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O94979 (SC31A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein transport protein Sec31A
Alternative name(s):
ABP125
ABP130
SEC31-like protein 1
SEC31-related protein A
Web1-like protein
Gene names
Name:SEC31A
Synonyms:KIAA0905, SEC31L1
ORF Names:HSPC275, HSPC334
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules By similarity. Ref.1

Subunit structure

COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13 By similarity. Interacts with PDCD6 in a calcium-dependent manner. Interacts with KLHL12. Ref.14 Ref.16 Ref.22

Subcellular location

Cytoplasm By similarity. Cytoplasmic vesicleCOPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Note: Associates with membranes in a GTP-dependent manner By similarity. Ref.1 Ref.14 Ref.22

Tissue specificity

Abundantly and ubiquitously expressed. Ref.1 Ref.12

Post-translational modification

Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, leading to regulate the size of COPII coats.

Involvement in disease

A chromosomal aberration involving SEC31A is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;4)(p23;q21) with ALK.

Sequence similarities

Belongs to the WD repeat SEC31 family.

Contains 8 WD repeats.

Sequence caution

The sequence AAF28953.1 differs from that shown. Reason: Frameshift at positions 857 and 1079.

The sequence AAF29012.1 differs from that shown. Reason: Frameshift at positions 922, 946, 1029 and 1080.

The sequence CAI45995.1 differs from that shown. Reason: Erroneous termination at position 221. Translated as Trp.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Endoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
WD repeat
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCOPII vesicle coating

Traceable author statement. Source: Reactome

ER to Golgi vesicle-mediated transport

Non-traceable author statement Ref.1. Source: UniProtKB

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

response to calcium ion

Inferred from direct assay Ref.16. Source: UniProtKB

   Cellular_componentCOPII vesicle coat

Non-traceable author statement Ref.1. Source: UniProtKB

ER to Golgi transport vesicle

Inferred from direct assay Ref.22. Source: UniProtKB

ER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi membrane

Traceable author statement. Source: GOC

cytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from direct assay Ref.16. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

vesicle coat

Inferred from direct assay PubMed 22792322. Source: MGI

   Molecular_functioncalcium-dependent protein binding

Inferred from physical interaction Ref.14Ref.16. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16PubMed 17214967PubMed 18256029. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDCD6O753406EBI-1767898,EBI-352915

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O94979-1)

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.
Isoform 2 (identifier: O94979-2)

The sequence of this isoform differs from the canonical sequence as follows:
     974-988: Missing.
Isoform 3 (identifier: O94979-3)

The sequence of this isoform differs from the canonical sequence as follows:
     876-876: P → R
     877-990: Missing.
Isoform 4 (identifier: O94979-4)

The sequence of this isoform differs from the canonical sequence as follows:
     504-542: Missing.
Isoform 5 (identifier: O94979-5)

The sequence of this isoform differs from the canonical sequence as follows:
     504-509: IALALN → VNFWES
     510-1220: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: O94979-6)

The sequence of this isoform differs from the canonical sequence as follows:
     504-542: Missing.
     876-876: P → R
     877-990: Missing.
Isoform 7 (identifier: O94979-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-228: Missing.
     229-260: MVLASEDDRLPVIQMWDLRFASSPLRVLENHA → MVKLVLLSIVLLKVTVPKLSNYLLQLDFMPIH
     504-542: Missing.
     834-834: H → HVRIAPTVTTWSNKTPTALPSHPPAASPSDTQ
     974-988: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: O94979-8)

The sequence of this isoform differs from the canonical sequence as follows:
     989-989: T → TENQSIQDQAPMLE
Isoform 9 (identifier: O94979-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MKLKEVDRTAMQAWSPAQNHPIYLAT → MLGESDERCTNAGSGCRRSSP
     974-988: Missing.
Note: No experimental confirmation available.
Isoform 10 (identifier: O94979-10)

The sequence of this isoform differs from the canonical sequence as follows:
     504-542: Missing.
     974-988: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12201220Protein transport protein Sec31A
PRO_0000295147

Regions

Repeat4 – 4744WD 1
Repeat68 – 11144WD 2
Repeat120 – 16041WD 3
Repeat166 – 20641WD 4
Repeat209 – 25446WD 5
Repeat258 – 29841WD 6
Repeat301 – 34242WD 7
Repeat397 – 43034WD 8; interaction with SEC13 By similarity
Region161 – 471311Interaction with SEC13
Region800 – 1113314Interaction with PDCD6
Compositional bias800 – 1091292Pro-rich

Amino acid modifications

Modified residue5271Phosphoserine Ref.13 Ref.21
Modified residue5321Phosphoserine Ref.13
Modified residue7991Phosphoserine Ref.17 Ref.19 Ref.21
Modified residue11611Phosphothreonine Ref.19
Modified residue11631Phosphoserine Ref.17
Cross-link647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22
Cross-link1217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22

Natural variations

Alternative sequence1 – 228228Missing in isoform 7.
VSP_026742
Alternative sequence1 – 2626MKLKE…IYLAT → MLGESDERCTNAGSGCRRSS P in isoform 9.
VSP_044602
Alternative sequence229 – 26032MVLAS…LENHA → MVKLVLLSIVLLKVTVPKLS NYLLQLDFMPIH in isoform 7.
VSP_026743
Alternative sequence504 – 54239Missing in isoform 4, isoform 6, isoform 7 and isoform 10.
VSP_026744
Alternative sequence504 – 5096IALALN → VNFWES in isoform 5.
VSP_026745
Alternative sequence510 – 1220711Missing in isoform 5.
VSP_026746
Alternative sequence8341H → HVRIAPTVTTWSNKTPTALP SHPPAASPSDTQ in isoform 7.
VSP_026747
Alternative sequence8761P → R in isoform 3 and isoform 6.
VSP_026748
Alternative sequence877 – 990114Missing in isoform 3 and isoform 6.
VSP_026749
Alternative sequence974 – 98815Missing in isoform 2, isoform 7, isoform 9 and isoform 10.
VSP_026750
Alternative sequence9891T → TENQSIQDQAPMLE in isoform 8.
VSP_026751
Natural variant2631I → V.
Corresponds to variant rs34554214 [ dbSNP | Ensembl ].
VAR_033225
Natural variant4561N → K.
Corresponds to variant rs3797036 [ dbSNP | Ensembl ].
VAR_053414
Natural variant8411P → L.
Corresponds to variant rs35579207 [ dbSNP | Ensembl ].
VAR_033226
Natural variant10551P → T.
Corresponds to variant rs35739017 [ dbSNP | Ensembl ].
VAR_033227

Experimental info

Mutagenesis6471K → R: Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-1217. Ref.22
Mutagenesis12171K → R: Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-647. Ref.22
Sequence conflict2001K → E in BAA84923. Ref.2
Sequence conflict2841K → R in BAC86336. Ref.5
Sequence conflict8541A → S in BAA84923. Ref.2
Sequence conflict8541A → S in BAA84924. Ref.2
Sequence conflict10071K → R in BAG58628. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 10, 2007. Version 3.
Checksum: 2A633B4436DB7482

FASTA1,220133,015
        10         20         30         40         50         60 
MKLKEVDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC 

        70         80         90        100        110        120 
ATFSSSHRYH KLIWGPYKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQNDK 

       130        140        150        160        170        180 
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV 

       190        200        210        220        230        240 
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV 

       250        260        270        280        290        300 
IQMWDLRFAS SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP 

       310        320        330        340        350        360 
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSTDG LRQKQVDKLS SSFGNLDPFG 

       370        380        390        400        410        420 
TGQPLPPLQI PQQTAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFENV RMPSHQGAEQ 

       430        440        450        460        470        480 
QQQQHHVFIS QVVTEKEFLS RSDQLQQAVQ SQGFINYCQK KIDASQTEFE KNVWSFLKVN 

       490        500        510        520        530        540 
FEDDSRGKYL ELLGYRKEDL GKKIALALNK VDGANVALKD SDQVAQSDGE ESPAAEEQLL 

       550        560        570        580        590        600 
GEHIKEEKEE SEFLPSSGGT FNISVSGDID GLITQALLTG NFESAVDLCL HDNRMADAII 

       610        620        630        640        650        660 
LAIAGGQELL ARTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR EALAAVLTYA 

       670        680        690        700        710        720 
KPDEFSALCD LLGTRLENEG DSLLQTQACL CYICAGNVEK LVACWTKAQD GSHPLSLQDL 

       730        740        750        760        770        780 
IEKVVILRKA VQLTQAMDTS TVGVLLAAKM SQYANLLAAQ GSIAAALAFL PDNTNQPNIM 

       790        800        810        820        830        840 
QLRDRLCRAQ GEPVAGHESP KIPYEKQQLP KGRPGPVAGH HQMPRVQTQQ YYPHGENPPP 

       850        860        870        880        890        900 
PGFIMHGNVN PNAAGQLPTS PGHMHTQVPP YPQPQPYQPA QPYPFGTGGS AMYRPQQPVA 

       910        920        930        940        950        960 
PPTSNAYPNT PYISSASSYT GQSQLYAAQH QASSPTSSPA TSFPPPPSSG ASFQHGGPGA 

       970        980        990       1000       1010       1020 
PPSSSAYALP PGTTGTLPAA SELPASQRTG PQNGWNDPPA LNRVPKKKKM PENFMPPVPI 

      1030       1040       1050       1060       1070       1080 
TSPIMNPLGD PQSQMLQQQP SAPVPLSSQS SFPQPHLPGG QPFHGVQQPL GQTGMPPSFS 

      1090       1100       1110       1120       1130       1140 
KPNIEGAPGA PIGNTFQHVQ SLPTKKITKK PIPDEHLILK TTFEDLIQRC LSSATDPQTK 

      1150       1160       1170       1180       1190       1200 
RKLDDASKRL EFLYDKLREQ TLSPTITSGL HNIARSIETR NYSEGLTMHT HIVSTSNFSE 

      1210       1220 
TSAFMPVLKV VLTQANKLGV 

« Hide

Isoform 2 [UniParc].

Checksum: 245E11A9AD589F74
Show »

FASTA1,205131,534
Isoform 3 [UniParc].

Checksum: D21AB6B647E1291B
Show »

FASTA1,106121,651
Isoform 4 [UniParc].

Checksum: 6FCDB50DE1A19BF0
Show »

FASTA1,181129,036
Isoform 5 [UniParc].

Checksum: 883FD8815650FA25
Show »

FASTA50956,731
Isoform 6 [UniParc].

Checksum: F2D05279DCE51522
Show »

FASTA1,067117,673
Isoform 7 [UniParc].

Checksum: C968C7ACE341CCAB
Show »

FASTA969105,753
Isoform 8 [UniParc].

Checksum: 1D63F1DEA3EC45F4
Show »

FASTA1,233134,499
Isoform 9 [UniParc].

Checksum: F2E4A99D905A6389
Show »

FASTA1,200130,747
Isoform 10 [UniParc].

Checksum: C780B386B096906E
Show »

FASTA1,166127,556

References

« Hide 'large scale' references
[1]"Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport."
Tang B.L., Zhang T., Low D.Y.H., Wong E.T., Horstmann H., Hong W.
J. Biol. Chem. 275:13597-13604(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Pancreas.
[2]"The yeast web1-like human protein that has WD repeat domain."
Noguchi J., Shibata M.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
Tissue: Spleen.
[3]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
Tissue: Hippocampus and Testis.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Uterine endothelium and Uterus.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORMS 2; 3; 5 AND 10).
Tissue: Brain and PNS.
[10]"SEC31 splicing variant."
Yang Y., Trejo J.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 599-1220 (ISOFORMS 3/6).
Tissue: Placenta.
[11]"Human partial CDS from CD34+ stem cells."
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 852-1220 (ISOFORM 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 899-1220 (ISOFORM 1).
Tissue: Blood.
[12]"Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat."
Shugrue C.A., Kolen E.R., Peters H., Czernik A., Kaiser C., Matovcik L., Hubbard A.L., Gorelick F.
J. Cell Sci. 112:4547-4556(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"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-527 AND SER-532, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.
Mol. Biol. Cell 17:4876-4887(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDCD6 AND SEC13, SUBCELLULAR LOCATION.
[15]"Fusion of the SEC31L1 and ALK genes in an inflammatory myofibroblastic tumor."
Panagopoulos I., Nilsson T., Domanski H.A., Isaksson M., Lindblom P., Mertens F., Mandahl N.
Int. J. Cancer 118:1181-1186(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH ALK.
[16]"ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner."
Shibata H., Suzuki H., Yoshida H., Maki M.
Biochem. Biophys. Res. Commun. 353:756-763(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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-799 AND THR-1161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-527 AND SER-799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Ubiquitin-dependent regulation of COPII coat size and function."
Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M.
Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217, MUTAGENESIS OF LYS-647 AND LYS-1217, INTERACTION WITH KLHL12.
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF139184 mRNA. Translation: AAF67836.1.
AB018358 mRNA. Translation: BAA84923.1.
AB018359 mRNA. Translation: BAA84924.1.
AB020712 mRNA. Translation: BAA74928.2.
AK125897 mRNA. Translation: BAC86336.1.
AK295810 mRNA. Translation: BAG58628.1.
AL049463 mRNA. Translation: CAH56418.1.
CR933696 mRNA. Translation: CAI45995.1. Sequence problems.
AC021105 Genomic DNA. No translation available.
AC108469 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05908.1.
BC047883 mRNA. Translation: AAH47883.1.
BC084583 mRNA. Translation: AAH84583.1.
BC117221 mRNA. Translation: AAI17222.1.
BC143489 mRNA. Translation: AAI43490.1.
BC143491 mRNA. Translation: AAI43492.1.
BC143492 mRNA. Translation: AAI43493.1.
AY137583 mRNA. Translation: AAN15221.1.
AF161393 mRNA. Translation: AAF28953.1. Frameshift.
AF161452 mRNA. Translation: AAF29012.1. Frameshift.
CCDSCCDS3596.1. [O94979-1]
CCDS3597.1. [O94979-4]
CCDS43244.1. [O94979-3]
CCDS47088.1. [O94979-2]
CCDS54773.1. [O94979-9]
RefSeqNP_001070674.1. NM_001077206.2. [O94979-3]
NP_001070675.1. NM_001077207.2. [O94979-1]
NP_001070676.1. NM_001077208.2. [O94979-2]
NP_001177978.1. NM_001191049.1. [O94979-9]
NP_055748.2. NM_014933.3. [O94979-1]
NP_057295.2. NM_016211.3. [O94979-4]
XP_005262904.1. XM_005262847.1. [O94979-8]
XP_005262907.1. XM_005262850.1. [O94979-2]
XP_005262909.1. XM_005262852.1. [O94979-10]
XP_005262911.1. XM_005262854.1. [O94979-6]
XP_006714204.1. XM_006714141.1. [O94979-8]
XP_006714205.1. XM_006714142.1. [O94979-8]
XP_006714206.1. XM_006714143.1. [O94979-8]
UniGeneHs.370024.

3D structure databases

ProteinModelPortalO94979.
SMRO94979. Positions 4-770.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116539. 13 interactions.
DIPDIP-40438N.
IntActO94979. 32 interactions.
MINTMINT-3002555.

PTM databases

PhosphoSiteO94979.

Proteomic databases

MaxQBO94979.
PaxDbO94979.
PRIDEO94979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311785; ENSP00000309070; ENSG00000138674. [O94979-3]
ENST00000326950; ENSP00000325087; ENSG00000138674. [O94979-4]
ENST00000348405; ENSP00000337602; ENSG00000138674. [O94979-4]
ENST00000355196; ENSP00000347329; ENSG00000138674. [O94979-1]
ENST00000395310; ENSP00000378721; ENSG00000138674. [O94979-1]
ENST00000432794; ENSP00000407944; ENSG00000138674. [O94979-8]
ENST00000443462; ENSP00000408027; ENSG00000138674. [O94979-9]
ENST00000448323; ENSP00000400926; ENSG00000138674. [O94979-1]
ENST00000500777; ENSP00000421464; ENSG00000138674. [O94979-6]
ENST00000505984; ENSP00000424451; ENSG00000138674.
ENST00000508502; ENSP00000424635; ENSG00000138674. [O94979-2]
ENST00000509142; ENSP00000426569; ENSG00000138674. [O94979-3]
ENST00000513858; ENSP00000426886; ENSG00000138674. [O94979-6]
GeneID22872.
KEGGhsa:22872.
UCSCuc003hnf.3. human. [O94979-1]
uc003hng.3. human. [O94979-2]
uc003hni.3. human. [O94979-3]
uc003hnk.3. human. [O94979-4]
uc003hnl.3. human. [O94979-6]
uc003hno.3. human. [O94979-5]

Organism-specific databases

CTD22872.
GeneCardsGC04M083739.
HGNCHGNC:17052. SEC31A.
HPAHPA005457.
MIM610257. gene.
neXtProtNX_O94979.
PharmGKBPA162402737.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248389.
HOVERGENHBG055626.
InParanoidO94979.
KOK14005.
OrthoDBEOG7B31M1.
PhylomeDBO94979.
TreeFamTF313842.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.
SignaLinkO94979.

Gene expression databases

ArrayExpressO94979.
BgeeO94979.
GenevestigatorO94979.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 1 hit.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSEC31A. human.
GeneWikiSEC31A.
GenomeRNAi22872.
NextBio35481219.
PROO94979.
SOURCESearch...

Entry information

Entry nameSC31A_HUMAN
AccessionPrimary (citable) accession number: O94979
Secondary accession number(s): B4DIW6 expand/collapse secondary AC list , B7ZKZ7, B7ZL00, H7C2W3, Q17RR5, Q5H9P6, Q5XG74, Q659G7, Q6ZU90, Q7LCX9, Q86TJ0, Q8IZH4, Q9P048, Q9P0A6, Q9UM05, Q9UM06
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM