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P80723 (BASP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brain acid soluble protein 1
Alternative name(s):
22 kDa neuronal tissue-enriched acidic protein
Neuronal axonal membrane protein NAP-22
Gene names
Name:BASP1
Synonyms:NAP22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Cell membrane; Lipid-anchor. Cell projectiongrowth cone. Note: Associated with the membranes of growth cones that form the tips of elongating axons.

Tissue specificity

Brain.

Sequence similarities

Belongs to the BASP1 family.

Mass spectrometry

Molecular mass is 22780 Da from positions 2 - 227. Determined by ESI. Ref.6

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdiaphragm development

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular visceral epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

gonad development

Inferred from sequence or structural similarity. Source: UniProtKB

mesenchymal to epithelial transition

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric mesenchyme development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 19050011. Source: UniProtKB

positive regulation of heart growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metanephric ureteric bud development

Inferred from sequence or structural similarity. Source: UniProtKB

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

thorax and anterior abdomen determination

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay PubMed 14701728. Source: UniProtKB

cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 14701728. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionprotein domain specific binding

Inferred from physical interaction PubMed 14701728. Source: UniProtKB

transcription corepressor activity

Inferred from mutant phenotype PubMed 14701728. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P80723-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P80723-2)

The sequence of this isoform differs from the canonical sequence as follows:
     88-141: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 227226Brain acid soluble protein 1
PRO_0000142895

Amino acid modifications

Modified residue311Phosphothreonine Ref.8
Modified residue361Phosphothreonine Ref.7 Ref.8 Ref.10
Modified residue1641Phosphoserine Ref.8
Modified residue1701Phosphoserine Ref.8
Modified residue1721Phosphoserine Ref.8
Modified residue1761Phosphoserine Ref.8
Modified residue1961Phosphothreonine Ref.8 Ref.10
Modified residue2051Phosphoserine Ref.8
Lipidation21N-myristoyl glycine

Natural variations

Alternative sequence88 – 14154Missing in isoform 2.
VSP_037994
Natural variant761A → V.
Corresponds to variant rs3733748 [ dbSNP | Ensembl ].
VAR_048396

Experimental info

Sequence conflict451A → P in AAC67374. Ref.1
Sequence conflict114 – 1152AA → LR in AAC67374. Ref.1
Sequence conflict128 – 1325APAES → GPRPR in AAC67374. Ref.1
Sequence conflict1521E → G in AAH00518. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 56FFFCEA441062AB

FASTA22722,693
        10         20         30         40         50         60 
MGGKLSKKKK GYNVNDEKAK EKDKKAEGAA TEEEGTPKES EPQAAAEPAE AKEGKEKPDQ 

        70         80         90        100        110        120 
DAEGKAEEKE GEKDAAAAKE EAPKAEPEKT EGAAEAKAEP PKAPEQEQAA PGPAAGGEAP 

       130        140        150        160        170        180 
KAAEAAAAPA ESAAPAAGEE PSKEEGEPKK TEAPAAPAAQ ETKSDGAPAS DSKPGSSEAA 

       190        200        210        220 
PSSKETPAAT EAPSSTPKAQ GPAASAEEPK PVEAPAANSD QTVTVKE 

« Hide

Isoform 2 [UniParc].

Checksum: 562F9FC9D05A565C
Show »

FASTA17317,664

References

« Hide 'large scale' references
[1]"Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa neuronal tissue-enriched acidic protein) homologs."
Park S., Kim Y.-I., Kim B., Seong C., Oh Y., Baek K., Yoon J.
Mol. Cells 8:471-477(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Subthalamic nucleus.
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[6]"The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties."
Mosevitsky M.I., Capony J.-P., Skladchikova G.Y.U., Novitskaya V.A., Plekhanov A.Y.U., Zakharov V.V.
Biochimie 79:373-384(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-227, MASS SPECTROMETRY.
Tissue: Brain.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-164; SER-170; SER-172; SER-176; THR-196 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039656 mRNA. Translation: AAC67374.1.
BT019340 mRNA. Translation: AAV38147.1.
BT019341 mRNA. Translation: AAV38148.1.
AK295995 mRNA. Translation: BAG58770.1.
CH471102 Genomic DNA. Translation: EAX08012.1.
CH471102 Genomic DNA. Translation: EAX08013.1.
BC000518 mRNA. Translation: AAH00518.1.
RefSeqNP_001258535.1. NM_001271606.1.
NP_006308.3. NM_006317.4.
UniGeneHs.201641.
Hs.646924.

3D structure databases

ProteinModelPortalP80723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115680. 16 interactions.
IntActP80723. 7 interactions.
MINTMINT-5000418.
STRING9606.ENSP00000319281.

Protein family/group databases

TCDB1.A.71.1.1. the brain acid-soluble protein channel (basp1 channel) family.

PTM databases

PhosphoSiteP80723.

Polymorphism databases

DMDM6686256.

Proteomic databases

PaxDbP80723.
PeptideAtlasP80723.
PRIDEP80723.

Protocols and materials databases

DNASU10409.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322611; ENSP00000319281; ENSG00000176788. [P80723-1]
GeneID10409.
KEGGhsa:10409.
UCSCuc003jfx.4. human. [P80723-1]

Organism-specific databases

CTD10409.
GeneCardsGC05P017065.
HGNCHGNC:957. BASP1.
HPAHPA045218.
HPA050333.
MIM605940. gene.
neXtProtNX_P80723.
PharmGKBPA25261.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46129.
HOGENOMHOG000095176.
InParanoidP80723.
KOK17272.
OMAPSKADDK.
OrthoDBEOG7RJPVZ.
PhylomeDBP80723.

Gene expression databases

BgeeP80723.
CleanExHS_BASP1.
GenevestigatorP80723.

Family and domain databases

InterProIPR008408. BASP1.
[Graphical view]
PANTHERPTHR23212. PTHR23212. 1 hit.
PfamPF05466. BASP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBASP1. human.
GeneWikiBASP1.
GenomeRNAi10409.
NextBio39453.
PROP80723.
SOURCESearch...

Entry information

Entry nameBASP1_HUMAN
AccessionPrimary (citable) accession number: P80723
Secondary accession number(s): B4DJA8 expand/collapse secondary AC list , D3DTD5, O43596, Q5U0S0, Q9BWA5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM