UBAP1_MOUSE
ID UBAP1_MOUSE Reviewed; 502 AA.
AC Q8BH48; Q8BQ80; Q8BSW6; Q9D749; Q9ERV5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ubiquitin-associated protein 1 {ECO:0000303|PubMed:11599797};
DE Short=UBAP-1 {ECO:0000303|PubMed:11599797};
GN Name=Ubap1 {ECO:0000303|PubMed:11599797, ECO:0000312|MGI:MGI:2149543};
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11599797; DOI=10.1007/s004320100252;
RA Qian J., Yang J., Zhang X., Zhang B., Wang J., Zhou M., Tang K., Li W.,
RA Zeng Z., Zhao X., Shen S., Li G.;
RT "Isolation and characterization of a novel cDNA, UBAP1, derived from the
RT tumor suppressor locus in human chromosome 9p21-22.";
RL J. Cancer Res. Clin. Oncol. 127:613-618(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Pituitary, Skin, Spinal ganglion, Testis, and Tongue;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PROTEIN SEQUENCE OF 246-251, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31203368; DOI=10.1093/brain/awz158;
RA Lin X., Su H.Z., Dong E.L., Lin X.H., Zhao M., Yang C., Wang C., Wang J.,
RA Chen Y.J., Yu H., Xu J., Ma L.X., Xiong Z.Q., Wang N., Chen W.J.;
RT "Stop-gain mutations in UBAP1 cause pure autosomal-dominant spastic
RT paraplegia.";
RL Brain 142:2238-2252(2019).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process (PubMed:31203368). Binds to ubiquitinated cargo
CC proteins and is required for the sorting of endocytic ubiquitinated
CC cargos into multivesicular bodies (MVBs) (By similarity). Plays a role
CC in the proteasomal degradation of ubiquitinated cell-surface proteins,
CC such as EGFR and BST2 (PubMed:31203368). {ECO:0000250|UniProtKB:Q9NZ09,
CC ECO:0000269|PubMed:31203368}.
CC -!- SUBUNIT: Component of an ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, VPS37A and
CC UBAP1 in a 1:1:1:1 stoichiometry. Interacts with PTPN23. Interacts (via
CC UBA domains) with ubiquitinated proteins.
CC {ECO:0000250|UniProtKB:Q9NZ09}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NZ09}. Endosome
CC {ECO:0000250|UniProtKB:Q9NZ09}. Note=Predominantly cytosolic. Recruited
CC to endosomes as part of the ESCRT-I complex.
CC {ECO:0000250|UniProtKB:Q9NZ09}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BH48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BH48-2; Sequence=VSP_013651;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver,
CC brain, kidney, spleen, skeletal muscle, stomach, testis and lung.
CC {ECO:0000269|PubMed:11599797}.
CC -!- DOMAIN: The UMA domain mediates association with the ESCRT-I complex.
CC {ECO:0000250|UniProtKB:Q9NZ09}.
CC -!- DISRUPTION PHENOTYPE: Lethality by postnatal day 14 (PubMed:31203368).
CC Conditional deletion in neurons impairs endosomal ubiquitin processing
CC and promotes neurodegeneration (PubMed:31203368).
CC {ECO:0000269|PubMed:31203368}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09810.3; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC26927.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF275549; AAG09810.3; ALT_FRAME; mRNA.
DR EMBL; AK028477; BAC25970.1; -; mRNA.
DR EMBL; AK028670; BAC26057.1; -; mRNA.
DR EMBL; AK009596; BAB26382.1; -; mRNA.
DR EMBL; AK030370; BAC26927.1; ALT_FRAME; mRNA.
DR EMBL; AK033121; BAC28160.1; -; mRNA.
DR EMBL; AK051346; BAC34609.1; -; mRNA.
DR EMBL; AK076078; BAC36165.1; -; mRNA.
DR EMBL; BC065996; AAH65996.1; -; mRNA.
DR CCDS; CCDS51140.1; -. [Q8BH48-1]
DR CCDS; CCDS71361.1; -. [Q8BH48-2]
DR RefSeq; NP_001277383.1; NM_001290454.1. [Q8BH48-2]
DR RefSeq; NP_075794.3; NM_023305.3. [Q8BH48-1]
DR RefSeq; XP_006538259.1; XM_006538196.2. [Q8BH48-1]
DR RefSeq; XP_006538260.1; XM_006538197.2.
DR AlphaFoldDB; Q8BH48; -.
DR SMR; Q8BH48; -.
DR BioGRID; 211957; 1.
DR STRING; 10090.ENSMUSP00000072643; -.
DR iPTMnet; Q8BH48; -.
DR PhosphoSitePlus; Q8BH48; -.
DR EPD; Q8BH48; -.
DR MaxQB; Q8BH48; -.
DR PaxDb; Q8BH48; -.
DR PeptideAtlas; Q8BH48; -.
DR PRIDE; Q8BH48; -.
DR ProteomicsDB; 298059; -. [Q8BH48-1]
DR ProteomicsDB; 298060; -. [Q8BH48-2]
DR Antibodypedia; 11158; 215 antibodies from 30 providers.
DR DNASU; 67123; -.
DR Ensembl; ENSMUST00000072866; ENSMUSP00000072643; ENSMUSG00000028437. [Q8BH48-1]
DR Ensembl; ENSMUST00000108060; ENSMUSP00000103695; ENSMUSG00000028437. [Q8BH48-2]
DR GeneID; 67123; -.
DR KEGG; mmu:67123; -.
DR UCSC; uc008sin.1; mouse. [Q8BH48-1]
DR UCSC; uc012dca.1; mouse. [Q8BH48-2]
DR CTD; 51271; -.
DR MGI; MGI:2149543; Ubap1.
DR VEuPathDB; HostDB:ENSMUSG00000028437; -.
DR eggNOG; ENOG502QTJC; Eukaryota.
DR GeneTree; ENSGT00390000008092; -.
DR HOGENOM; CLU_041679_0_0_1; -.
DR InParanoid; Q8BH48; -.
DR OMA; ETQYDFS; -.
DR OrthoDB; 683409at2759; -.
DR PhylomeDB; Q8BH48; -.
DR TreeFam; TF329247; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 67123; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Ubap1; mouse.
DR PRO; PR:Q8BH48; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BH48; protein.
DR Bgee; ENSMUSG00000028437; Expressed in granulocyte and 256 other tissues.
DR ExpressionAtlas; Q8BH48; baseline and differential.
DR Genevisible; Q8BH48; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000813; C:ESCRT I complex; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR Gene3D; 1.20.120.1920; -; 1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR038870; UBAP1.
DR InterPro; IPR042575; UBAP1_C.
DR InterPro; IPR023340; UMA.
DR PANTHER; PTHR15960; PTHR15960; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS51497; UMA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; Endosome;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..502
FT /note="Ubiquitin-associated protein 1"
FT /id="PRO_0000211018"
FT DOMAIN 17..63
FT /note="UMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00830"
FT DOMAIN 389..430
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 451..498
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..95
FT /note="Interaction with ESCRT-I"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT REGION 80..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..290
FT /note="Interaction with PTPN23"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT VAR_SEQ 362..422
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013651"
SQ SEQUENCE 502 AA; 55028 MW; 4DE473D8AF0EA510 CRC64;
MASKKLGTDV HGTFSYLDDV PFKIGDKFKT PAKVGLPIGF SLPDCLQVVR EMQYDFSLEK
KTIEWAEDIK LIQEAQREAE RKAEEAEAKV NSKSGPEGDS KVSFPKTHNT ATMPPPINPI
LASLQHNNIL TPTRVSSSAT KQKVLSPPHT KADFNPADFE CEEDPFDNLE LKTIDEKEEL
RNILVGTTGP IMAQLLDSNT ARGSSGAVLQ DEEVLASLEQ ATLDFKPLHK PNGFITLPQL
GNCEKMSLSS KVSLPPIPTV SNIKSLSFPK LDSDDSNQKT VKLASTFHST SCLRSGASRS
LLKPSTQSSA SELNGDHTLG LSALNLNSGT EVPTLTSSQM PSLSSVSVCT EESSPPDPCP
TVTPLNFSVS QVPNMPSCPQ AYLELQALSP SERQCVETVV NMGYSYDCVL RAMRKKGENI
EQILDYLFAH GQLCEKGFDP LLVEEALEMH QCSEEKMMEF LQLMSKFKEM GFELKDIKEV
LLLHNNDQDN ALEDLMARAG AS
