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UniProtKB/Swiss-Prot entry O75396


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SC22B_HUMAN
Primary accession number O75396
Secondary accession number A8K1G0
Integrated into Swiss-Prot on March 29, 2004
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 78)
Name and origin of the protein
Protein name Vesicle-trafficking protein SEC22b
Synonyms SEC22 vesicle-trafficking protein homolog B
SEC22 vesicle-trafficking protein-like 1
ERS24
ERS-24
Gene name
Name: SEC22B
Synonyms: SEC22L1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
DOI=10.1073/pnas.95.14.8175; PubMed=9653160 [NCBI, ExPASy, EBI, Israel, Japan]
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.;
"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Caudate nucleus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
PROTEIN SEQUENCE OF 2-9; 29-38 AND 134-147, CLEAVAGE OF INITIATOR METHIONINE, AND MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[5]
FUNCTION, AND INTERACTION WITH BNIP1, STX18 AND USE1L.
DOI=10.1038/sj.emboj.7600333; PubMed=15272311 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K., Nagahama M., Tani K., Yamamoto A., Tagaya M.;
"Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion.";
EMBO J. 23:3216-3226(2004).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-137, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
  • SUBUNIT: Component of two distinct SNARE complexes consisting of STX5, GOSR2/BOS1, BET1 and SEC22B or STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably replace SEC22B in either complex.
  • SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type IV membrane protein (By similarity). Golgi apparatus membrane; Single-pass type IV membrane protein (By similarity). Endoplasmic reticulum membrane; Single-pass type IV membrane protein (By similarity). Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
  • SIMILARITY: Belongs to the synaptobrevin family.
  • SIMILARITY: Contains 1 longin domain.
  • SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF047442; AAC39893.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK289875; BAF82564.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001364; AAH01364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00006865; -.
RefSeq NP_004883.2; -.
UniGene Hs.632438
3D structure databases
PDB
2NUP; X-ray; 2.80 A; C=1-195.[ExPASy / RCSB / EBI]
2NUT; X-ray; 2.30 A; C=1-195.[ExPASy / RCSB / EBI]
3EGD; X-ray; 2.70 A; C=1-157.[ExPASy / RCSB / EBI]
3EGX; X-ray; 3.30 A; C=1-157.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2NUP; -.
2NUT; -.
3EGD; -.
3EGX; -.
ModBase O75396.
PTM databases
PhosphoSite O75396; -.
Organism-specific databases
GeneCards GC01P143807; -.
HGNC HGNC:10700; SEC22B.
GenAtlas SEC22B.
MIM 604029; gene. [NCBI / EBI]
Gene expression databases
CleanEx HS_SEC22B; -.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0033116; Cellular component: ER-Golgi intermediate compartment membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000139; Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006888; Biological process: ER to Golgi vesicle-mediated transport (traceable author statement from ProtInc).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR010908; Longin.
IPR001388; Synaptobrevin.
Graphical view of domain structure.
Pfam PF00957; Synaptobrevin; 1.
Pfam graphical view of domain structure.
PRINTS PR00219; SYNAPTOBREVN.
PROSITE PS50859; LONGIN; 1.
PS50892; V_SNARE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas O75396; -.
PRIDE O75396; -.
Genome annotation databases
GeneID 9554; -.
KEGG hsa:9554; -.
Phylogenomic databases
HOVERGEN O75396; -.
Other
NextBio 35831; -.
SOURCE SEC22B; Homo sapiens.
ProtoNet O75396.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Coiled coil; Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism; Protein transport; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   215  214     Vesicle-trafficking protein SEC22b. PRO_0000206770
TOPO_DOM   2   194  193     Cytoplasmic (Potential). 
TRANSMEM   195   215  21     Anchor for type IV membrane protein (Potential). 
DOMAIN   6   119  114     Longin. 
DOMAIN   134   194  61     v-SNARE coiled-coil homology. 
MOD_RES   35    35        Phosphoserine. 
MOD_RES   48    48        Phosphoserine. 
MOD_RES   137   137        Phosphoserine. 
MOD_RES   168   168        Phosphoserine (By similarity). 
VARIANT   108   108  1     R -> Q (in dbSNP:rs2655551 [NCBI]). VAR_057343 [3D]
VARIANT   214   214  1     W -> C (in dbSNP:rs7534444 [NCBI]). VAR_057344 
STRAND   5     9  5      
TURN   10    12  3      
STRAND   15    19  5      
HELIX   30    43  14      
STRAND   50    56  7      
STRAND   59    66  8      
STRAND   69    76  8      
HELIX   81    99  19      
TURN   100   105  6      
TURN   109   112  4      
HELIX   113   115  3      
HELIX   116   123  8      
TURN   124   126  3      
STRAND   150   152  3      
HELIX   153   156  4      
Sequence information
Length: 215 AA [This is the length of the unprocessed precursor] Molecular weight: 24741 Da [This is the MW of the unprocessed precursor] CRC64: 29B4C55961C5A044 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT 

        70         80         90        100        110        120 
FHYIIEQGVC YLVLCEAAFP KKLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ 

       130        140        150        160        170        180 
KTKKLYIDSR ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY 

       190        200        210 
RQDAKYLNMR STYAKLAAVA VFFIMLIVYV RFWWL 

O75396 in FASTA format

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