US6NL_MOUSE
ID US6NL_MOUSE Reviewed; 819 AA.
AC Q80XC3; A2AR45; A2AR46; Q3U2W3; Q6ZQK8;
DT 30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=USP6 N-terminal-like protein;
GN Name=Usp6nl; Synonyms=Kiaa0019;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; SER-547 AND SER-665, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EPS8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic
CC vesicle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80XC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80XC3-2; Sequence=VSP_011153;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97847.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BC051184; Type=Frameshift; Evidence={ECO:0000305};
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 EMBL; AK129037; BAC97847.1; ALT_INIT; mRNA.
DR EMBL; AK155073; BAE33027.1; -; mRNA.
DR EMBL; AL845275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051184; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS38043.1; -. [Q80XC3-1]
DR CCDS; CCDS38044.1; -. [Q80XC3-2]
DR RefSeq; NP_001074017.1; NM_001080548.1. [Q80XC3-1]
DR RefSeq; NP_852064.2; NM_181399.3. [Q80XC3-2]
DR RefSeq; XP_006497632.1; XM_006497569.3. [Q80XC3-1]
DR AlphaFoldDB; Q80XC3; -.
DR SMR; Q80XC3; -.
DR BioGRID; 221154; 2.
DR STRING; 10090.ENSMUSP00000043178; -.
DR iPTMnet; Q80XC3; -.
DR PhosphoSitePlus; Q80XC3; -.
DR EPD; Q80XC3; -.
DR MaxQB; Q80XC3; -.
DR PaxDb; Q80XC3; -.
DR PRIDE; Q80XC3; -.
DR ProteomicsDB; 275395; -. [Q80XC3-1]
DR ProteomicsDB; 275396; -. [Q80XC3-2]
DR Antibodypedia; 52457; 108 antibodies from 20 providers.
DR DNASU; 98910; -.
DR Ensembl; ENSMUST00000042503; ENSMUSP00000043178; ENSMUSG00000039046. [Q80XC3-2]
DR Ensembl; ENSMUST00000114937; ENSMUSP00000110587; ENSMUSG00000039046. [Q80XC3-1]
DR GeneID; 98910; -.
DR KEGG; mmu:98910; -.
DR UCSC; uc008igk.1; mouse. [Q80XC3-1]
DR UCSC; uc008igl.1; mouse. [Q80XC3-2]
DR CTD; 9712; -.
DR MGI; MGI:2138893; Usp6nl.
DR VEuPathDB; HostDB:ENSMUSG00000039046; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000156715; -.
DR HOGENOM; CLU_005350_10_3_1; -.
DR InParanoid; Q80XC3; -.
DR OMA; YNKLKHR; -.
DR OrthoDB; 976276at2759; -.
DR PhylomeDB; Q80XC3; -.
DR TreeFam; TF318099; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 98910; 2 hits in 42 CRISPR screens.
DR ChiTaRS; Usp6nl; mouse.
DR PRO; PR:Q80XC3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80XC3; protein.
DR Bgee; ENSMUSG00000039046; Expressed in sciatic nerve and 213 other tissues.
DR Genevisible; Q80XC3; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0048227; P:plasma membrane to endosome transport; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:MGI.
DR GO; GO:0035526; P:retrograde transport, plasma membrane to Golgi; ISS:UniProtKB.
DR GO; GO:0019068; P:virion assembly; ISO:MGI.
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..819
FT /note="USP6 N-terminal-like protein"
FT /id="PRO_0000208057"
FT DOMAIN 100..292
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 355..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..807
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 378..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT MOD_RES 717
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q92738"
FT VAR_SEQ 1..2
FT /note="MN -> MIQVLQLVKELVTPSRQKAATAKED (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011153"
FT CONFLICT 446
FT /note="E -> G (in Ref. 2; BAE33027)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="A -> V (in Ref. 2; BAE33027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 93574 MW; AD6B72BB42A00B54 CRC64;
MNSDQDVALK LAQERAEIVA KYDRGREGAE IEPWEDADYL VYKVTDRFGF LHEEELPYHN
AAADRQKQLE IERTSKWLKM LKKWERYKNT EKFHRRIYKG IPLQLRGEVW ALLLEIPKMK
EETRDLYSKL KHRARGCSPD IRQIDLDVNR TFRDHIMFRD RYGVKQQSLF HVLAAYSIYN
TEVGYCQGMS QITALLLMYM NEEDAFWALV KLFSGPKHAM HGFFVQGFPK LLRFQEHHEK
ILNKFLSKLK QHLDSQEIYT SFYTMKWFFQ CFLDRTPFRL NLRIWDIYIF EGERVLTAMS
YTILKLHKKH LMKLSMEELV EFLQETLAKD FFFEDDFVIE QLQVSMAELK RAKLDLPEPG
KEDEYPKKPL GQLPPESACV NHLSNGQRSV GRPSPKTSSR REDGSPRKNH EHSPVHHSRN
GTPERAGQSR RKSVDEGSKN LKHEAESQRK PSPGMQDSSR HYNHAAANQN SNAISNVRKE
FMPKWRKPSD ASAIERTTKY AVEGKSHSAL PALPVAIPGS AETRLPNSRQ KMKALDGGEG
KRGSNASQYD NVPGGESEHG ASAEEGPERT HPHSPRKHPE PSPSPPKVPN KFTFKVQPPS
HVRYPPQLPE EDHRAAYPPS YSNPPVYHGN SPKHVPTAHS GFVSTQISPR PQINPSRRPY
GSSLSVDTSP EKAYSRPTPV VLPSSRIEVL PIDMGARGYG SSGSPKNGQF ILPPVDYLPE
NRKWSEVSYT YRPEMHGQSW TRDAHRSHLS NLPNYAAFQH IPFQAHGLPE VSVDSPVRYK
MSAAVEDASP PGYPYAGPSP SAHHYRNGEG LSVQESVLL
