SC22B_HUMAN
ID SC22B_HUMAN Reviewed; 215 AA.
AC O75396; A8K1G0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 5.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Vesicle-trafficking protein SEC22b;
DE AltName: Full=ER-Golgi SNARE of 24 kDa;
DE Short=ERS-24;
DE Short=ERS24;
DE AltName: Full=SEC22 vesicle-trafficking protein homolog B;
DE AltName: Full=SEC22 vesicle-trafficking protein-like 1;
GN Name=SEC22B; Synonyms=SEC22L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-9; 29-38 AND 134-147, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [6]
RP FUNCTION, AND INTERACTION WITH BNIP1; STX18 AND USE1L.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; THR-140 AND SER-177, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-164; SER-168;
RP SER-174 AND SER-177, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-168, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17] {ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2NUT}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-195 IN COMPLEX WITH SEC23A AND
RP SEC24A, AND INTERACTION WITH SEC23A AND SEC24A.
RX PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
RA Mancias J.D., Goldberg J.;
RT "The transport signal on Sec22 for packaging into COPII-coated vesicles is
RT a conformational epitope.";
RL Mol. Cell 26:403-414(2007).
RN [18] {ECO:0007744|PDB:3EGD, ECO:0007744|PDB:3EGX}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-157 IN COMPLEX WITH SEC23A AND
RP SEC24A, AND INTERACTION WITH SEC23A AND SEC24A.
RX PubMed=18843296; DOI=10.1038/emboj.2008.208;
RA Mancias J.D., Goldberg J.;
RT "Structural basis of cargo membrane protein discrimination by the human
RT COPII coat machinery.";
RL EMBO J. 27:2918-2928(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: SNARE involved in targeting and fusion of ER-derived
CC transport vesicles with the Golgi complex as well as Golgi-derived
CC retrograde transport vesicles with the ER.
CC {ECO:0000269|PubMed:15272311}.
CC -!- SUBUNIT: Interacts with STX17 (By similarity). Component of two
CC distinct SNARE complexes consisting of STX5, GOSR2/BOS1, BET1 and
CC SEC22B or STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably
CC replace SEC22B in either complex. Interacts with the COPII Sec23/24
CC complex composed of SEC23A and SEC24A; recruits SEC22B into COPII-
CC coated vesicles to allow its transport from the endoplasmic reticulum
CC to the Golgi (PubMed:17499046, PubMed:18843296).
CC {ECO:0000250|UniProtKB:Q4KM74, ECO:0000269|PubMed:15272311,
CC ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296}.
CC -!- INTERACTION:
CC O75396; O95870: ABHD16A; NbExp=3; IntAct=EBI-1058865, EBI-348517;
CC O75396; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-1058865, EBI-11957045;
CC O75396; Q13520: AQP6; NbExp=3; IntAct=EBI-1058865, EBI-13059134;
CC O75396; P11912: CD79A; NbExp=3; IntAct=EBI-1058865, EBI-7797864;
CC O75396; Q6ZMG9-2: CERS6; NbExp=3; IntAct=EBI-1058865, EBI-18038706;
CC O75396; O95471: CLDN7; NbExp=3; IntAct=EBI-1058865, EBI-740744;
CC O75396; P58418: CLRN1; NbExp=3; IntAct=EBI-1058865, EBI-17274839;
CC O75396; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-1058865, EBI-18013275;
CC O75396; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1058865, EBI-6942903;
CC O75396; Q9P2X0-2: DPM3; NbExp=3; IntAct=EBI-1058865, EBI-10962476;
CC O75396; Q15125: EBP; NbExp=3; IntAct=EBI-1058865, EBI-3915253;
CC O75396; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-1058865, EBI-18535450;
CC O75396; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1058865, EBI-781551;
CC O75396; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-1058865, EBI-18636064;
CC O75396; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-1058865, EBI-18304435;
CC O75396; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-1058865, EBI-12142257;
CC O75396; P48165: GJA8; NbExp=3; IntAct=EBI-1058865, EBI-17458373;
CC O75396; O95377: GJB5; NbExp=3; IntAct=EBI-1058865, EBI-3909454;
CC O75396; O95452: GJB6; NbExp=3; IntAct=EBI-1058865, EBI-13345609;
CC O75396; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-1058865, EBI-3917143;
CC O75396; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-1058865, EBI-13345167;
CC O75396; Q8TED1: GPX8; NbExp=3; IntAct=EBI-1058865, EBI-11721746;
CC O75396; P31937: HIBADH; NbExp=3; IntAct=EBI-1058865, EBI-11427100;
CC O75396; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-1058865, EBI-1052304;
CC O75396; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-1058865, EBI-18053395;
CC O75396; P38484: IFNGR2; NbExp=3; IntAct=EBI-1058865, EBI-3905457;
CC O75396; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-1058865, EBI-10266796;
CC O75396; P43628: KIR2DL3; NbExp=3; IntAct=EBI-1058865, EBI-8632435;
CC O75396; Q86WI0: LHFPL1; NbExp=3; IntAct=EBI-1058865, EBI-18268016;
CC O75396; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-1058865, EBI-2820517;
CC O75396; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-1058865, EBI-11956541;
CC O75396; Q6N075: MFSD5; NbExp=3; IntAct=EBI-1058865, EBI-3920969;
CC O75396; Q99735: MGST2; NbExp=3; IntAct=EBI-1058865, EBI-11324706;
CC O75396; O14880: MGST3; NbExp=3; IntAct=EBI-1058865, EBI-724754;
CC O75396; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-1058865, EBI-6163737;
CC O75396; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-1058865, EBI-750085;
CC O75396; Q8N183: NDUFAF2; NbExp=3; IntAct=EBI-1058865, EBI-2682365;
CC O75396; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-1058865, EBI-7545592;
CC O75396; Q8NC24: RELL2; NbExp=3; IntAct=EBI-1058865, EBI-10269209;
CC O75396; Q8TEB9: RHBDD1; NbExp=3; IntAct=EBI-1058865, EBI-9916444;
CC O75396; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-1058865, EBI-17295964;
CC O75396; Q9P2W9: STX18; NbExp=3; IntAct=EBI-1058865, EBI-725334;
CC O75396; Q16623: STX1A; NbExp=3; IntAct=EBI-1058865, EBI-712466;
CC O75396; P32856-2: STX2; NbExp=3; IntAct=EBI-1058865, EBI-11956649;
CC O75396; Q12846: STX4; NbExp=4; IntAct=EBI-1058865, EBI-744942;
CC O75396; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-1058865, EBI-12947623;
CC O75396; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-1058865, EBI-6448756;
CC O75396; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-1058865, EBI-7238458;
CC O75396; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-1058865, EBI-17684533;
CC O75396; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-1058865, EBI-12195227;
CC O75396; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-1058865, EBI-2548832;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q4KM74}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q4KM74}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi
CC apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}.
CC Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q4KM74}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Note=Concentrated most in the
CC intermediate compartment/cis-Golgi network and the cis-Golgi cisternae
CC 1 and 2. Greatly reduced in concentration at the trans end of the Golgi
CC apparatus (By similarity). Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV (PubMed:17081065).
CC {ECO:0000250|UniProtKB:Q4KM74, ECO:0000269|PubMed:17081065}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF047442; AAC39893.1; -; mRNA.
DR EMBL; AK289875; BAF82564.1; -; mRNA.
DR EMBL; AC245008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001364; AAH01364.1; -; mRNA.
DR CCDS; CCDS83523.1; -.
DR RefSeq; NP_004883.3; NM_004892.5.
DR PDB; 2NUP; X-ray; 2.80 A; C=1-195.
DR PDB; 2NUT; X-ray; 2.30 A; C=1-195.
DR PDB; 3EGD; X-ray; 2.70 A; C=1-157.
DR PDB; 3EGX; X-ray; 3.30 A; C=1-157.
DR PDBsum; 2NUP; -.
DR PDBsum; 2NUT; -.
DR PDBsum; 3EGD; -.
DR PDBsum; 3EGX; -.
DR AlphaFoldDB; O75396; -.
DR SMR; O75396; -.
DR BioGRID; 114926; 340.
DR DIP; DIP-50458N; -.
DR IntAct; O75396; 157.
DR MINT; O75396; -.
DR STRING; 9606.ENSP00000463393; -.
DR ChEMBL; CHEMBL4295679; -.
DR GlyConnect; 1891; 2 N-Linked glycans (1 site).
DR GlyGen; O75396; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; O75396; -.
DR MetOSite; O75396; -.
DR PhosphoSitePlus; O75396; -.
DR SwissPalm; O75396; -.
DR BioMuta; SEC22B; -.
DR CPTAC; CPTAC-129; -.
DR CPTAC; CPTAC-130; -.
DR EPD; O75396; -.
DR jPOST; O75396; -.
DR MassIVE; O75396; -.
DR MaxQB; O75396; -.
DR PeptideAtlas; O75396; -.
DR PRIDE; O75396; -.
DR ProteomicsDB; 49967; -.
DR TopDownProteomics; O75396; -.
DR Antibodypedia; 72298; 212 antibodies from 24 providers.
DR DNASU; 9554; -.
DR Ensembl; ENST00000578049.4; ENSP00000463393.1; ENSG00000265808.4.
DR GeneID; 9554; -.
DR KEGG; hsa:9554; -.
DR MANE-Select; ENST00000578049.4; ENSP00000463393.1; NM_004892.6; NP_004883.3.
DR UCSC; uc031unv.2; human.
DR CTD; 9554; -.
DR DisGeNET; 9554; -.
DR GeneCards; SEC22B; -.
DR HGNC; HGNC:10700; SEC22B.
DR HPA; ENSG00000265808; Low tissue specificity.
DR MIM; 604029; gene.
DR neXtProt; NX_O75396; -.
DR OpenTargets; ENSG00000265808; -.
DR PharmGKB; PA35623; -.
DR VEuPathDB; HostDB:ENSG00000265808; -.
DR eggNOG; KOG0862; Eukaryota.
DR GeneTree; ENSGT00940000156349; -.
DR HOGENOM; CLU_054453_4_1_1; -.
DR InParanoid; O75396; -.
DR OrthoDB; 903466at2759; -.
DR PhylomeDB; O75396; -.
DR PathwayCommons; O75396; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; O75396; -.
DR SIGNOR; O75396; -.
DR BioGRID-ORCS; 9554; 25 hits in 128 CRISPR screens.
DR ChiTaRS; SEC22B; human.
DR EvolutionaryTrace; O75396; -.
DR GeneWiki; SEC22B; -.
DR GenomeRNAi; 9554; -.
DR Pharos; O75396; Tbio.
DR PRO; PR:O75396; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75396; protein.
DR Bgee; ENSG00000265808; Expressed in calcaneal tendon and 135 other tissues.
DR ExpressionAtlas; O75396; baseline and differential.
DR Genevisible; O75396; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR CDD; cd14824; Longin; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR044565; Sec22.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45837; PTHR45837; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:25944712"
FT CHAIN 2..215
FT /note="Vesicle-trafficking protein SEC22b"
FT /id="PRO_0000206770"
FT TOPO_DOM 2..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 6..119
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 134..194
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 100..105
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:3EGD"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2NUT"
SQ SEQUENCE 215 AA; 24741 MW; 29B4C55961C5A044 CRC64;
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT
FHYIIEQGVC YLVLCEAAFP KKLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ
KTKKLYIDSR ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY
RQDAKYLNMR STYAKLAAVA VFFIMLIVYV RFWWL
