Q9H115 (SNAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-soluble NSF attachment protein
Short name=SNAP-beta

Alternative name(s):
N-ethylmaleimide-sensitive factor attachment protein beta

Gene names

Name:	NAPB
Synonyms:	SNAPB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus By similarity.
Subunit structure	Interacts with PRKCABP, and disrupts the interaction between GRIA2 and PRKCABP, leading to the internalization of GRIA2 By similarity.
Subcellular location	Membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the SNAP family.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular protein transport Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 298	298	Beta-soluble NSF attachment protein		PRO_0000219060
Amino acid modifications
	Modified residue	203	1	N6-acetyllysine Ref.4
Natural variations
	Natural variant	61	1	A → T. Corresponds to variant rs6036399 [ dbSNP | Ensembl ].		VAR_052026

Sequences

	Sequence		Length	Mass (Da)
	Q9H115 [UniParc]. Last modified August 29, 2001. Version 2. Checksum: 5B7BE0FB84BABD83	FASTA	298	33,557
	10 20 30 40 50 60 MDNAGKEREA VQLMAEAEKR VKASHSFLRG LFGGNTRIEE ACEMYTRAAN MFKMAKNWSA 70 80 90 100 110 120 AGNAFCQAAK LHMQLQSKHD SATSFVDAGN AYKKADPQEA INCLNAAIDI YTDMGRFTIA 130 140 150 160 170 180 AKHHITIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAA YAAQLEQYQK 190 200 210 220 230 240 AIEIYEQVGA NTMDNPLLKY SAKDYFFKAA LCHFIVDELN AKLALEKYEE MFPAFTDSRE 250 260 270 280 290 CKLLKKLLEA HEEQNSEAYT EAVKEFDSIS RLDQWLTTML LRIKKSIQGD GEGDGDLK

References

[1]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-298. Tissue: Amygdala.
[4]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-203, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL096677 Genomic DNA. Translation: CAI20156.1. BC060840 mRNA. Translation: AAH60840.1. AL834445 mRNA. Translation: CAD39105.1.
IPI	IPI00942239.
RefSeq	NP_071363.1. NM_022080.2.
UniGene	Hs.269471.
3D structure databases
ProteinModelPortal	Q9H115.
SMR	Q9H115. Positions 9-293.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H115. 1 interaction.
STRING	Q9H115.
PTM databases
PhosphoSite	Q9H115.
Polymorphism databases
DMDM	18202933.
Proteomic databases
PRIDE	Q9H115.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377026; ENSP00000366225; ENSG00000125814.
GeneID	63908.
KEGG	hsa:63908.
UCSC	uc002wta.1. human.
Organism-specific databases
CTD	63908.
GeneCards	GC20M023355.
H-InvDB	HIX0015692.
HGNC	HGNC:15751. NAPB.
HPA	CAB037227.
MIM	611270. gene.
neXtProt	NX_Q9H115.
PharmGKB	PA31444.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000005826.
HOVERGEN	HBG001325.
InParanoid	Q9H115.
OrthoDB	EOG428227.
PhylomeDB	Q9H115.
Gene expression databases
ArrayExpress	Q9H115.
Bgee	Q9H115.
CleanEx	HS_NAPB.
Genevestigator	Q9H115.
GermOnline	ENSG00000125814. Homo sapiens.
Family and domain databases
InterPro	IPR000744. NSF_attach. IPR011990. TPR-like_helical. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PANTHER	PTHR13768. NSF_attach. 1 hit.
PRINTS	PR00448. NSFATTACHMNT.
ProtoNet	Search...
Other
NextBio	65622.
SOURCE	Search...

Entry information

Entry name

SNAB_HUMAN

Accession

Primary (citable) accession number: Q9H115
Secondary accession number(s): Q4G187, Q5JXF9, Q8N3C4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	August 29, 2001
Last modified:	January 25, 2012
This is version 84 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.