Full text data of UBAP1
UBAP1
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-associated protein 1; UBAP-1 (Nasopharyngeal carcinoma-associated gene 20 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-associated protein 1; UBAP-1 (Nasopharyngeal carcinoma-associated gene 20 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NZ09
ID UBAP1_HUMAN Reviewed; 502 AA.
AC Q9NZ09; B7Z348; B7Z8N9; D3DRL7; F5GXE2; F5H0J8; Q4V759; Q53FP7;
read moreAC Q5T7B3; Q6FI75; Q8NC52; Q8NCG6; Q8NCH9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Ubiquitin-associated protein 1;
DE Short=UBAP-1;
DE AltName: Full=Nasopharyngeal carcinoma-associated gene 20 protein;
GN Name=UBAP1; ORFNames=NAG20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Li W., Zeng Z., Zhao X., Shen S., Li G.;
RT "Isolation and characterization of a novel cDNA, UBAP1, derived from
RT the 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RP NUCLEOTIDE 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
RP GLU-59; 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 STRUCTURE BY NMR OF 381-430.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of UBA domain of human ubiquitin associated
RT protein 1 (UBAP1).";
RL Submitted (NOV-2004) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 389-502, FUNCTION,
RP IDENTIFICATION IN ESCRT-I COMPLEX, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 17-LEU--ASP-19 AND 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).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process. Binds to ubiquitinated cargo
CC proteins and is required for the sorting of endocytic
CC ubiquitinated cargos into multivesicular bodies (MVBs). Plays a
CC role in the proteasomal degradation of ubiquitinated cell-surface
CC proteins, such as EGFR and BST2.
CC -!- SUBUNIT: Component of an ESCRT-I complex (endosomal sorting
CC complex required for transport I) which consists of TSG101, VPS28,
CC VPS37A and UBAP1 in a 1:1:1:1 stoechiometry. Can be a component of
CC ESCRT-I complexes containing VPS37B, VPS37C and VPS37D (in vitro)
CC (PubMed:22405001), but may have a preference for the ESCRT-I
CC complex containing VPS37A (PubMed:21757351). Interacts with
CC PTPN23. Interacts (via UBA domains) with ubiquitinated proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome.
CC Note=Predominantly cytosolic. Recruited to endosomes as part of
CC the ESCRT-I complex.
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 Note=Derived from EST data. No experimental confirmation
CC available;
CC Name=3;
CC IsoId=Q9NZ09-3; Sequence=VSP_046866;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NZ09-4; Sequence=VSP_046867;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain,
CC placenta, lung, liver, skeletal muscle and pancreas.
CC -!- DOMAIN: The UMA domain mediates association with the ESCRT-I
CC complex.
CC -!- SIMILARITY: Contains 2 UBA domains.
CC -!- SIMILARITY: Contains 1 UMA domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11162.1; Type=Erroneous initiation;
CC Sequence=BAH12084.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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; CAI15914.1; -; Genomic_DNA.
DR EMBL; AL353662; CAI15915.1; -; 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 RefSeq; NP_001164672.1; NM_001171201.1.
DR RefSeq; NP_001164673.1; NM_001171202.1.
DR RefSeq; NP_001164674.1; NM_001171203.2.
DR RefSeq; NP_001164675.1; NM_001171204.2.
DR RefSeq; NP_057609.2; NM_016525.4.
DR UniGene; Hs.268963; -.
DR PDB; 1WGN; NMR; -; A=381-430.
DR PDB; 4AE4; X-ray; 1.65 A; A/B=389-502.
DR PDBsum; 1WGN; -.
DR PDBsum; 4AE4; -.
DR ProteinModelPortal; Q9NZ09; -.
DR SMR; Q9NZ09; 381-499.
DR DIP; DIP-47291N; -.
DR MINT; MINT-3077159; -.
DR STRING; 9606.ENSP00000297661; -.
DR PhosphoSite; Q9NZ09; -.
DR DMDM; 67475018; -.
DR PaxDb; Q9NZ09; -.
DR PRIDE; Q9NZ09; -.
DR DNASU; 51271; -.
DR Ensembl; ENST00000297661; ENSP00000297661; ENSG00000165006.
DR Ensembl; ENST00000359544; ENSP00000352541; ENSG00000165006.
DR Ensembl; ENST00000379186; ENSP00000368484; ENSG00000165006.
DR Ensembl; ENST00000536252; ENSP00000440456; ENSG00000165006.
DR Ensembl; ENST00000540348; ENSP00000439976; ENSG00000165006.
DR Ensembl; ENST00000543944; ENSP00000439806; ENSG00000165006.
DR Ensembl; ENST00000545103; ENSP00000441024; ENSG00000165006.
DR GeneID; 51271; -.
DR KEGG; hsa:51271; -.
DR UCSC; uc011loj.2; human.
DR CTD; 51271; -.
DR GeneCards; GC09P034179; -.
DR HGNC; HGNC:12461; UBAP1.
DR HPA; HPA019804; -.
DR MIM; 609787; gene.
DR neXtProt; NX_Q9NZ09; -.
DR PharmGKB; PA37111; -.
DR eggNOG; NOG42214; -.
DR HOVERGEN; HBG060426; -.
DR InParanoid; Q9NZ09; -.
DR OMA; YLFAHGQ; -.
DR OrthoDB; EOG75MVWG; -.
DR PhylomeDB; Q9NZ09; -.
DR ChiTaRS; UBAP1; human.
DR EvolutionaryTrace; Q9NZ09; -.
DR GeneWiki; UBAP1; -.
DR GenomeRNAi; 51271; -.
DR NextBio; 54471; -.
DR PRO; PR:Q9NZ09; -.
DR ArrayExpress; Q9NZ09; -.
DR Bgee; Q9NZ09; -.
DR CleanEx; HS_UBAP1; -.
DR Genevestigator; Q9NZ09; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA: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; IMP:UniProtKB.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR023340; UMA.
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; Complete proteome; Cytoplasm;
KW Endosome; Polymorphism; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1 502 Ubiquitin-associated protein 1.
FT /FTId=PRO_0000211017.
FT DOMAIN 17 63 UMA.
FT DOMAIN 389 430 UBA 1.
FT DOMAIN 451 498 UBA 2.
FT VAR_SEQ 1 53 MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFS
FT LPDCLQVVREVQ -> MSGAVRGRRREVGLQHGGCGTGGGY
FT GDGLARSGQSWRWWRSLSLGAVGSSAGTEPGRPAGASTFRL
FT LRRRQQRHSGSKWLLRSWVQIFM (in isoform 3).
FT /FTId=VSP_046866.
FT VAR_SEQ 1 11 MASKKLGADFH -> MSGAVRGRRREVGLQHGGCGTGGGYG
FT DGLARSGQSWRWWRSLSLGAVGSSAGTEPGRPAGASTFRLL
FT RRRQQRHS (in isoform 4).
FT /FTId=VSP_046867.
FT VAR_SEQ 362 422 Missing (in isoform 2).
FT /FTId=VSP_013650.
FT VARIANT 357 357 N -> K (in dbSNP:rs16935457).
FT /FTId=VAR_034577.
FT MUTAGEN 17 19 LDD->AAA: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 20 22 VPF->AAA: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 37 37 P->A: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 59 59 E->G: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 404 404 Y->A: Strongly reduced interaction with
FT ubiquitinated proteins.
FT MUTAGEN 472 472 F->A: Strongly reduced interaction with
FT ubiquitinated proteins.
FT CONFLICT 81 81 C -> R (in Ref. 4; CAG38582).
FT CONFLICT 187 187 T -> N (in Ref. 3; BAH14025).
FT CONFLICT 331 331 E -> D (in Ref. 3; BAC11176).
FT CONFLICT 398 398 T -> M (in Ref. 3; BAH12084).
FT CONFLICT 403 403 G -> C (in Ref. 3; BAC11323).
FT HELIX 383 386
FT HELIX 390 401
FT HELIX 406 416
FT HELIX 420 435
FT HELIX 440 449
FT HELIX 454 469
FT HELIX 474 483
FT TURN 484 486
FT HELIX 488 498
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
//
ID UBAP1_HUMAN Reviewed; 502 AA.
AC Q9NZ09; B7Z348; B7Z8N9; D3DRL7; F5GXE2; F5H0J8; Q4V759; Q53FP7;
read moreAC Q5T7B3; Q6FI75; Q8NC52; Q8NCG6; Q8NCH9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Ubiquitin-associated protein 1;
DE Short=UBAP-1;
DE AltName: Full=Nasopharyngeal carcinoma-associated gene 20 protein;
GN Name=UBAP1; ORFNames=NAG20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Li W., Zeng Z., Zhao X., Shen S., Li G.;
RT "Isolation and characterization of a novel cDNA, UBAP1, derived from
RT the 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RP NUCLEOTIDE 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
RP GLU-59; 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 STRUCTURE BY NMR OF 381-430.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of UBA domain of human ubiquitin associated
RT protein 1 (UBAP1).";
RL Submitted (NOV-2004) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 389-502, FUNCTION,
RP IDENTIFICATION IN ESCRT-I COMPLEX, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 17-LEU--ASP-19 AND 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).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process. Binds to ubiquitinated cargo
CC proteins and is required for the sorting of endocytic
CC ubiquitinated cargos into multivesicular bodies (MVBs). Plays a
CC role in the proteasomal degradation of ubiquitinated cell-surface
CC proteins, such as EGFR and BST2.
CC -!- SUBUNIT: Component of an ESCRT-I complex (endosomal sorting
CC complex required for transport I) which consists of TSG101, VPS28,
CC VPS37A and UBAP1 in a 1:1:1:1 stoechiometry. Can be a component of
CC ESCRT-I complexes containing VPS37B, VPS37C and VPS37D (in vitro)
CC (PubMed:22405001), but may have a preference for the ESCRT-I
CC complex containing VPS37A (PubMed:21757351). Interacts with
CC PTPN23. Interacts (via UBA domains) with ubiquitinated proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome.
CC Note=Predominantly cytosolic. Recruited to endosomes as part of
CC the ESCRT-I complex.
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 Note=Derived from EST data. No experimental confirmation
CC available;
CC Name=3;
CC IsoId=Q9NZ09-3; Sequence=VSP_046866;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NZ09-4; Sequence=VSP_046867;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain,
CC placenta, lung, liver, skeletal muscle and pancreas.
CC -!- DOMAIN: The UMA domain mediates association with the ESCRT-I
CC complex.
CC -!- SIMILARITY: Contains 2 UBA domains.
CC -!- SIMILARITY: Contains 1 UMA domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11162.1; Type=Erroneous initiation;
CC Sequence=BAH12084.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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; CAI15914.1; -; Genomic_DNA.
DR EMBL; AL353662; CAI15915.1; -; 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 RefSeq; NP_001164672.1; NM_001171201.1.
DR RefSeq; NP_001164673.1; NM_001171202.1.
DR RefSeq; NP_001164674.1; NM_001171203.2.
DR RefSeq; NP_001164675.1; NM_001171204.2.
DR RefSeq; NP_057609.2; NM_016525.4.
DR UniGene; Hs.268963; -.
DR PDB; 1WGN; NMR; -; A=381-430.
DR PDB; 4AE4; X-ray; 1.65 A; A/B=389-502.
DR PDBsum; 1WGN; -.
DR PDBsum; 4AE4; -.
DR ProteinModelPortal; Q9NZ09; -.
DR SMR; Q9NZ09; 381-499.
DR DIP; DIP-47291N; -.
DR MINT; MINT-3077159; -.
DR STRING; 9606.ENSP00000297661; -.
DR PhosphoSite; Q9NZ09; -.
DR DMDM; 67475018; -.
DR PaxDb; Q9NZ09; -.
DR PRIDE; Q9NZ09; -.
DR DNASU; 51271; -.
DR Ensembl; ENST00000297661; ENSP00000297661; ENSG00000165006.
DR Ensembl; ENST00000359544; ENSP00000352541; ENSG00000165006.
DR Ensembl; ENST00000379186; ENSP00000368484; ENSG00000165006.
DR Ensembl; ENST00000536252; ENSP00000440456; ENSG00000165006.
DR Ensembl; ENST00000540348; ENSP00000439976; ENSG00000165006.
DR Ensembl; ENST00000543944; ENSP00000439806; ENSG00000165006.
DR Ensembl; ENST00000545103; ENSP00000441024; ENSG00000165006.
DR GeneID; 51271; -.
DR KEGG; hsa:51271; -.
DR UCSC; uc011loj.2; human.
DR CTD; 51271; -.
DR GeneCards; GC09P034179; -.
DR HGNC; HGNC:12461; UBAP1.
DR HPA; HPA019804; -.
DR MIM; 609787; gene.
DR neXtProt; NX_Q9NZ09; -.
DR PharmGKB; PA37111; -.
DR eggNOG; NOG42214; -.
DR HOVERGEN; HBG060426; -.
DR InParanoid; Q9NZ09; -.
DR OMA; YLFAHGQ; -.
DR OrthoDB; EOG75MVWG; -.
DR PhylomeDB; Q9NZ09; -.
DR ChiTaRS; UBAP1; human.
DR EvolutionaryTrace; Q9NZ09; -.
DR GeneWiki; UBAP1; -.
DR GenomeRNAi; 51271; -.
DR NextBio; 54471; -.
DR PRO; PR:Q9NZ09; -.
DR ArrayExpress; Q9NZ09; -.
DR Bgee; Q9NZ09; -.
DR CleanEx; HS_UBAP1; -.
DR Genevestigator; Q9NZ09; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA: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; IMP:UniProtKB.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR023340; UMA.
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; Complete proteome; Cytoplasm;
KW Endosome; Polymorphism; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1 502 Ubiquitin-associated protein 1.
FT /FTId=PRO_0000211017.
FT DOMAIN 17 63 UMA.
FT DOMAIN 389 430 UBA 1.
FT DOMAIN 451 498 UBA 2.
FT VAR_SEQ 1 53 MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFS
FT LPDCLQVVREVQ -> MSGAVRGRRREVGLQHGGCGTGGGY
FT GDGLARSGQSWRWWRSLSLGAVGSSAGTEPGRPAGASTFRL
FT LRRRQQRHSGSKWLLRSWVQIFM (in isoform 3).
FT /FTId=VSP_046866.
FT VAR_SEQ 1 11 MASKKLGADFH -> MSGAVRGRRREVGLQHGGCGTGGGYG
FT DGLARSGQSWRWWRSLSLGAVGSSAGTEPGRPAGASTFRLL
FT RRRQQRHS (in isoform 4).
FT /FTId=VSP_046867.
FT VAR_SEQ 362 422 Missing (in isoform 2).
FT /FTId=VSP_013650.
FT VARIANT 357 357 N -> K (in dbSNP:rs16935457).
FT /FTId=VAR_034577.
FT MUTAGEN 17 19 LDD->AAA: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 20 22 VPF->AAA: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 37 37 P->A: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 59 59 E->G: Abolishes association with the
FT ESCRT-I complex.
FT MUTAGEN 404 404 Y->A: Strongly reduced interaction with
FT ubiquitinated proteins.
FT MUTAGEN 472 472 F->A: Strongly reduced interaction with
FT ubiquitinated proteins.
FT CONFLICT 81 81 C -> R (in Ref. 4; CAG38582).
FT CONFLICT 187 187 T -> N (in Ref. 3; BAH14025).
FT CONFLICT 331 331 E -> D (in Ref. 3; BAC11176).
FT CONFLICT 398 398 T -> M (in Ref. 3; BAH12084).
FT CONFLICT 403 403 G -> C (in Ref. 3; BAC11323).
FT HELIX 383 386
FT HELIX 390 401
FT HELIX 406 416
FT HELIX 420 435
FT HELIX 440 449
FT HELIX 454 469
FT HELIX 474 483
FT TURN 484 486
FT HELIX 488 498
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
//
MIM
609787
*RECORD*
*FIELD* NO
609787
*FIELD* TI
*609787 UBIQUITIN-ASSOCIATED PROTEIN 1; UBAP1
;;UBAP
*FIELD* TX
CLONING
By screening the expression patterns of ESTs located in a region at
read more9p22-p21 undergoing loss of heterozygosity in nasopharyngeal carcinoma
(NPC), Yang et al. (1999) identified an EST that is downregulated in
NPC. Using the clone for this EST and 5-prime RACE, Qian et al. (2001)
identified the full-length cDNA sequence, which they designated UBAP1.
The deduced 502-amino acid protein has a predicted molecular mass of 55
kD and contains 2 putative tandem UBA domains at the C terminus, a
coiled-coil domain, 2 possible N-glycosylation sites, 5 PKC
phosphorylation sites, 7 casein kinase II phosphorylation sites, and 3
N-myristoylation sites. Qian et al. (2001) also identified mouse Ubap1.
The human and mouse proteins share 90% sequence identity. Northern blot
analysis of human tissues detected ubiquitous expression of a 2.7-kb
transcript, with highest expression in heart, skeletal muscle, and
liver. RT-PCR of mouse tissues also revealed ubiquitous expression.
MOLECULAR GENETICS
Using RT-PCR and direct sequencing, Qian et al. (2001) screened the NPC
cell line HNE1 and 10 primary NPCs for mutations in the UBAP1 gene. They
found no sequence alterations.
MAPPING
By sequence analysis, Qian et al. (2001) mapped the UBAP1 gene to
chromosome 9p22-p21.
*FIELD* RF
1. Qian, J.; Yang, J.; Zhang, X.; Zhang, B.; Wang, J.; Zhou, M.; Tang,
K.; Li, W.; Zeng, Z.; Zhao, X.; Shen, S.; Li, G.: Isolation and characterization
of a novel cDNA, UBAP1, derived from the tumor suppressor locus in
human chromosome 9p21-22. J. Cancer Res. Clin. Oncol. 127: 613-618,
2001.
2. Yang, J. B.; Tang, X. N.; Deng, L. W.: Detailed deletion mapping
of chromosome 9p21-22 in nasopharyngeal carcinoma. Chin. J. Oncol. 21:
419-421, 1999. Note: Article in Chinese.
*FIELD* CD
Jennifer L. Goldstein: 12/13/2005
*FIELD* ED
terry: 04/12/2012
carol: 12/13/2005
*RECORD*
*FIELD* NO
609787
*FIELD* TI
*609787 UBIQUITIN-ASSOCIATED PROTEIN 1; UBAP1
;;UBAP
*FIELD* TX
CLONING
By screening the expression patterns of ESTs located in a region at
read more9p22-p21 undergoing loss of heterozygosity in nasopharyngeal carcinoma
(NPC), Yang et al. (1999) identified an EST that is downregulated in
NPC. Using the clone for this EST and 5-prime RACE, Qian et al. (2001)
identified the full-length cDNA sequence, which they designated UBAP1.
The deduced 502-amino acid protein has a predicted molecular mass of 55
kD and contains 2 putative tandem UBA domains at the C terminus, a
coiled-coil domain, 2 possible N-glycosylation sites, 5 PKC
phosphorylation sites, 7 casein kinase II phosphorylation sites, and 3
N-myristoylation sites. Qian et al. (2001) also identified mouse Ubap1.
The human and mouse proteins share 90% sequence identity. Northern blot
analysis of human tissues detected ubiquitous expression of a 2.7-kb
transcript, with highest expression in heart, skeletal muscle, and
liver. RT-PCR of mouse tissues also revealed ubiquitous expression.
MOLECULAR GENETICS
Using RT-PCR and direct sequencing, Qian et al. (2001) screened the NPC
cell line HNE1 and 10 primary NPCs for mutations in the UBAP1 gene. They
found no sequence alterations.
MAPPING
By sequence analysis, Qian et al. (2001) mapped the UBAP1 gene to
chromosome 9p22-p21.
*FIELD* RF
1. Qian, J.; Yang, J.; Zhang, X.; Zhang, B.; Wang, J.; Zhou, M.; Tang,
K.; Li, W.; Zeng, Z.; Zhao, X.; Shen, S.; Li, G.: Isolation and characterization
of a novel cDNA, UBAP1, derived from the tumor suppressor locus in
human chromosome 9p21-22. J. Cancer Res. Clin. Oncol. 127: 613-618,
2001.
2. Yang, J. B.; Tang, X. N.; Deng, L. W.: Detailed deletion mapping
of chromosome 9p21-22 in nasopharyngeal carcinoma. Chin. J. Oncol. 21:
419-421, 1999. Note: Article in Chinese.
*FIELD* CD
Jennifer L. Goldstein: 12/13/2005
*FIELD* ED
terry: 04/12/2012
carol: 12/13/2005