKM LKGWEKYKNT EKFHRRIYKG IPLQLRGEVW ALLLEIPKMK
EETRDLYSKL KHRARGCSPD IRQIDLDVNR TFRDHIMFRD RYGVKQQSLF HVLAAYSIYN
TEVGYCQGMS QITALLLMYM NEEDAFWALV KLFSGPKHAM HGFFVQGFPK LLRFQEHHEK
ILNKFLSKLK QHLDSQEIYT SFYTMKWFFQ CFLDRTPFTL NLRIWDIYIF EGERVLTAMS
YTILKLHKKH LMKLSMEELV EFFQETLAKD FFFEDDFVIE QLQISMTELK RAKLDLPEPG
KEDEYPKKPL GQLPPELQSW GVHHLSNGQR SVGRPSPLAS GRRESGAPHR RHEHSPHPQS
RTGTPERAQP PRRKSVEEES KKLKDEADFQ RKLPSGPQDS SRQYNHAAAN QNSNATSNIR
KEFVPKWNKP SDVSATERTA KYTMEGKGRA AHPALAVTVP GPAEVRVSNV RPKMKALDAE
DGKRGSTASQ YDNVPGPELD SGASVEEALE RAYSQSPRHA LYPPSPRKHA EPSSSPSKVS
NKFTFKVQPP SHARYPSQLD GEARGLAHPP SYSNPPVYHG NSPKHFPTAN SSFASPQFSP
GTQLNPSRRP HGSTLSVSAS PEKSYSRPSP LVLPSSRIEV LPVDTGAGGY SGNSGSPKNG
KLIIPPVDYL PDNRTWSEVS YTYRPETQGQ SWTRDASRGN LPKYSAFQLA PFQDHGLPAV
SVDSPVRYKA SPAAEDASPS GYPYSGPPPP AYHYRNRDGL SIQESVLL
