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Protein

Protein transport protein Sec16A

Gene

SEC16A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Defines endoplasmic reticulum exit sites (ERES) and is required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for normal transitional endoplasmic reticulum (tER) organization.2 Publications

GO - Biological processi

  • COPII vesicle coating Source: Reactome
  • endoplasmic reticulum organization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • substantia nigra development Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
SIGNORiO15027.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein Sec16A
Alternative name(s):
SEC16 homolog A
Gene namesi
Name:SEC16A
Synonyms:KIAA0310, SEC16, SEC16L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:29006. SEC16A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: HPA
  • Golgi membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162402611.

Polymorphism and mutation databases

BioMutaiSEC16A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21792179Protein transport protein Sec16APRO_0000050746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei136 – 1361PhosphoserineCombined sources
Modified residuei153 – 1531PhosphoserineCombined sources
Modified residuei381 – 3811PhosphoserineCombined sources
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei411 – 4111PhosphoserineCombined sources
Modified residuei414 – 4141PhosphoserineCombined sources
Modified residuei415 – 4151PhosphothreonineCombined sources
Modified residuei417 – 4171PhosphoserineCombined sources
Modified residuei891 – 8911PhosphoserineCombined sources
Modified residuei1029 – 10291PhosphoserineCombined sources
Modified residuei1051 – 10511PhosphoserineCombined sources
Modified residuei1127 – 11271PhosphoserineCombined sources
Modified residuei1147 – 11471PhosphothreonineCombined sources
Modified residuei1149 – 11491PhosphoserineCombined sources
Modified residuei1169 – 11691PhosphoserineCombined sources
Modified residuei1172 – 11721PhosphoserineCombined sources
Modified residuei1178 – 11781PhosphoserineCombined sources
Modified residuei1181 – 11811PhosphoserineCombined sources
Modified residuei1184 – 11841PhosphoserineCombined sources
Modified residuei1191 – 11911PhosphoserineCombined sources
Modified residuei1395 – 13951PhosphoserineCombined sources
Modified residuei1423 – 14231PhosphoserineCombined sources
Modified residuei1729 – 17291PhosphothreonineCombined sources
Modified residuei1761 – 17611PhosphoserineCombined sources
Modified residuei1786 – 17861PhosphoserineCombined sources
Modified residuei1844 – 18441PhosphoserineCombined sources
Modified residuei1864 – 18641PhosphoserineCombined sources
Modified residuei1876 – 18761PhosphothreonineCombined sources
Modified residuei1878 – 18781PhosphoserineCombined sources
Modified residuei1895 – 18951PhosphoserineCombined sources
Modified residuei1905 – 19051PhosphoserineCombined sources
Modified residuei2093 – 20931PhosphoserineCombined sources
Modified residuei2113 – 21131PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO15027.
MaxQBiO15027.
PaxDbiO15027.
PeptideAtlasiO15027.
PRIDEiO15027.

PTM databases

iPTMnetiO15027.
PhosphoSiteiO15027.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at higher levels in the pancreas.1 Publication

Gene expression databases

BgeeiO15027.
CleanExiHS_SEC16A.
ExpressionAtlasiO15027. baseline and differential.
GenevisibleiO15027. HS.

Organism-specific databases

HPAiHPA005684.

Interactioni

Subunit structurei

SEC16A and SEC16B are each present in multiple copies in a heteromeric complex. Interacts with SEC23A.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0076EBI-357515,EBI-5323863

Protein-protein interaction databases

BioGridi115247. 149 interactions.
DIPiDIP-27588N.
IntActiO15027. 111 interactions.
MINTiMINT-1155646.
STRINGi9606.ENSP00000325827.

Structurei

3D structure databases

ProteinModelPortaliO15027.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni924 – 1227304Required for endoplasmic reticulum localizationAdd
BLAST
Regioni1928 – 2179252Required for interaction with SEC23AAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi935 – 100369Pro-richAdd
BLAST
Compositional biasi981 – 9844Poly-Tyr
Compositional biasi1413 – 14164Poly-Glu
Compositional biasi1753 – 2107355Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the SEC16 family.Curated

Phylogenomic databases

eggNOGiKOG1913. Eukaryota.
ENOG4111J6D. LUCA.
GeneTreeiENSGT00530000063746.
HOVERGENiHBG079941.
InParanoidiO15027.
OrthoDBiEOG7MH0XQ.
PhylomeDBiO15027.

Family and domain databases

InterProiIPR024298. ACE1_Sec16_Sec31.
IPR024880. Sec16.
IPR024340. Sec16_CCD.
[Graphical view]
PANTHERiPTHR13402. PTHR13402. 2 hits.
PfamiPF12932. Sec16. 1 hit.
PF12931. Sec16_C. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15027-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPGLDRPLSR QNPHDGVVTP AASPSLPQPG LQMPGQWGPV QGGPQPSGQH
60 70 80 90 100
RSPCPEGPVP SGVPCATSVP HFPTPSILHQ GPGHEQHSPL VAPPAALPSD
110 120 130 140 150
GRDEVSHLQS GSHLANNSDP ESTFRQNPRI VNHWASPELR QNPGVKNEHR
160 170 180 190 200
PASALVNPLA RGDSPENRTH HPLGAGAGSG CAPLEADSGA SGALAMFFQG
210 220 230 240 250
GETENEENLS SEKAGLSGQA DFDDFCSSPG LGRPPAPTHV GAGSLCQALL
260 270 280 290 300
PGPSNEAAGD VWGDTASTGV PDASGSQYEN VENLEFVQNQ EVLPSEPLNL
310 320 330 340 350
DPSSPSDQFR YGPLPGPAVP RHGAVCHTGA PDATLHTVHP DSVSSSYSSR
360 370 380 390 400
SHGRLSGSAR PQELVGTFIQ QEVGKPEDEA SGSFFKQIDS SPVGGETDET
410 420 430 440 450
TVSQNYRGSV SQPSTPSPPK PTGIFQTSAN SSFEPVKSHL VGVKPFEADR
460 470 480 490 500
ANVVGEVRET CVRQKQCRPA AALPDASPGN LEQPPDNMET LCAPQVCPLP
510 520 530 540 550
LNSTTEAVHM LPHAGAPPLD TVYPAPEKRP SARTQGPVKC ESPATTLWAQ
560 570 580 590 600
SELPDFGGNV LLAPAAPALY VCAKPQPPVV QPPEEAMSGQ QSRNPSSAAP
610 620 630 640 650
VQSRGGIGAS ENLENPPKMG EEEALQSQAS SGYASLLSSP PTESLQNPPV
660 670 680 690 700
LIAQPDHSYN LAQPINFSVS LSNSHEKNQS WREALVGDRP AVSSWALGGD
710 720 730 740 750
SGENTSLSGI PTSSVLSLSL PSSVAQSNFP QGSGASEMVS NQPANLLVQP
760 770 780 790 800
PSQPVPENLV PESQKDRKAG SALPGFANSP AGSTSVVLVP PAHGTLVPDG
810 820 830 840 850
NKANHSSHQE DTYGALDFTL SRTLENPVNV YNPSHSDSLA SQQSVASHPR
860 870 880 890 900
QSGPGAPNLD RFYQQVTKDA QGQPGLERAQ QELVPPQQQA SPPQLPKAMF
910 920 930 940 950
SELSNPESLP AQGQAQNSAQ SPASLVLVDA GQQLPPRPPQ SSSVSLVSSG
960 970 980 990 1000
SGQAAVPSEQ PWPQPVPALA PGPPPQDLAA YYYYRPLYDA YQPQYSLPYP
1010 1020 1030 1040 1050
PEPGAASLYY QDVYSLYEPR YRPYDGAASA YAQNYRYPEP ERPSSRASHS
1060 1070 1080 1090 1100
SERPPPRQGY PEGYYSSKSG WSSQSDYYAS YYSSQYDYGD PGHWDRYHYS
1110 1120 1130 1140 1150
ARVRDPRTYD RRYWCDAEYD AYRREHSAFG DRPEKRDNNW RYDPRFTGSF
1160 1170 1180 1190 1200
DDDPDPHRDP YGEEVDRRSV HSEHSARSLH SAHSLASRRS SLSSHSHQSQ
1210 1220 1230 1240 1250
IYRSHNVAAG SYEAPLPPGS FHGDFAYGTY RSNFSSGPGF PEYGYPADTV
1260 1270 1280 1290 1300
WPAMEQVSSR PTSPEKFSVP HVCARFGPGG QLIKVIPNLP SEGQPALVEV
1310 1320 1330 1340 1350
HSMEALLQHT SEQEEMRAFP GPLAKDDTHK VDVINFAQNK AMKCLQNENL
1360 1370 1380 1390 1400
IDKESASLLW NFIVLLCRQN GTVVGTDIAE LLLRDHRTVW LPGKSPNEAN
1410 1420 1430 1440 1450
LIDFTNEAVE QVEEEESGEA QLSFLTGGPA AAASSLERET ERFRELLLYG
1460 1470 1480 1490 1500
RKKDALESAM KNGLWGHALL LASKMDSRTH ARVMTRFANS LPINDPLQTV
1510 1520 1530 1540 1550
YQLMSGRMPA ASTCCGDEKW GDWRPHLAMV LSNLNNNMDV ESRTMATMGD
1560 1570 1580 1590 1600
TLASRGLLDA AHFCYLMAQA GFGVYTKKTT KLVLIGSNHS LPFLKFATNE
1610 1620 1630 1640 1650
AIQRTEAYEY AQSLGAETCP LPSFQVFKFI YSCRLAEMGL ATQAFHYCEA
1660 1670 1680 1690 1700
IAKSILTQPH LYSPVLISQL VQMASQLRLF DPQLKEKPEE ESLAAPTWLV
1710 1720 1730 1740 1750
HLQQVERQIK EGAGVWHQDG ALPQQCPGTP SSEMEQLDRP GLSQPGALGI
1760 1770 1780 1790 1800
ANPLLAVPAP SPEHSSPSVR LLPSAPQTLP DGPLASPARV PMFPVPLPPG
1810 1820 1830 1840 1850
PLEPGPGCVT PGPALGFLEP SGPGLPPGVP PLQERRHLLQ EARSPDPGIV
1860 1870 1880 1890 1900
PQEAPVGNSL SELSEENFDG KFANLTPSRT VPDSEAPPGW DRADSGPTQP
1910 1920 1930 1940 1950
PLSLSPAPET KRPGQAAKKE TKEPKKGESW FFRWLPGKKK TEAYLPDDKN
1960 1970 1980 1990 2000
KSIVWDEKKN QWVNLNEPEE EKKAPPPPPT SMPKTVQAAP PALPGPPGAP
2010 2020 2030 2040 2050
VNMYSRRAAG TRARYVDVLN PSGTQRSEPA LAPADFVAPL APLPIPSNLF
2060 2070 2080 2090 2100
VPTPDAEEPQ LPDGTGREGP AAARGLANPE PAPEPKVLSS AASLPGSELP
2110 2120 2130 2140 2150
SSRPEGSQGG ELSRCSSMSS LSREVSQHFN QAPGDLPAAG GPPSGAMPFY
2160 2170
NPAQLAQACA TSGSSRLGRI GQRKHLVLN
Length:2,179
Mass (Da):233,517
Last modified:August 30, 2005 - v3
Checksum:i7E2CB328F87B8211
GO
Isoform 2 (identifier: O15027-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2087-2131: Missing.

Note: No experimental confirmation available.
Show »
Length:2,134
Mass (Da):228,870
Checksum:iFA89ECBF1F97F4F7
GO
Isoform 3 (identifier: O15027-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2112-2131: Missing.

Note: No experimental confirmation available.
Show »
Length:2,159
Mass (Da):231,252
Checksum:iEE0FBD9AE12E80DF
GO
Isoform 4 (identifier: O15027-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2087-2111: Missing.

Show »
Length:2,154
Mass (Da):231,136
Checksum:i51E525859C1AD868
GO
Isoform 5 (identifier: O15027-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2053-2053: T → TPVSSVRPQGRSGRNDGLLALSS

Note: No experimental confirmation available.
Show »
Length:2,201
Mass (Da):235,753
Checksum:iECE7CD89574B3FF5
GO

Sequence cautioni

The sequence BAA20769.4 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI13949.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI13951.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1099 – 10991Y → A in AAH28183 (PubMed:15489334).Curated
Sequence conflicti2101 – 21011S → P in AAH28183 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti861 – 8611R → C.
Corresponds to variant rs3812594 [ dbSNP | Ensembl ].
VAR_023332

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2053 – 20531T → TPVSSVRPQGRSGRNDGLLA LSS in isoform 5. 1 PublicationVSP_036029
Alternative sequencei2087 – 213145Missing in isoform 2. CuratedVSP_015252Add
BLAST
Alternative sequencei2087 – 211125Missing in isoform 4. 1 PublicationVSP_034370Add
BLAST
Alternative sequencei2112 – 213120Missing in isoform 3. 1 PublicationVSP_015253Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ903855 mRNA. Translation: ABI78944.1.
AB002308 mRNA. Translation: BAA20769.4. Different initiation.
AL592301 Genomic DNA. Translation: CAI13949.1. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13951.1. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13952.1.
BC008332 mRNA. Translation: AAH08332.1.
BC028183 mRNA. Translation: AAH28183.1.
BC098454 mRNA. Translation: AAH98454.1.
RefSeqiNP_001263347.1. NM_001276418.1.
NP_055681.1. NM_014866.1.
XP_011517554.1. XM_011519252.1.
UniGeneiHs.522500.

Genome annotation databases

EnsembliENST00000371706; ENSP00000360771; ENSG00000148396. [O15027-2]
ENST00000431893; ENSP00000387583; ENSG00000148396. [O15027-4]
GeneIDi9919.
KEGGihsa:9919.
UCSCiuc064xch.1. human. [O15027-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ903855 mRNA. Translation: ABI78944.1.
AB002308 mRNA. Translation: BAA20769.4. Different initiation.
AL592301 Genomic DNA. Translation: CAI13949.1. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13951.1. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13952.1.
BC008332 mRNA. Translation: AAH08332.1.
BC028183 mRNA. Translation: AAH28183.1.
BC098454 mRNA. Translation: AAH98454.1.
RefSeqiNP_001263347.1. NM_001276418.1.
NP_055681.1. NM_014866.1.
XP_011517554.1. XM_011519252.1.
UniGeneiHs.522500.

3D structure databases

ProteinModelPortaliO15027.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115247. 149 interactions.
DIPiDIP-27588N.
IntActiO15027. 111 interactions.
MINTiMINT-1155646.
STRINGi9606.ENSP00000325827.

PTM databases

iPTMnetiO15027.
PhosphoSiteiO15027.

Polymorphism and mutation databases

BioMutaiSEC16A.

Proteomic databases

EPDiO15027.
MaxQBiO15027.
PaxDbiO15027.
PeptideAtlasiO15027.
PRIDEiO15027.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371706; ENSP00000360771; ENSG00000148396. [O15027-2]
ENST00000431893; ENSP00000387583; ENSG00000148396. [O15027-4]
GeneIDi9919.
KEGGihsa:9919.
UCSCiuc064xch.1. human. [O15027-1]

Organism-specific databases

CTDi9919.
GeneCardsiSEC16A.
H-InvDBHIX0169092.
HGNCiHGNC:29006. SEC16A.
HPAiHPA005684.
MIMi612854. gene.
neXtProtiNX_O15027.
PharmGKBiPA162402611.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1913. Eukaryota.
ENOG4111J6D. LUCA.
GeneTreeiENSGT00530000063746.
HOVERGENiHBG079941.
InParanoidiO15027.
OrthoDBiEOG7MH0XQ.
PhylomeDBiO15027.

Enzyme and pathway databases

ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
SIGNORiO15027.

Miscellaneous databases

GeneWikiiSEC16A.
GenomeRNAii9919.
PROiO15027.
SOURCEiSearch...

Gene expression databases

BgeeiO15027.
CleanExiHS_SEC16A.
ExpressionAtlasiO15027. baseline and differential.
GenevisibleiO15027. HS.

Family and domain databases

InterProiIPR024298. ACE1_Sec16_Sec31.
IPR024880. Sec16.
IPR024340. Sec16_CCD.
[Graphical view]
PANTHERiPTHR13402. PTHR13402. 2 hits.
PfamiPF12932. Sec16. 1 hit.
PF12931. Sec16_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization."
    Bhattacharyya D., Glick B.S.
    Mol. Biol. Cell 18:839-849(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SEC23A.
    Tissue: Liver.
  2. "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."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1429-2179 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1098-2179 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1666-2179 (ISOFORM 5).
    Tissue: Lung, Placenta and Testis.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-1786, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1786; SER-1844 AND SER-1905, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells."
    Watson P., Townley A.K., Koka P., Palmer K.J., Stephens D.J.
    Traffic 7:1678-1687(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-1786, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1786 AND SER-1844, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-411; SER-414; THR-415; SER-417; SER-1149; SER-1786; SER-1844; THR-1876 AND SER-1905, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1786, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1786; SER-1844; SER-1864 AND SER-1905, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-891; SER-1178; SER-1786; SER-1844; THR-1876; SER-1895 AND SER-1905, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178; SER-1181 AND SER-1184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-153; SER-409; SER-417; SER-891; SER-1029; SER-1051; SER-1127; SER-1149; SER-1178; SER-1191; SER-1786; THR-1876; SER-1878; SER-1895; SER-1905; SER-2093 AND SER-2113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-381; SER-417; SER-891; THR-1147; SER-1169; SER-1172; SER-1178; SER-1181; SER-1395; SER-1423; THR-1729; SER-1761; SER-1786; THR-1876; SER-1905 AND SER-2093, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSC16A_HUMAN
AccessioniPrimary (citable) accession number: O15027
Secondary accession number(s): A1YCA4
, Q4G0D7, Q5SXP0, Q5SXP1, Q8N347, Q96HP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 30, 2005
Last modified: July 6, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.