ID E9PK14_HUMAN Unreviewed; 625 AA.
AC E9PK14;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN Name=SEC16B {ECO:0000313|Ensembl:ENSP00000431727.2};
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 {ECO:0000313|Ensembl:ENSP00000431727.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000431727.2, ECO:0000313|Proteomes:UP000005640}
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., 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., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H.,
RA Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C.,
RA Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R.,
RA Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.,
RA Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.,
RA Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R.,
RA Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D.,
RA Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A.,
RA Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S.,
RA Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A.,
RA Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S.,
RA Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A.,
RA Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L.,
RA Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z.,
RA Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C.,
RA Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M.,
RA Langford C.F., Pandian R.D., Porter K.M., Prigmore E.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0000313|Ensembl:ENSP00000431727.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a role in the organization of the endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). Required for secretory cargo traffic from the endoplasmic
CC reticulum to the Golgi apparatus. {ECO:0000256|RuleBase:RU364101}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex. {ECO:0000256|RuleBase:RU364101}.
CC -!- INTERACTION:
CC E9PK14; P55735-3: SEC13; NbExp=6; IntAct=EBI-12372595, EBI-12235008;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU364101}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR EMBL; AL160007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E9PK14; -.
DR IntAct; E9PK14; 1.
DR MassIVE; E9PK14; -.
DR PeptideAtlas; E9PK14; -.
DR ProteomicsDB; 21316; -.
DR Antibodypedia; 35113; 143 antibodies from 28 providers.
DR Ensembl; ENST00000464631.6; ENSP00000431727.2; ENSG00000120341.19.
DR UCSC; uc001gll.5; human.
DR HGNC; HGNC:30301; SEC16B.
DR VEuPathDB; HostDB:ENSG00000120341; -.
DR GeneTree; ENSGT00940000160138; -.
DR HOGENOM; CLU_437394_0_0_1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000120341; Expressed in right lobe of liver and 93 other cell types or tissues.
DR ExpressionAtlas; E9PK14; baseline and differential.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:UniProt.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd09233; ACE1-Sec16-like; 1.
DR Gene3D; 1.25.40.1030; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402:SF11; PROTEIN TRANSPORT PROTEIN SEC16B; 1.
DR PANTHER; PTHR13402; RGPR-RELATED; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU364101};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU364101};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU364101}; Membrane {ECO:0000256|RuleBase:RU364101};
KW Peroxisome biogenesis {ECO:0000256|ARBA:ARBA00022593};
KW Protein transport {ECO:0000256|RuleBase:RU364101};
KW Proteomics identification {ECO:0007829|EPD:E9PK14,
KW ECO:0007829|PeptideAtlas:E9PK14};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 283..379
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 448..598
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 70782 MW; 009EE3B6791389A7 CRC64;
MELWAPQRLP QTRGKATAPS KDPDRGFRRD GHHRPVPHSW HNGERFHQWQ DNRGSPQPQQ
EPRADHQQQP HYASRPGDWH QPVSGVDYYE GGYRNQLYSR PGYENSYQSY QSPTMREEYA
YGSYYYHGHP QWLQEERVPR QRSPYIWHED YREQKYLDEH HYENQHSPFG TNSETHFQSN
SRNPCKDSPA SNSGQEWPGE LFPGSLLAEA QKNKPSLASE SNLLQQRESG LSSSSYELSQ
YIRDAPERDD PPASAAWSPV QAEDVSSAGP KAPMKFYIPH VPVSFGPGGQ LVHVGPSSPT
DGQAALVELH SMEVILNDSE EQEEMRSFSG PLIREDVHKV DIMTFCQQKA AQSCKSETLG
SRDSALLWQL LVLLCRQNGS MVGSDIAELL MQDCKKLEKY KRQPPVANLI NLTDEDWPVL
SSGTPNLLTG EIPPSVETPA QIVEKFTRLL YYGRKKEALE WAMKNHLWGH ALFLSSKMDP
QTYSWVMSGF TSTLALNDPL QTLFQLMSGR IPQAATCCGE KQWGDWRPHL AVILSNQAGD
PELYQRAIVA IGDTLAGKGL VEAAHFCYLM AHVPFGHYTV KTDHLVLLGS SHRYATWEKG
NSKDIFQGTV LALVGFYGSI FHFLM
//
