SEC16A

Protein transport protein Sec16A is a protein that in humans is encoded by the SEC16A gene.[5][6]

SEC16A
Identifiers
Aliases	SEC16A, KIAA0310, SEC16L, p250, SEC16 homolog A, endoplasmic reticulum export factor
External IDs	OMIM: 612854 MGI: 2139207 HomoloGene: 10533 GeneCards: SEC16A
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q34.3 Start 136,440,096 bp[1] End 136,483,759 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 A3 Start 26,409,431 bp[2] End 26,445,216 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding Cellular component • cytosol • Golgi membrane • Golgi apparatus • endoplasmic reticulum membrane • membrane • endoplasmic reticulum • cytoplasm • ER to Golgi transport vesicle membrane • organelle membrane • intracellular membrane-bounded organelle • perinuclear region of cytoplasm • endoplasmic reticulum exit site Biological process • protein transport • COPII vesicle coating • substantia nigra development • vesicle-mediated transport • endoplasmic reticulum organization • transport • ER to Golgi vesicle-mediated transport • Golgi organization • protein exit from endoplasmic reticulum • response to endoplasmic reticulum stress • Golgi to plasma membrane CFTR protein transport • protein stabilization • positive regulation of protein exit from endoplasmic reticulum • protein localization to endoplasmic reticulum exit site • protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9919	227648
Ensembl	ENSG00000148396	ENSMUSG00000026924
UniProt	O15027	E9QAT4
RefSeq (mRNA)	NM_001276418 NM_014866	NM_153125
RefSeq (protein)	NP_001263347 NP_055681	NP_694765
Location (UCSC)	Chr 9: 136.44 – 136.48 Mb	Chr 2: 26.41 – 26.45 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000148396 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026924 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (April 1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841.
6. "Entrez Gene: KIAA0310 KIAA0310".

Further reading

• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (June 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. CiteSeerX 10.1.1.500.923. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Iinuma T, Shiga A, Nakamoto K, O'Brien MB, Aridor M, Arimitsu N, Tagaya M, Tani K (June 2007). "Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum". The Journal of Biological Chemistry. 282 (24): 17632–9. doi:10.1074/jbc.M611237200. PMID 17428803.
• Bhattacharyya D, Glick BS (March 2007). "Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization". Molecular Biology of the Cell. 18 (3): 839–49. doi:10.1091/mbc.E06-08-0707. PMC 1805085. PMID 17192411.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Watson P, Townley AK, Koka P, Palmer KJ, Stephens DJ (December 2006). "Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells". Traffic. 7 (12): 1678–87. doi:10.1111/j.1600-0854.2006.00493.x. PMC 1761133. PMID 17005010.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.