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Brain acid soluble protein 1 (22 kDa neuronal tissue-enriched acidic protein) (Neuronal axonal membrane protein NAP-22)

 BASP1_HUMAN             Reviewed;         227 AA.
P80723; B4DJA8; D3DTD5; O43596; Q5U0S0; Q9BWA5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 157.
RecName: Full=Brain acid soluble protein 1;
AltName: Full=22 kDa neuronal tissue-enriched acidic protein;
AltName: Full=Neuronal axonal membrane protein NAP-22;
Name=BASP1; Synonyms=NAP22;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9749536;
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.";
Mol. Cells 8:471-477(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-227, MYRISTOYLATION AT GLY-2, AND MASS
SPECTROMETRY.
TISSUE=Brain;
PubMed=9310187; DOI=10.1016/S0300-9084(97)80032-6;
Mosevitsky M.I., Capony J.-P., Skladchikova G.Y.U., Novitskaya V.A.,
Plekhanov A.Y.U., 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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-164;
SER-170; SER-172; SER-176; THR-196 AND SER-205, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-196, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36; SER-164; SER-205 AND
SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-163, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-84 AND LYS-97, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell
projection, growth cone. Note=Associated with the membranes of
growth cones that form the tips of elongating axons.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P80723-1; Sequence=Displayed;
Name=2;
IsoId=P80723-2; Sequence=VSP_037994;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Brain.
-!- MASS SPECTROMETRY: Mass=22780; Method=Electrospray; Range=2-227;
Evidence={ECO:0000269|PubMed:9310187};
-!- SIMILARITY: Belongs to the BASP1 family. {ECO:0000305}.
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EMBL; AF039656; AAC67374.1; -; mRNA.
EMBL; BT019340; AAV38147.1; -; mRNA.
EMBL; BT019341; AAV38148.1; -; mRNA.
EMBL; AK295995; BAG58770.1; -; mRNA.
EMBL; CH471102; EAX08012.1; -; Genomic_DNA.
EMBL; CH471102; EAX08013.1; -; Genomic_DNA.
EMBL; BC000518; AAH00518.1; -; mRNA.
CCDS; CCDS3888.1; -. [P80723-1]
RefSeq; NP_001258535.1; NM_001271606.1. [P80723-1]
RefSeq; NP_006308.3; NM_006317.4. [P80723-1]
UniGene; Hs.201641; -.
UniGene; Hs.646924; -.
DisProt; DP00930; -.
ProteinModelPortal; P80723; -.
BioGrid; 115680; 60.
IntAct; P80723; 36.
STRING; 9606.ENSP00000319281; -.
TCDB; 1.A.71.1.1; the brain acid-soluble protein channel (basp1 channel) family.
iPTMnet; P80723; -.
PhosphoSitePlus; P80723; -.
SwissPalm; P80723; -.
DMDM; 6686256; -.
EPD; P80723; -.
MaxQB; P80723; -.
PaxDb; P80723; -.
PeptideAtlas; P80723; -.
PRIDE; P80723; -.
TopDownProteomics; P80723-1; -. [P80723-1]
TopDownProteomics; P80723-2; -. [P80723-2]
DNASU; 10409; -.
Ensembl; ENST00000322611; ENSP00000319281; ENSG00000176788. [P80723-1]
Ensembl; ENST00000616743; ENSP00000482066; ENSG00000176788. [P80723-1]
GeneID; 10409; -.
KEGG; hsa:10409; -.
UCSC; uc003jfx.5; human. [P80723-1]
CTD; 10409; -.
DisGeNET; 10409; -.
EuPathDB; HostDB:ENSG00000176788.8; -.
GeneCards; BASP1; -.
HGNC; HGNC:957; BASP1.
HPA; HPA045218; -.
HPA; HPA050333; -.
MIM; 605940; gene.
neXtProt; NX_P80723; -.
OpenTargets; ENSG00000176788; -.
PharmGKB; PA25261; -.
eggNOG; ENOG410J14G; Eukaryota.
eggNOG; ENOG4112CMG; LUCA.
GeneTree; ENSGT00730000111450; -.
HOGENOM; HOG000095176; -.
InParanoid; P80723; -.
KO; K17272; -.
OMA; TNSDQTI; -.
OrthoDB; EOG091G10E1; -.
ChiTaRS; BASP1; human.
GeneWiki; BASP1; -.
GenomeRNAi; 10409; -.
PRO; PR:P80723; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000176788; -.
CleanEx; HS_BASP1; -.
ExpressionAtlas; P80723; baseline and differential.
Genevisible; P80723; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0060539; P:diaphragm development; ISS:UniProtKB.
GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0008406; P:gonad development; ISS:UniProtKB.
GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB.
GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB.
InterPro; IPR008408; BASP1.
PANTHER; PTHR23212; PTHR23212; 1.
Pfam; PF05466; BASP1; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Isopeptide bond;
Lipoprotein; Membrane; Myristate; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:9310187}.
CHAIN 2 227 Brain acid soluble protein 1.
/FTId=PRO_0000142895.
MOD_RES 31 31 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 36 36 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:Q91XV3}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:Q91XV3}.
MOD_RES 196 196 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:9310187}.
CROSSLNK 25 25 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 84 84 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 97 97 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 88 141 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037994.
VARIANT 76 76 A -> V (in dbSNP:rs3733748).
/FTId=VAR_048396.
CONFLICT 45 45 A -> P (in Ref. 1; AAC67374).
{ECO:0000305}.
CONFLICT 114 115 AA -> LR (in Ref. 1; AAC67374).
{ECO:0000305}.
CONFLICT 128 132 APAES -> GPRPR (in Ref. 1; AAC67374).
{ECO:0000305}.
CONFLICT 152 152 E -> G (in Ref. 5; AAH00518).
{ECO:0000305}.
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


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