UBAP1_HUMAN
ID UBAP1_HUMAN Reviewed; 502 AA.
AC Q9NZ09; B7Z348; B7Z8N9; D3DRL7; F5GXE2; F5H0J8; Q4V759; Q53FP7; Q5T7B3;
AC Q6FI75; Q8NC52; Q8NCG6; Q8NCH9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Ubiquitin-associated protein 1 {ECO:0000303|PubMed:11599797};
DE Short=UBAP-1 {ECO:0000303|PubMed:11599797};
DE AltName: Full=Nasopharyngeal carcinoma-associated gene 20 protein;
GN Name=UBAP1 {ECO:0000303|PubMed:11599797, ECO:0000312|HGNC:HGNC:12461};
GN ORFNames=NAG20;
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), 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] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 11-502 (ISOFORM 3).
RC TISSUE=Hippocampus, and Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-357.
RC TISSUE=Stomach;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP FUNCTION, INTERACTION WITH PTPN23, IDENTIFICATION IN ESCRT-I COMPLEX,
RP SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PRO-37; GLU-59;
RP TYR-404 AND PHE-472.
RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is
RT essential for MVB sorting.";
RL Curr. Biol. 21:1245-1250(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-289, AND
RP IDENTIFICATION BY 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 [11]
RP FUNCTION, AND INTERACTION WITH VPS37A.
RX PubMed=24284069; DOI=10.1242/jcs.140673;
RA Wunderley L., Brownhill K., Stefani F., Tabernero L., Woodman P.;
RT "The molecular basis for selective assembly of the UBAP1-containing
RT endosome-specific ESCRT-I complex.";
RL J. Cell Sci. 127:663-672(2014).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY
RP 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).
RN [13]
RP STRUCTURE BY NMR OF 381-430.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of UBA domain of human ubiquitin associated protein 1
RT (UBAP1).";
RL Submitted (NOV-2004) to the PDB data bank.
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 389-502, FUNCTION, IDENTIFICATION
RP IN ESCRT-I COMPLEX, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 17-LEU--ASP-19 AND
RP 20-VAL--PHE-22.
RX PubMed=22405001; DOI=10.1016/j.str.2011.12.013;
RA Agromayor M., Soler N., Caballe A., Kueck T., Freund S.M., Allen M.D.,
RA Bycroft M., Perisic O., Ye Y., McDonald B., Scheel H., Hofmann K.,
RA Neil S.J., Martin-Serrano J., Williams R.L.;
RT "The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA
RT domain.";
RL Structure 20:414-428(2012).
RN [15] {ECO:0007744|PDB:5LM1}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 261-280 IN COMPLEX WITH PTPN23,
RP AND MUTAGENESIS OF PHE-268; PRO-269 AND LEU-271.
RX PubMed=27839950; DOI=10.1016/j.str.2016.10.006;
RA Gahloth D., Levy C., Heaven G., Stefani F., Wunderley L., Mould P.,
RA Cliff M.J., Bella J., Fielding A.J., Woodman P., Tabernero L.;
RT "Structural basis for selective interaction between the ESCRT regulator HD-
RT PTP and UBAP1.";
RL Structure 24:2115-2126(2016).
RN [16]
RP INVOLVEMENT IN SPG80, VARIANT SPG80 125-GLN--SER-502 DEL, INTERACTION WITH
RP VPS28, AND UBIQUITIN-BINDING.
RX PubMed=30929741; DOI=10.1016/j.ajhg.2019.03.001;
RA Farazi Fard M.A., Rebelo A.P., Buglo E., Nemati H., Dastsooz H.,
RA Gehweiler I., Reich S., Reichbauer J., Quintans B., Ordonez-Ugalde A.,
RA Cortese A., Courel S., Abreu L., Powell E., Danzi M.C., Martuscelli N.B.,
RA Bis-Brewer D.M., Tao F., Zarei F., Habibzadeh P., Yavarian M.,
RA Modarresi F., Silawi M., Tabatabaei Z., Yousefi M., Farpour H.R.,
RA Kessler C., Mangold E., Kobeleva X., Tournev I., Chamova T., Mueller A.J.,
RA Haack T.B., Tarnopolsky M., Gan-Or Z., Rouleau G.A., Synofzik M.,
RA Sobrido M.J., Jordanova A., Schuele R., Zuchner S., Faghihi M.A.;
RT "Truncating mutations in UBAP1 cause hereditary spastic paraplegia.";
RL Am. J. Hum. Genet. 104:767-773(2019).
RN [17]
RP VARIANT SPG80 176-GLU--SER-502 DEL, FUNCTION, AND SUBUNIT.
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:21757351, PubMed:22405001,
CC PubMed:31203368). Binds to ubiquitinated cargo proteins and is required
CC for the sorting of endocytic ubiquitinated cargos into multivesicular
CC bodies (MVBs) (PubMed:21757351, PubMed:22405001). Plays a role in the
CC proteasomal degradation of ubiquitinated cell-surface proteins, such as
CC EGFR and BST2 (PubMed:24284069, PubMed:22405001, PubMed:31203368).
CC {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001,
CC ECO:0000269|PubMed:24284069, 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 (PubMed:21757351, PubMed:24284069,
CC PubMed:22405001, PubMed:31203368) (Probable). Interacts with PTPN23
CC (PubMed:21757351, PubMed:27839950). Interacts (via UBA domains) with
CC ubiquitinated proteins (PubMed:22405001, PubMed:30929741).
CC {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001,
CC ECO:0000269|PubMed:24284069, ECO:0000269|PubMed:27839950,
CC ECO:0000269|PubMed:30929741, ECO:0000269|PubMed:31203368,
CC ECO:0000305|PubMed:30929741}.
CC -!- INTERACTION:
CC Q9NZ09; P45877: PPIC; NbExp=3; IntAct=EBI-9641159, EBI-953909;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21757351}.
CC Endosome {ECO:0000269|PubMed:21757351}. Note=Predominantly cytosolic
CC (PubMed:21757351). Recruited to endosomes as part of the ESCRT-I
CC complex (PubMed:21757351). {ECO:0000269|PubMed:21757351}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NZ09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZ09-2; Sequence=VSP_013650;
CC Name=3;
CC IsoId=Q9NZ09-3; Sequence=VSP_046866;
CC Name=4;
CC IsoId=Q9NZ09-4; Sequence=VSP_046867;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain,
CC placenta, lung, liver, skeletal muscle and pancreas.
CC {ECO:0000269|PubMed:11599797}.
CC -!- DOMAIN: The UMA domain mediates association with the ESCRT-I complex.
CC {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001}.
CC -!- DISEASE: Spastic paraplegia 80, autosomal dominant (SPG80)
CC [MIM:618418]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body.
CC {ECO:0000269|PubMed:30929741, ECO:0000269|PubMed:31203368}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- CAUTION: According to a report, can also be a component of ESCRT-I
CC complexes containing VPS37B, VPS37C or VPS37D (PubMed:22405001).
CC However, another publication showed that UBAP1 has specificity for
CC complexes containing VPS37A and not VPS37 paralogs (PubMed:24284069).
CC {ECO:0000269|PubMed:22405001, ECO:0000269|PubMed:24284069}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAH12084.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF222043; AAF37827.2; -; mRNA.
DR EMBL; AL136733; CAB66667.1; -; mRNA.
DR EMBL; AK074724; BAC11162.1; ALT_INIT; mRNA.
DR EMBL; AK074745; BAC11176.1; -; mRNA.
DR EMBL; AK074812; BAC11224.1; -; mRNA.
DR EMBL; AK074969; BAC11323.1; -; mRNA.
DR EMBL; AK074995; BAC11342.1; -; mRNA.
DR EMBL; AK295482; BAH12084.1; ALT_INIT; mRNA.
DR EMBL; AK303711; BAH14025.1; -; mRNA.
DR EMBL; CR533551; CAG38582.1; -; mRNA.
DR EMBL; AK223235; BAD96955.1; -; mRNA.
DR EMBL; AL353662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58467.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58468.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58469.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58470.1; -; Genomic_DNA.
DR EMBL; BC020950; AAH20950.1; -; mRNA.
DR EMBL; BC098141; AAH98141.1; -; mRNA.
DR EMBL; BC098316; AAH98316.1; -; mRNA.
DR EMBL; BC099726; AAH99726.1; -; mRNA.
DR EMBL; BC100668; AAI00669.1; -; mRNA.
DR CCDS; CCDS55303.1; -. [Q9NZ09-4]
DR CCDS; CCDS6550.1; -. [Q9NZ09-1]
DR RefSeq; NP_001164672.1; NM_001171201.1. [Q9NZ09-4]
DR RefSeq; NP_001164673.1; NM_001171202.1. [Q9NZ09-3]
DR RefSeq; NP_001164674.1; NM_001171203.2. [Q9NZ09-1]
DR RefSeq; NP_001164675.1; NM_001171204.2. [Q9NZ09-1]
DR RefSeq; NP_057609.2; NM_016525.4. [Q9NZ09-1]
DR RefSeq; XP_006716842.1; XM_006716779.3. [Q9NZ09-1]
DR RefSeq; XP_011516201.1; XM_011517899.1. [Q9NZ09-1]
DR RefSeq; XP_016870290.1; XM_017014801.1. [Q9NZ09-1]
DR PDB; 1WGN; NMR; -; A=381-430.
DR PDB; 4AE4; X-ray; 1.65 A; A/B=389-502.
DR PDB; 5LM1; X-ray; 2.55 A; B=261-280.
DR PDBsum; 1WGN; -.
DR PDBsum; 4AE4; -.
DR PDBsum; 5LM1; -.
DR AlphaFoldDB; Q9NZ09; -.
DR BMRB; Q9NZ09; -.
DR SMR; Q9NZ09; -.
DR BioGRID; 119424; 31.
DR ComplexPortal; CPX-7181; ESCRT-I complex, VPS37A-UBAP1 variant.
DR ComplexPortal; CPX-7201; ESCRT-I complex, VPS37B-UBAP1 variant.
DR ComplexPortal; CPX-7202; ESCRT-I complex, VPS37C-UBAP1 variant.
DR ComplexPortal; CPX-7203; ESCRT-I complex, VPS37D-UBAP1 variant.
DR DIP; DIP-47291N; -.
DR IntAct; Q9NZ09; 11.
DR MINT; Q9NZ09; -.
DR STRING; 9606.ENSP00000297661; -.
DR GlyGen; Q9NZ09; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZ09; -.
DR PhosphoSitePlus; Q9NZ09; -.
DR BioMuta; UBAP1; -.
DR DMDM; 67475018; -.
DR EPD; Q9NZ09; -.
DR jPOST; Q9NZ09; -.
DR MassIVE; Q9NZ09; -.
DR MaxQB; Q9NZ09; -.
DR PaxDb; Q9NZ09; -.
DR PeptideAtlas; Q9NZ09; -.
DR PRIDE; Q9NZ09; -.
DR ProteomicsDB; 24396; -.
DR ProteomicsDB; 25363; -.
DR ProteomicsDB; 83314; -. [Q9NZ09-1]
DR ProteomicsDB; 83315; -. [Q9NZ09-2]
DR Antibodypedia; 11158; 215 antibodies from 30 providers.
DR DNASU; 51271; -.
DR Ensembl; ENST00000297661.9; ENSP00000297661.4; ENSG00000165006.14. [Q9NZ09-1]
DR Ensembl; ENST00000359544.2; ENSP00000352541.2; ENSG00000165006.14. [Q9NZ09-1]
DR Ensembl; ENST00000379186.8; ENSP00000368484.3; ENSG00000165006.14. [Q9NZ09-2]
DR Ensembl; ENST00000625521.2; ENSP00000486574.1; ENSG00000165006.14. [Q9NZ09-4]
DR GeneID; 51271; -.
DR KEGG; hsa:51271; -.
DR MANE-Select; ENST00000297661.9; ENSP00000297661.4; NM_016525.5; NP_057609.2.
DR UCSC; uc003ztx.4; human. [Q9NZ09-1]
DR CTD; 51271; -.
DR DisGeNET; 51271; -.
DR GeneCards; UBAP1; -.
DR HGNC; HGNC:12461; UBAP1.
DR HPA; ENSG00000165006; Low tissue specificity.
DR MalaCards; UBAP1; -.
DR MIM; 609787; gene.
DR MIM; 618418; phenotype.
DR neXtProt; NX_Q9NZ09; -.
DR OpenTargets; ENSG00000165006; -.
DR Orphanet; 100993; Autosomal dominant spastic paraplegia type 12.
DR PharmGKB; PA37111; -.
DR VEuPathDB; HostDB:ENSG00000165006; -.
DR eggNOG; ENOG502QTJC; Eukaryota.
DR GeneTree; ENSGT00390000008092; -.
DR HOGENOM; CLU_041679_0_0_1; -.
DR InParanoid; Q9NZ09; -.
DR OMA; ETQYDFS; -.
DR OrthoDB; 683409at2759; -.
DR PhylomeDB; Q9NZ09; -.
DR TreeFam; TF329247; -.
DR PathwayCommons; Q9NZ09; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR SignaLink; Q9NZ09; -.
DR BioGRID-ORCS; 51271; 604 hits in 1085 CRISPR screens.
DR ChiTaRS; UBAP1; human.
DR EvolutionaryTrace; Q9NZ09; -.
DR GeneWiki; UBAP1; -.
DR GenomeRNAi; 51271; -.
DR Pharos; Q9NZ09; Tbio.
DR PRO; PR:Q9NZ09; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NZ09; protein.
DR Bgee; ENSG00000165006; Expressed in lower esophagus mucosa and 198 other tissues.
DR ExpressionAtlas; Q9NZ09; baseline and differential.
DR Genevisible; Q9NZ09; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0036258; P:multivesicular body assembly; IC:ComplexPortal.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP: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; 2.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS51497; UMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Endosome;
KW Hereditary spastic paraplegia; Neurodegeneration; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..502
FT /note="Ubiquitin-associated protein 1"
FT /id="PRO_0000211017"
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:0000269|PubMed:24284069"
FT REGION 86..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..290
FT /note="Interaction with PTPN23"
FT /evidence="ECO:0000269|PubMed:27839950"
FT COMPBIAS 96..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..53
FT /note="MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFSLPDCLQVVREV
FT Q -> MSGAVRGRRREVGLQHGGCGTGGGYGDGLARSGQSWRWWRSLSLGAVGSSAGTE
FT PGRPAGASTFRLLRRRQQRHSGSKWLLRSWVQIFM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046866"
FT VAR_SEQ 1..11
FT /note="MASKKLGADFH -> MSGAVRGRRREVGLQHGGCGTGGGYGDGLARSGQSWR
FT WWRSLSLGAVGSSAGTEPGRPAGASTFRLLRRRQQRHS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046867"
FT VAR_SEQ 362..422
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_013650"
FT VARIANT 125..502
FT /note="Missing (in SPG80)"
FT /evidence="ECO:0000269|PubMed:30929741"
FT /id="VAR_082199"
FT VARIANT 176..502
FT /note="Missing (in SPG80; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31203368"
FT /id="VAR_082200"
FT VARIANT 357
FT /note="N -> K (in dbSNP:rs16935457)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_034577"
FT MUTAGEN 17..19
FT /note="LDD->AAA: Abolishes association with the ESCRT-I
FT complex."
FT /evidence="ECO:0000269|PubMed:22405001"
FT MUTAGEN 20..22
FT /note="VPF->AAA: Abolishes association with the ESCRT-I
FT complex."
FT /evidence="ECO:0000269|PubMed:22405001"
FT MUTAGEN 37
FT /note="P->A: Abolishes association with the ESCRT-I
FT complex."
FT /evidence="ECO:0000269|PubMed:21757351"
FT MUTAGEN 59
FT /note="E->G: Abolishes association with the ESCRT-I
FT complex."
FT /evidence="ECO:0000269|PubMed:21757351"
FT MUTAGEN 268
FT /note="F->S: Abolished interaction with PTPN23."
FT /evidence="ECO:0000269|PubMed:27839950"
FT MUTAGEN 269
FT /note="P->A: Does not affect interaction with PTPN23."
FT /evidence="ECO:0000269|PubMed:27839950"
FT MUTAGEN 271
FT /note="L->A: Does not affect interaction with PTPN23."
FT /evidence="ECO:0000269|PubMed:27839950"
FT MUTAGEN 404
FT /note="Y->A: Strongly reduced interaction with
FT ubiquitinated proteins."
FT /evidence="ECO:0000269|PubMed:21757351"
FT MUTAGEN 472
FT /note="F->A: Strongly reduced interaction with
FT ubiquitinated proteins."
FT /evidence="ECO:0000269|PubMed:21757351"
FT CONFLICT 81
FT /note="C -> R (in Ref. 4; CAG38582)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="T -> N (in Ref. 3; BAH14025)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="E -> D (in Ref. 3; BAC11176)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="T -> M (in Ref. 3; BAH12084)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="G -> C (in Ref. 3; BAC11323)"
FT /evidence="ECO:0000305"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5LM1"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1WGN"
FT HELIX 390..401
FT /evidence="ECO:0007829|PDB:4AE4"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:4AE4"
FT HELIX 420..435
FT /evidence="ECO:0007829|PDB:4AE4"
FT HELIX 440..449
FT /evidence="ECO:0007829|PDB:4AE4"
FT HELIX 454..469
FT /evidence="ECO:0007829|PDB:4AE4"
FT HELIX 474..483
FT /evidence="ECO:0007829|PDB:4AE4"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:4AE4"
FT HELIX 488..498
FT /evidence="ECO:0007829|PDB:4AE4"
SQ SEQUENCE 502 AA; 55084 MW; 548457B0B2ABC0F4 CRC64;
MASKKLGADF HGTFSYLDDV PFKTGDKFKT PAKVGLPIGF SLPDCLQVVR EVQYDFSLEK
KTIEWAEEIK KIEEAEREAE CKIAEAEAKV NSKSGPEGDS KMSFSKTHST ATMPPPINPI
LASLQHNSIL TPTRVSSSAT KQKVLSPPHI KADFNLADFE CEEDPFDNLE LKTIDEKEEL
RNILVGTTGP IMAQLLDNNL PRGGSGSVLQ DEEVLASLER ATLDFKPLHK PNGFITLPQL
GNCEKMSLSS KVSLPPIPAV SNIKSLSFPK LDSDDSNQKT AKLASTFHST SCLRNGTFQN
SLKPSTQSSA SELNGHHTLG LSALNLDSGT EMPALTSSQM PSLSVLSVCT EESSPPNTGP
TVTPPNFSVS QVPNMPSCPQ AYSELQMLSP SERQCVETVV NMGYSYECVL RAMKKKGENI
EQILDYLFAH GQLCEKGFDP LLVEEALEMH QCSEEKMMEF LQLMSKFKEM GFELKDIKEV
LLLHNNDQDN ALEDLMARAG AS
