Reviewed, UniProtKB/Swiss-Prot O75396 (SC22B_HUMAN)

Names and origin

Protein names

Recommended name:
    Vesicle-trafficking protein SEC22b
Alternative name(s):
    SEC22 vesicle-trafficking protein homolog B
    SEC22 vesicle-trafficking protein-like 1
    ERS24
    ERS-24

Gene names

Name:	SEC22B
Synonyms:	SEC22L1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	215 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)

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. Ref.5
Subunit structure	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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9
Sequence similarities	Belongs to the synaptobrevin family. Contains 1 longin domain. Contains 1 v-SNARE coiled-coil homology domain.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Transmembrane
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ER to Golgi vesicle-mediated transport Traceable author statement. Source: ProtInc protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ER-Golgi intermediate compartment membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.5 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 215

214

Vesicle-trafficking protein SEC22b

PRO_0000206770

Regions

Topological domain

2 – 194

193

Cytoplasmic Potential

Transmembrane

195 – 215

21

Anchor for type IV membrane protein Potential

Domain

6 – 119

114

Longin

Domain

134 – 194

61

v-SNARE coiled-coil homology

Amino acid modifications

Modified residue

35

1

Phosphoserine Ref.7

Modified residue

48

1

Phosphoserine Ref.8

Modified residue

137

1

Phosphoserine Ref.8 Ref.9

Modified residue

168

1

Phosphoserine By similarity

Natural variations

Natural variant

108

1

R → Q: dbSNP rs2655551.

VAR_057343

Natural variant

214

1

W → C: dbSNP rs7534444.

VAR_057344

Secondary structure

1

.

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215

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Turn

10 – 12

3

Beta strand

15 – 19

5

Helix

30 – 43

14

Beta strand

50 – 56

7

Beta strand

59 – 66

8

Beta 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

Beta strand

150 – 152

3

Helix

153 – 156

4

Sequences

	Sequence		Length	Mass (Da)
	O75396-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 29B4C55961C5A044	FASTA	215	24,741
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning." 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. Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed: 9653160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Caudate nucleus.
[3]	"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: Skin.
[4]	Bienvenut W.V., Claeys D. Submitted (NOV-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-9; 29-38 AND 134-147, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Platelet.
[5]	"Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion." Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K., Nagahama M., Tani K., Yamamoto A., Tagaya M. EMBO J. 23:3216-3226(2004) [PubMed: 15272311] [Abstract] Cited for: FUNCTION, INTERACTION WITH BNIP1, STX18 AND USE1L.
[6]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." 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. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-137, MASS SPECTROMETRY.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF047442 mRNA. Translation: AAC39893.1.
AK289875 mRNA. Translation: BAF82564.1.
BC001364 mRNA. Translation: AAH01364.1.

IPI

IPI00006865.

RefSeq

NP_004883.2.

UniGene

Hs.632438

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NUP	X-ray	2.80	C	1-195	[»]
2NUT	X-ray	2.30	C	1-195	[»]
3EGD	X-ray	2.70	C	1-157	[»]
3EGX	X-ray	3.30	C	1-157	[»]

ModBase

Search...

PTM databases

PhosphoSite

O75396.

Proteomic databases

PeptideAtlas

O75396.

PRIDE

O75396.

Genome annotation databases

GeneID

9554.

KEGG

hsa:9554.

Organism-specific databases

GeneCards

GC01P143807.

HGNC

HGNC:10700. SEC22B.

MIM

604029. gene.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O75396.

Gene expression databases

CleanEx

HS_SEC22B.

Family and domain databases

InterPro

IPR010908. Longin.
IPR001388. Synaptobrevin.
[Graphical view]

Pfam

PF00957. Synaptobrevin. 1 hit.
[Graphical view]

PRINTS

PR00219. SYNAPTOBREVN.

PROSITE

PS50859. LONGIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

35831.

SOURCE

Search...

Entry information

Entry name

SC22B_HUMAN

Accession

Primary (citable) accession number: O75396
Secondary accession number(s): A8K1G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)