P80723 (BASP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
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 component	Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	diaphragm 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-dependent 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 thorax and anterior abdomen determination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 14701728. Source: UniProtKB cytoskeleton Traceable author statement Ref.1. Source: ProtInc growth cone Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 227	226	Brain acid soluble protein 1		PRO_0000142895
Amino acid modifications
	Modified residue	31	1	Phosphothreonine Ref.8
	Modified residue	36	1	Phosphothreonine Ref.7 Ref.8 Ref.9
	Modified residue	164	1	Phosphoserine Ref.8
	Modified residue	170	1	Phosphoserine Ref.8
	Modified residue	172	1	Phosphoserine Ref.8
	Modified residue	176	1	Phosphoserine Ref.8
	Modified residue	196	1	Phosphothreonine Ref.8 Ref.9
	Modified residue	205	1	Phosphoserine Ref.8
	Modified residue	219	1	Phosphoserine By similarity
	Lipidation	2	1	N-myristoyl glycine
Natural variations
	Alternative sequence	88 – 141	54	Missing in isoform 2.		VSP_037994
	Natural variant	76	1	A → V. Corresponds to variant rs3733748 [ dbSNP | Ensembl ].		VAR_048396
Experimental info
	Sequence conflict	45	1	A → P in AAC67374. Ref.1
	Sequence conflict	114 – 115	2	AA → LR in AAC67374. Ref.1
	Sequence conflict	128 – 132	5	APAES → GPRPR in AAC67374. Ref.1
	Sequence conflict	152	1	E → G in AAH00518. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 56FFFCEA441062AB	FASTA	227	22,693
	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
	Isoform 2 [UniParc]. Checksum: 562F9FC9D05A565C	FASTA	173	17,664
	10 20 30 40 50 60 MGGKLSKKKK GYNVNDEKAK EKDKKAEGAA TEEEGTPKES EPQAAAEPAE AKEGKEKPDQ 70 80 90 100 110 120 DAEGKAEEKE GEKDAAAAKE EAPKAEPSKE EGEPKKTEAP AAPAAQETKS DGAPASDSKP 130 140 150 160 170 GSSEAAPSSK ETPAATEAPS STPKAQGPAA SAEEPKPVEA PAANSDQTVT VKE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"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.
IPI	IPI00299024. IPI00908521.
RefSeq	NP_001258535.1. NM_001271606.1. NP_006308.3. NM_006317.4.
UniGene	Hs.201641. Hs.646924. Hs.744329.
3D structure databases
ProteinModelPortal	P80723.
ModBase	Search...
Protein-protein interaction databases
IntAct	P80723. 5 interactions.
MINT	MINT-5000418.
STRING	9606.ENSP00000319281.
Protein family/group databases
TCDB	1.A.71.1.1. brain acid-soluble protein channel (BASP1 Channel) family.
PTM databases
PhosphoSite	P80723.
Polymorphism databases
DMDM	6686256.
Proteomic databases
PaxDb	P80723.
PeptideAtlas	P80723.
PRIDE	P80723.
Protocols and materials databases
DNASU	10409.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322611; ENSP00000319281; ENSG00000176788.
GeneID	10409.
KEGG	hsa:10409.
UCSC	uc003jfx.3. human.
Organism-specific databases
CTD	10409.
GeneCards	GC05P017217.
HGNC	HGNC:957. BASP1.
HPA	HPA045218.
MIM	605940. gene.
neXtProt	NX_P80723.
PharmGKB	PA25261.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG46129.
HOGENOM	HOG000095176.
InParanoid	P80723.
OMA	EDAQQTT.
OrthoDB	EOG4XPQFT.
PhylomeDB	P80723.
Gene expression databases
Bgee	P80723.
CleanEx	HS_BASP1.
Genevestigator	P80723.
GermOnline	ENSG00000176788. Homo sapiens.
Family and domain databases
InterPro	IPR008408. BASP1. [Graphical view]
PANTHER	PTHR23212. PTHR23212. 1 hit.
Pfam	PF05466. BASP1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	BASP1. human.
GenomeRNAi	10409.
NextBio	39453.
SOURCE	Search...

Entry information

Entry name

BASP1_HUMAN

Accession

Primary (citable) accession number: P80723
Secondary accession number(s): B4DJA8 , D3DTD5, O43596, Q5U0S0, Q9BWA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.