Full text data of BASP1
BASP1
(NAP22)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Brain acid soluble protein 1 (22 kDa neuronal tissue-enriched acidic protein; Neuronal axonal membrane protein NAP-22)
Brain acid soluble protein 1 (22 kDa neuronal tissue-enriched acidic protein; Neuronal axonal membrane protein NAP-22)
UniProt
P80723
ID BASP1_HUMAN Reviewed; 227 AA.
AC P80723; B4DJA8; D3DTD5; O43596; Q5U0S0; Q9BWA5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Brain acid soluble protein 1;
DE AltName: Full=22 kDa neuronal tissue-enriched acidic protein;
DE AltName: Full=Neuronal axonal membrane protein NAP-22;
GN Name=BASP1; Synonyms=NAP22;
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).
RX PubMed=9749536;
RA Park S., Kim Y.-I., Kim B., Seong C., Oh Y., Baek K., Yoon J.;
RT "Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa
RT neuronal tissue-enriched acidic protein) homologs.";
RL Mol. Cells 8:471-477(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Subthalamic nucleus;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP PROTEIN SEQUENCE OF 2-227, AND MASS SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=9310187; DOI=10.1016/S0300-9084(97)80032-6;
RA Mosevitsky M.I., Capony J.-P., Skladchikova G.Y.U., Novitskaya V.A.,
RA Plekhanov A.Y.U., Zakharov V.V.;
RT "The BASP1 family of myristoylated proteins abundant in axonal
RT termini. Primary structure analysis and physico-chemical properties.";
RL Biochimie 79:373-384(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-164;
RP SER-170; SER-172; SER-176; THR-196 AND SER-205, AND MASS SPECTROMETRY.
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 [9]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-196, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell
CC projection, growth cone. Note=Associated with the membranes of
CC growth cones that form the tips of elongating axons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80723-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80723-2; Sequence=VSP_037994;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- MASS SPECTROMETRY: Mass=22780; Method=Electrospray; Range=2-227;
CC Source=PubMed:9310187;
CC -!- SIMILARITY: Belongs to the BASP1 family.
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DR EMBL; AF039656; AAC67374.1; -; mRNA.
DR EMBL; BT019340; AAV38147.1; -; mRNA.
DR EMBL; BT019341; AAV38148.1; -; mRNA.
DR EMBL; AK295995; BAG58770.1; -; mRNA.
DR EMBL; CH471102; EAX08012.1; -; Genomic_DNA.
DR EMBL; CH471102; EAX08013.1; -; Genomic_DNA.
DR EMBL; BC000518; AAH00518.1; -; mRNA.
DR RefSeq; NP_001258535.1; NM_001271606.1.
DR RefSeq; NP_006308.3; NM_006317.4.
DR UniGene; Hs.201641; -.
DR UniGene; Hs.646924; -.
DR ProteinModelPortal; P80723; -.
DR IntAct; P80723; 6.
DR MINT; MINT-5000418; -.
DR STRING; 9606.ENSP00000319281; -.
DR TCDB; 1.A.71.1.1; the brain acid-soluble protein channel (basp1 channel) family.
DR PhosphoSite; P80723; -.
DR DMDM; 6686256; -.
DR PaxDb; P80723; -.
DR PeptideAtlas; P80723; -.
DR PRIDE; P80723; -.
DR DNASU; 10409; -.
DR Ensembl; ENST00000322611; ENSP00000319281; ENSG00000176788.
DR GeneID; 10409; -.
DR KEGG; hsa:10409; -.
DR UCSC; uc003jfx.4; human.
DR CTD; 10409; -.
DR GeneCards; GC05P017065; -.
DR HGNC; HGNC:957; BASP1.
DR HPA; HPA045218; -.
DR MIM; 605940; gene.
DR neXtProt; NX_P80723; -.
DR PharmGKB; PA25261; -.
DR eggNOG; NOG46129; -.
DR HOGENOM; HOG000095176; -.
DR InParanoid; P80723; -.
DR KO; K17272; -.
DR OMA; PSKADDK; -.
DR OrthoDB; EOG7RJPVZ; -.
DR PhylomeDB; P80723; -.
DR ChiTaRS; BASP1; human.
DR GeneWiki; BASP1; -.
DR GenomeRNAi; 10409; -.
DR NextBio; 39453; -.
DR PRO; PR:P80723; -.
DR Bgee; P80723; -.
DR CleanEx; HS_BASP1; -.
DR Genevestigator; P80723; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
DR GO; GO:0060539; P:diaphragm development; ISS:UniProtKB.
DR GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; ISS:UniProtKB.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
DR GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB.
DR GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB.
DR GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB.
DR InterPro; IPR008408; BASP1.
DR PANTHER; PTHR23212; PTHR23212; 1.
DR Pfam; PF05466; BASP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Complete proteome; Direct protein sequencing; Lipoprotein; Membrane;
KW Myristate; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 227 Brain acid soluble protein 1.
FT /FTId=PRO_0000142895.
FT MOD_RES 31 31 Phosphothreonine.
FT MOD_RES 36 36 Phosphothreonine.
FT MOD_RES 164 164 Phosphoserine.
FT MOD_RES 170 170 Phosphoserine.
FT MOD_RES 172 172 Phosphoserine.
FT MOD_RES 176 176 Phosphoserine.
FT MOD_RES 196 196 Phosphothreonine.
FT MOD_RES 205 205 Phosphoserine.
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 88 141 Missing (in isoform 2).
FT /FTId=VSP_037994.
FT VARIANT 76 76 A -> V (in dbSNP:rs3733748).
FT /FTId=VAR_048396.
FT CONFLICT 45 45 A -> P (in Ref. 1; AAC67374).
FT CONFLICT 114 115 AA -> LR (in Ref. 1; AAC67374).
FT CONFLICT 128 132 APAES -> GPRPR (in Ref. 1; AAC67374).
FT CONFLICT 152 152 E -> G (in Ref. 5; AAH00518).
SQ SEQUENCE 227 AA; 22693 MW; 56FFFCEA441062AB CRC64;
MGGKLSKKKK GYNVNDEKAK EKDKKAEGAA TEEEGTPKES EPQAAAEPAE AKEGKEKPDQ
DAEGKAEEKE GEKDAAAAKE EAPKAEPEKT EGAAEAKAEP PKAPEQEQAA PGPAAGGEAP
KAAEAAAAPA ESAAPAAGEE PSKEEGEPKK TEAPAAPAAQ ETKSDGAPAS DSKPGSSEAA
PSSKETPAAT EAPSSTPKAQ GPAASAEEPK PVEAPAANSD QTVTVKE
//
ID BASP1_HUMAN Reviewed; 227 AA.
AC P80723; B4DJA8; D3DTD5; O43596; Q5U0S0; Q9BWA5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Brain acid soluble protein 1;
DE AltName: Full=22 kDa neuronal tissue-enriched acidic protein;
DE AltName: Full=Neuronal axonal membrane protein NAP-22;
GN Name=BASP1; Synonyms=NAP22;
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).
RX PubMed=9749536;
RA Park S., Kim Y.-I., Kim B., Seong C., Oh Y., Baek K., Yoon J.;
RT "Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa
RT neuronal tissue-enriched acidic protein) homologs.";
RL Mol. Cells 8:471-477(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Subthalamic nucleus;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP PROTEIN SEQUENCE OF 2-227, AND MASS SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=9310187; DOI=10.1016/S0300-9084(97)80032-6;
RA Mosevitsky M.I., Capony J.-P., Skladchikova G.Y.U., Novitskaya V.A.,
RA Plekhanov A.Y.U., Zakharov V.V.;
RT "The BASP1 family of myristoylated proteins abundant in axonal
RT termini. Primary structure analysis and physico-chemical properties.";
RL Biochimie 79:373-384(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-164;
RP SER-170; SER-172; SER-176; THR-196 AND SER-205, AND MASS SPECTROMETRY.
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 [9]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-196, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell
CC projection, growth cone. Note=Associated with the membranes of
CC growth cones that form the tips of elongating axons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80723-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80723-2; Sequence=VSP_037994;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- MASS SPECTROMETRY: Mass=22780; Method=Electrospray; Range=2-227;
CC Source=PubMed:9310187;
CC -!- SIMILARITY: Belongs to the BASP1 family.
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DR EMBL; AF039656; AAC67374.1; -; mRNA.
DR EMBL; BT019340; AAV38147.1; -; mRNA.
DR EMBL; BT019341; AAV38148.1; -; mRNA.
DR EMBL; AK295995; BAG58770.1; -; mRNA.
DR EMBL; CH471102; EAX08012.1; -; Genomic_DNA.
DR EMBL; CH471102; EAX08013.1; -; Genomic_DNA.
DR EMBL; BC000518; AAH00518.1; -; mRNA.
DR RefSeq; NP_001258535.1; NM_001271606.1.
DR RefSeq; NP_006308.3; NM_006317.4.
DR UniGene; Hs.201641; -.
DR UniGene; Hs.646924; -.
DR ProteinModelPortal; P80723; -.
DR IntAct; P80723; 6.
DR MINT; MINT-5000418; -.
DR STRING; 9606.ENSP00000319281; -.
DR TCDB; 1.A.71.1.1; the brain acid-soluble protein channel (basp1 channel) family.
DR PhosphoSite; P80723; -.
DR DMDM; 6686256; -.
DR PaxDb; P80723; -.
DR PeptideAtlas; P80723; -.
DR PRIDE; P80723; -.
DR DNASU; 10409; -.
DR Ensembl; ENST00000322611; ENSP00000319281; ENSG00000176788.
DR GeneID; 10409; -.
DR KEGG; hsa:10409; -.
DR UCSC; uc003jfx.4; human.
DR CTD; 10409; -.
DR GeneCards; GC05P017065; -.
DR HGNC; HGNC:957; BASP1.
DR HPA; HPA045218; -.
DR MIM; 605940; gene.
DR neXtProt; NX_P80723; -.
DR PharmGKB; PA25261; -.
DR eggNOG; NOG46129; -.
DR HOGENOM; HOG000095176; -.
DR InParanoid; P80723; -.
DR KO; K17272; -.
DR OMA; PSKADDK; -.
DR OrthoDB; EOG7RJPVZ; -.
DR PhylomeDB; P80723; -.
DR ChiTaRS; BASP1; human.
DR GeneWiki; BASP1; -.
DR GenomeRNAi; 10409; -.
DR NextBio; 39453; -.
DR PRO; PR:P80723; -.
DR Bgee; P80723; -.
DR CleanEx; HS_BASP1; -.
DR Genevestigator; P80723; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
DR GO; GO:0060539; P:diaphragm development; ISS:UniProtKB.
DR GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; ISS:UniProtKB.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
DR GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB.
DR GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB.
DR GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB.
DR InterPro; IPR008408; BASP1.
DR PANTHER; PTHR23212; PTHR23212; 1.
DR Pfam; PF05466; BASP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Complete proteome; Direct protein sequencing; Lipoprotein; Membrane;
KW Myristate; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 227 Brain acid soluble protein 1.
FT /FTId=PRO_0000142895.
FT MOD_RES 31 31 Phosphothreonine.
FT MOD_RES 36 36 Phosphothreonine.
FT MOD_RES 164 164 Phosphoserine.
FT MOD_RES 170 170 Phosphoserine.
FT MOD_RES 172 172 Phosphoserine.
FT MOD_RES 176 176 Phosphoserine.
FT MOD_RES 196 196 Phosphothreonine.
FT MOD_RES 205 205 Phosphoserine.
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 88 141 Missing (in isoform 2).
FT /FTId=VSP_037994.
FT VARIANT 76 76 A -> V (in dbSNP:rs3733748).
FT /FTId=VAR_048396.
FT CONFLICT 45 45 A -> P (in Ref. 1; AAC67374).
FT CONFLICT 114 115 AA -> LR (in Ref. 1; AAC67374).
FT CONFLICT 128 132 APAES -> GPRPR (in Ref. 1; AAC67374).
FT CONFLICT 152 152 E -> G (in Ref. 5; AAH00518).
SQ SEQUENCE 227 AA; 22693 MW; 56FFFCEA441062AB CRC64;
MGGKLSKKKK GYNVNDEKAK EKDKKAEGAA TEEEGTPKES EPQAAAEPAE AKEGKEKPDQ
DAEGKAEEKE GEKDAAAAKE EAPKAEPEKT EGAAEAKAEP PKAPEQEQAA PGPAAGGEAP
KAAEAAAAPA ESAAPAAGEE PSKEEGEPKK TEAPAAPAAQ ETKSDGAPAS DSKPGSSEAA
PSSKETPAAT EAPSSTPKAQ GPAASAEEPK PVEAPAANSD QTVTVKE
//
MIM
605940
*RECORD*
*FIELD* NO
605940
*FIELD* TI
*605940 BRAIN-ABUNDANT SIGNAL PROTEIN, MEMBRANE-ATTACHED, 1; BASP1
;;BRAIN ACID-SOLUBLE PROTEIN 1;;
read moreNAP22, RAT, HOMOLOG OF; NAP22;;
CAP23, CHICKEN, HOMOLOG OF; CAP23
*FIELD* TX
DESCRIPTION
Intercellular signaling and nerve outgrowth are influenced by a number
of proteins expressed at nerve endings and synapses. GAP43 (162060) is a
determinant of neurite outgrowth and plasticity. The rat 22-kD neuronal
tissue-enriched acidic protein (Nap22), like GAP43, binds calmodulin
(see 114180), is phosphorylated by protein kinase C (see 176982), and is
expressed specifically in nervous tissue (summary by Park et al., 1998).
CLONING
By biochemical purification, microsequencing, and protein database
searching, Mosevitsky et al. (1997) determined the complete amino acid
sequences of rat, bovine, and human BASP1. Rat Basp1 is identical to
Nap22. The 226-amino acid human protein, which is myristoylated at its N
terminus, is 80% and 70% similar to the bovine and rat proteins,
respectively. SDS-PAGE and Western blot analysis determined that BASP1
is expressed as a nearly 23-kD protein. Sequence analysis indicated the
presence of several transient phosphorylation sites as well as PEST
sequences, which are typical of proteins with high turnover rates, such
as GAP43 and MARCKS (MACS; 177061).
By PCR analysis using degenerate primers based on the rat Nap22 and
chicken Cap23 sequences, followed by screening a bovine retina cDNA
library, searching an EST database, and sequencing a purchased human
cDNA clone, Park et al. (1998) obtained cDNAs encoding bovine and human
BASP1, which they called NAP22. The deduced 227-amino acid human protein
is 60 to 70% identical to the rat protein, with nearly total identity
within the N-terminal 50 residues. BASP1 has 1 potential myristoylation
site, 3 potential phosphorylation sites, and several C-terminal PEST
sequences. Southern blot analysis indicated that bovine Basp1 is a
single-copy gene. Northern blot analysis revealed expression of a 1.7-kb
transcript in cow brain but not in liver, ovary, or retina.
Using Northern blot analysis, Fitzgibbon et al. (2000) detected
differential expression of BASP1 in cancer cell lines, with highest
expression in HeLa S3 cervical adenocarcinoma cells. They determined,
however, that elevated expression of BASP1 in this cell line is due to
multiple copies of chromosome 5p in HeLa S3 cells.
MAPPING
Fitzgibbon et al. (2000) mapped the BASP1 gene to 5p15.1-p14, a region
frequently amplified in human cancers, by FISH.
*FIELD* RF
1. Fitzgibbon, J.; Neat, M. J.; Foot, N.; Hill, A. S.; Lister, T.
A.; Gupta, R. K.: Assignment of brain acid-soluble protein 1 (BASP1)
to human chromosome 5p15.1-p14, differential expression in human cancer
cell lines as a result of alterations in gene dosage. Cytogenet.
Cell Genet. 89: 147-149, 2000.
2. Mosevitsky, M. I.; Capony, J. P.; Skladchikova, G. Y.; Novitskaya,
V. A.; Plekhanov, A. Y.; Zakharov, V. V.: The BASP1 family of myristoylated
proteins abundant in axonal termini: primary structure analysis and
physico-chemical properties. Biochimie 79: 373-384, 1997.
3. Park, S.; Kim, Y.-I.; Kim, B.; Seong, C.; Oh, Y.; Baek, K.; Yoon,
J.: Characterization of bovine and human cDNAs encoding NAP-22 (22
kDa neuronal tissue-enriched acidic protein) homologs. Molec. Cells 8:
471-477, 1998.
*FIELD* CD
Paul J. Converse: 5/16/2001
*FIELD* ED
carol: 08/05/2013
alopez: 3/26/2012
mgross: 5/16/2001
*RECORD*
*FIELD* NO
605940
*FIELD* TI
*605940 BRAIN-ABUNDANT SIGNAL PROTEIN, MEMBRANE-ATTACHED, 1; BASP1
;;BRAIN ACID-SOLUBLE PROTEIN 1;;
read moreNAP22, RAT, HOMOLOG OF; NAP22;;
CAP23, CHICKEN, HOMOLOG OF; CAP23
*FIELD* TX
DESCRIPTION
Intercellular signaling and nerve outgrowth are influenced by a number
of proteins expressed at nerve endings and synapses. GAP43 (162060) is a
determinant of neurite outgrowth and plasticity. The rat 22-kD neuronal
tissue-enriched acidic protein (Nap22), like GAP43, binds calmodulin
(see 114180), is phosphorylated by protein kinase C (see 176982), and is
expressed specifically in nervous tissue (summary by Park et al., 1998).
CLONING
By biochemical purification, microsequencing, and protein database
searching, Mosevitsky et al. (1997) determined the complete amino acid
sequences of rat, bovine, and human BASP1. Rat Basp1 is identical to
Nap22. The 226-amino acid human protein, which is myristoylated at its N
terminus, is 80% and 70% similar to the bovine and rat proteins,
respectively. SDS-PAGE and Western blot analysis determined that BASP1
is expressed as a nearly 23-kD protein. Sequence analysis indicated the
presence of several transient phosphorylation sites as well as PEST
sequences, which are typical of proteins with high turnover rates, such
as GAP43 and MARCKS (MACS; 177061).
By PCR analysis using degenerate primers based on the rat Nap22 and
chicken Cap23 sequences, followed by screening a bovine retina cDNA
library, searching an EST database, and sequencing a purchased human
cDNA clone, Park et al. (1998) obtained cDNAs encoding bovine and human
BASP1, which they called NAP22. The deduced 227-amino acid human protein
is 60 to 70% identical to the rat protein, with nearly total identity
within the N-terminal 50 residues. BASP1 has 1 potential myristoylation
site, 3 potential phosphorylation sites, and several C-terminal PEST
sequences. Southern blot analysis indicated that bovine Basp1 is a
single-copy gene. Northern blot analysis revealed expression of a 1.7-kb
transcript in cow brain but not in liver, ovary, or retina.
Using Northern blot analysis, Fitzgibbon et al. (2000) detected
differential expression of BASP1 in cancer cell lines, with highest
expression in HeLa S3 cervical adenocarcinoma cells. They determined,
however, that elevated expression of BASP1 in this cell line is due to
multiple copies of chromosome 5p in HeLa S3 cells.
MAPPING
Fitzgibbon et al. (2000) mapped the BASP1 gene to 5p15.1-p14, a region
frequently amplified in human cancers, by FISH.
*FIELD* RF
1. Fitzgibbon, J.; Neat, M. J.; Foot, N.; Hill, A. S.; Lister, T.
A.; Gupta, R. K.: Assignment of brain acid-soluble protein 1 (BASP1)
to human chromosome 5p15.1-p14, differential expression in human cancer
cell lines as a result of alterations in gene dosage. Cytogenet.
Cell Genet. 89: 147-149, 2000.
2. Mosevitsky, M. I.; Capony, J. P.; Skladchikova, G. Y.; Novitskaya,
V. A.; Plekhanov, A. Y.; Zakharov, V. V.: The BASP1 family of myristoylated
proteins abundant in axonal termini: primary structure analysis and
physico-chemical properties. Biochimie 79: 373-384, 1997.
3. Park, S.; Kim, Y.-I.; Kim, B.; Seong, C.; Oh, Y.; Baek, K.; Yoon,
J.: Characterization of bovine and human cDNAs encoding NAP-22 (22
kDa neuronal tissue-enriched acidic protein) homologs. Molec. Cells 8:
471-477, 1998.
*FIELD* CD
Paul J. Converse: 5/16/2001
*FIELD* ED
carol: 08/05/2013
alopez: 3/26/2012
mgross: 5/16/2001