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O94979 - SC31A_HUMAN

UniProt

O94979 - SC31A_HUMAN

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Protein

Protein transport protein Sec31A

Gene

SEC31A

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

Functioni

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).By similarity

GO - Molecular functioni

  1. calcium-dependent protein binding Source: UniProtKB

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  4. cellular protein metabolic process Source: Reactome
  5. COPII vesicle coating Source: Reactome
  6. endoplasmic reticulum unfolded protein response Source: Reactome
  7. ER to Golgi vesicle-mediated transport Source: UniProtKB
  8. membrane organization Source: Reactome
  9. post-translational protein modification Source: Reactome
  10. protein N-linked glycosylation via asparagine Source: Reactome
  11. protein transport Source: UniProtKB-KW
  12. response to calcium ion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
REACT_18273. XBP1(S) activates chaperone genes.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SignaLinkiO94979.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein Sec31A
Alternative name(s):
ABP125
ABP130
SEC31-like protein 1
SEC31-related protein A
Web1-like protein
Gene namesi
Name:SEC31A
Synonyms:KIAA0905, SEC31L1
ORF Names:HSPC275, HSPC334
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:17052. SEC31A.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmic vesicle › COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
Note: Associates with membranes in a GTP-dependent manner.By similarity

GO - Cellular componenti

  1. COPII vesicle coat Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. endoplasmic reticulum Source: UniProtKB
  5. endoplasmic reticulum exit site Source: UniProtKB
  6. endoplasmic reticulum membrane Source: Reactome
  7. ER to Golgi transport vesicle Source: UniProtKB
  8. ER to Golgi transport vesicle membrane Source: Reactome
  9. Golgi membrane Source: GOC
  10. intracellular membrane-bounded organelle Source: HPA
  11. perinuclear region of cytoplasm Source: UniProtKB
  12. vesicle coat Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi647 – 6471K → R: Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-1217. 1 Publication
Mutagenesisi1217 – 12171K → R: Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-647. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA162402737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12201220Protein transport protein Sec31APRO_0000295147Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei527 – 5271Phosphoserine2 Publications
Modified residuei532 – 5321Phosphoserine1 Publication
Cross-linki647 – 647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei799 – 7991Phosphoserine3 Publications
Modified residuei1161 – 11611Phosphothreonine1 Publication
Modified residuei1163 – 11631Phosphoserine1 Publication
Cross-linki1217 – 1217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, leading to regulate the size of COPII coats.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO94979.
PaxDbiO94979.
PRIDEiO94979.

PTM databases

PhosphoSiteiO94979.

Expressioni

Tissue specificityi

Abundantly and ubiquitously expressed.2 Publications

Gene expression databases

BgeeiO94979.
ExpressionAtlasiO94979. baseline and differential.
GenevestigatoriO94979.

Organism-specific databases

HPAiHPA005457.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDCD6O753406EBI-1767898,EBI-352915

Protein-protein interaction databases

BioGridi116539. 19 interactions.
DIPiDIP-40438N.
IntActiO94979. 32 interactions.
MINTiMINT-3002555.

Structurei

3D structure databases

ProteinModelPortaliO94979.
SMRiO94979. Positions 4-770.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati4 – 4744WD 1Add
BLAST
Repeati68 – 11144WD 2Add
BLAST
Repeati120 – 16041WD 3Add
BLAST
Repeati166 – 20641WD 4Add
BLAST
Repeati209 – 25446WD 5Add
BLAST
Repeati258 – 29841WD 6Add
BLAST
Repeati301 – 34242WD 7Add
BLAST
Repeati397 – 43034WD 8; interaction with SEC13PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni161 – 471311Interaction with SEC13Add
BLAST
Regioni800 – 1113314Interaction with PDCD6Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi800 – 1091292Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat SEC31 family.Curated
Contains 8 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiNOG248389.
GeneTreeiENSGT00390000003175.
HOVERGENiHBG055626.
InParanoidiO94979.
KOiK14005.
OrthoDBiEOG7B31M1.
PhylomeDBiO94979.
TreeFamiTF313842.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O94979-1) [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
MKLKEVDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL 
        60         70         80         90        100
SDPSLDMKSC ATFSSSHRYH KLIWGPYKMD SKGDVSGVLI AGGENGNIIL 
       110        120        130        140        150
YDPSKIIAGD KEVVIAQNDK HTGPVRALDV NIFQTNLVAS GANESEIYIW 
       160        170        180        190        200
DLNNFATPMT PGAKTQPPED ISCIAWNRQV QHILASASPS GRATVWDLRK 
       210        220        230        240        250
NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV IQMWDLRFAS 
       260        270        280        290        300
SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP 
       310        320        330        340        350
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSTDG LRQKQVDKLS 
       360        370        380        390        400
SSFGNLDPFG TGQPLPPLQI PQQTAQHSIV LPLKKPPKWI RRPVGASFSF 
       410        420        430        440        450
GGKLVTFENV RMPSHQGAEQ QQQQHHVFIS QVVTEKEFLS RSDQLQQAVQ 
       460        470        480        490        500
SQGFINYCQK KIDASQTEFE KNVWSFLKVN FEDDSRGKYL ELLGYRKEDL 
       510        520        530        540        550
GKKIALALNK VDGANVALKD SDQVAQSDGE ESPAAEEQLL GEHIKEEKEE 
       560        570        580        590        600
SEFLPSSGGT FNISVSGDID GLITQALLTG NFESAVDLCL HDNRMADAII 
       610        620        630        640        650
LAIAGGQELL ARTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR 
       660        670        680        690        700
EALAAVLTYA KPDEFSALCD LLGTRLENEG DSLLQTQACL CYICAGNVEK 
       710        720        730        740        750
LVACWTKAQD GSHPLSLQDL IEKVVILRKA VQLTQAMDTS TVGVLLAAKM 
       760        770        780        790        800
SQYANLLAAQ GSIAAALAFL PDNTNQPNIM QLRDRLCRAQ GEPVAGHESP 
       810        820        830        840        850
KIPYEKQQLP KGRPGPVAGH HQMPRVQTQQ YYPHGENPPP PGFIMHGNVN 
       860        870        880        890        900
PNAAGQLPTS PGHMHTQVPP YPQPQPYQPA QPYPFGTGGS AMYRPQQPVA 
       910        920        930        940        950
PPTSNAYPNT PYISSASSYT GQSQLYAAQH QASSPTSSPA TSFPPPPSSG 
       960        970        980        990       1000
ASFQHGGPGA PPSSSAYALP PGTTGTLPAA SELPASQRTG PQNGWNDPPA 
      1010       1020       1030       1040       1050
LNRVPKKKKM PENFMPPVPI TSPIMNPLGD PQSQMLQQQP SAPVPLSSQS 
      1060       1070       1080       1090       1100
SFPQPHLPGG QPFHGVQQPL GQTGMPPSFS KPNIEGAPGA PIGNTFQHVQ 
      1110       1120       1130       1140       1150
SLPTKKITKK PIPDEHLILK TTFEDLIQRC LSSATDPQTK RKLDDASKRL 
      1160       1170       1180       1190       1200
EFLYDKLREQ TLSPTITSGL HNIARSIETR NYSEGLTMHT HIVSTSNFSE 
      1210       1220
TSAFMPVLKV VLTQANKLGV
Length:1,220
Mass (Da):133,015
Last modified:July 10, 2007 - v3
Checksum:i2A633B4436DB7482
GO
Isoform 2 (identifier: O94979-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     974-988: Missing.

Show »
Length:1,205
Mass (Da):131,534
Checksum:i245E11A9AD589F74
GO
Isoform 3 (identifier: O94979-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     876-876: P → R
     877-990: Missing.

Show »
Length:1,106
Mass (Da):121,651
Checksum:iD21AB6B647E1291B
GO
Isoform 4 (identifier: O94979-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-542: Missing.

Show »
Length:1,181
Mass (Da):129,036
Checksum:i6FCDB50DE1A19BF0
GO
Isoform 5 (identifier: O94979-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-509: IALALN → VNFWES
     510-1220: Missing.

Note: No experimental confirmation available.

Show »
Length:509
Mass (Da):56,731
Checksum:i883FD8815650FA25
GO
Isoform 6 (identifier: O94979-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-542: Missing.
     876-876: P → R
     877-990: Missing.

Show »
Length:1,067
Mass (Da):117,673
Checksum:iF2D05279DCE51522
GO
Isoform 7 (identifier: O94979-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:969
Mass (Da):105,753
Checksum:iC968C7ACE341CCAB
GO
Isoform 8 (identifier: O94979-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     989-989: T → TENQSIQDQAPMLE

Show »
Length:1,233
Mass (Da):134,499
Checksum:i1D63F1DEA3EC45F4
GO
Isoform 9 (identifier: O94979-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MKLKEVDRTAMQAWSPAQNHPIYLAT → MLGESDERCTNAGSGCRRSSP
     974-988: Missing.

Note: No experimental confirmation available.

Show »
Length:1,200
Mass (Da):130,747
Checksum:iF2E4A99D905A6389
GO
Isoform 10 (identifier: O94979-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-542: Missing.
     974-988: Missing.

Note: No experimental confirmation available.

Show »
Length:1,166
Mass (Da):127,556
Checksum:iC780B386B096906E
GO

Sequence cautioni

The sequence AAF28953.1 differs from that shown. Reason: Frameshift at positions 857 and 1079. Curated
The sequence AAF29012.1 differs from that shown. Reason: Frameshift at positions 922, 946, 1029 and 1080. Curated
The sequence CAI45995.1 differs from that shown. Reason: Erroneous termination at position 221. Translated as Trp.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2001K → E in BAA84923. 1 PublicationCurated
Sequence conflicti284 – 2841K → R in BAC86336. (PubMed:14702039)Curated
Sequence conflicti854 – 8541A → S in BAA84923. 1 PublicationCurated
Sequence conflicti854 – 8541A → S in BAA84924. 1 PublicationCurated
Sequence conflicti1007 – 10071K → R in BAG58628. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti263 – 2631I → V.
Corresponds to variant rs34554214 [ dbSNP | Ensembl ].		VAR_033225
Natural varianti456 – 4561N → K.
Corresponds to variant rs3797036 [ dbSNP | Ensembl ].		VAR_053414
Natural varianti841 – 8411P → L.
Corresponds to variant rs35579207 [ dbSNP | Ensembl ].		VAR_033226
Natural varianti1055 – 10551P → T.
Corresponds to variant rs35739017 [ dbSNP | Ensembl ].		VAR_033227

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 228228Missing in isoform 7. 1 PublicationVSP_026742Add
BLAST
Alternative sequencei1 – 2626MKLKE…IYLAT → MLGESDERCTNAGSGCRRSS P in isoform 9. 1 PublicationVSP_044602Add
BLAST
Alternative sequencei229 – 26032MVLAS…LENHA → MVKLVLLSIVLLKVTVPKLS NYLLQLDFMPIH in isoform 7. 1 PublicationVSP_026743Add
BLAST
Alternative sequencei504 – 54239Missing in isoform 4, isoform 6, isoform 7 and isoform 10. 4 PublicationsVSP_026744Add
BLAST
Alternative sequencei504 – 5096IALALN → VNFWES in isoform 5. 1 PublicationVSP_026745
Alternative sequencei510 – 1220711Missing in isoform 5. 1 PublicationVSP_026746Add
BLAST
Alternative sequencei834 – 8341H → HVRIAPTVTTWSNKTPTALP SHPPAASPSDTQ in isoform 7. 1 PublicationVSP_026747
Alternative sequencei876 – 8761P → R in isoform 3 and isoform 6. 2 PublicationsVSP_026748
Alternative sequencei877 – 990114Missing in isoform 3 and isoform 6. 2 PublicationsVSP_026749Add
BLAST
Alternative sequencei974 – 98815Missing in isoform 2, isoform 7, isoform 9 and isoform 10. 2 PublicationsVSP_026750Add
BLAST
Alternative sequencei989 – 9891T → TENQSIQDQAPMLE in isoform 8. 1 PublicationVSP_026751

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3596.1. [O94979-1]
CCDS3597.1. [O94979-4]
CCDS43244.1. [O94979-3]
CCDS47088.1. [O94979-2]
CCDS54773.1. [O94979-9]
CCDS75155.1. [O94979-6]
CCDS75156.1. [O94979-10]
RefSeqiNP_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_001287673.1. NM_001300744.1. [O94979-6]
NP_001287674.1. NM_001300745.1. [O94979-10]
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_006714204.1. XM_006714141.1. [O94979-8]
XP_006714205.1. XM_006714142.1. [O94979-8]
XP_006714206.1. XM_006714143.1. [O94979-8]
UniGeneiHs.370024.

Genome annotation databases

EnsembliENST00000311785; ENSP00000309070; ENSG00000138674. [O94979-3]
ENST00000348405; ENSP00000337602; ENSG00000138674. [O94979-4]
ENST00000355196; ENSP00000347329; ENSG00000138674. [O94979-1]
ENST00000395310; ENSP00000378721; ENSG00000138674. [O94979-1]
ENST00000443462; ENSP00000408027; ENSG00000138674. [O94979-9]
ENST00000448323; ENSP00000400926; ENSG00000138674. [O94979-1]
ENST00000500777; ENSP00000421464; ENSG00000138674. [O94979-6]
ENST00000505984; ENSP00000424451; ENSG00000138674. [O94979-10]
ENST00000508502; ENSP00000424635; ENSG00000138674. [O94979-2]
ENST00000509142; ENSP00000426569; ENSG00000138674. [O94979-3]
ENST00000513858; ENSP00000426886; ENSG00000138674. [O94979-6]
GeneIDi22872.
KEGGihsa:22872.
UCSCiuc003hnf.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]
uc011ccl.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3596.1. [O94979-1]
CCDS3597.1. [O94979-4]
CCDS43244.1. [O94979-3]
CCDS47088.1. [O94979-2]
CCDS54773.1. [O94979-9]
CCDS75155.1. [O94979-6]
CCDS75156.1. [O94979-10]
RefSeqiNP_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_001287673.1. NM_001300744.1. [O94979-6]
NP_001287674.1. NM_001300745.1. [O94979-10]
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_006714204.1. XM_006714141.1. [O94979-8]
XP_006714205.1. XM_006714142.1. [O94979-8]
XP_006714206.1. XM_006714143.1. [O94979-8]
UniGeneiHs.370024.

3D structure databases

ProteinModelPortaliO94979.
SMRiO94979. Positions 4-770.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116539. 19 interactions.
DIPiDIP-40438N.
IntActiO94979. 32 interactions.
MINTiMINT-3002555.

PTM databases

PhosphoSiteiO94979.

Proteomic databases

MaxQBiO94979.
PaxDbiO94979.
PRIDEiO94979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311785; ENSP00000309070; ENSG00000138674. [O94979-3]
ENST00000348405; ENSP00000337602; ENSG00000138674. [O94979-4]
ENST00000355196; ENSP00000347329; ENSG00000138674. [O94979-1]
ENST00000395310; ENSP00000378721; ENSG00000138674. [O94979-1]
ENST00000443462; ENSP00000408027; ENSG00000138674. [O94979-9]
ENST00000448323; ENSP00000400926; ENSG00000138674. [O94979-1]
ENST00000500777; ENSP00000421464; ENSG00000138674. [O94979-6]
ENST00000505984; ENSP00000424451; ENSG00000138674. [O94979-10]
ENST00000508502; ENSP00000424635; ENSG00000138674. [O94979-2]
ENST00000509142; ENSP00000426569; ENSG00000138674. [O94979-3]
ENST00000513858; ENSP00000426886; ENSG00000138674. [O94979-6]
GeneIDi22872.
KEGGihsa:22872.
UCSCiuc003hnf.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]
uc011ccl.2. human.

Organism-specific databases

CTDi22872.
GeneCardsiGC04M083739.
HGNCiHGNC:17052. SEC31A.
HPAiHPA005457.
MIMi610257. gene.
neXtProtiNX_O94979.
PharmGKBiPA162402737.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248389.
GeneTreeiENSGT00390000003175.
HOVERGENiHBG055626.
InParanoidiO94979.
KOiK14005.
OrthoDBiEOG7B31M1.
PhylomeDBiO94979.
TreeFamiTF313842.

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
REACT_18273. XBP1(S) activates chaperone genes.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SignaLinkiO94979.

Miscellaneous databases

ChiTaRSiSEC31A. human.
GeneWikiiSEC31A.
GenomeRNAii22872.
NextBioi35481219.
PROiO94979.
SOURCEiSearch...

Gene expression databases

BgeeiO94979.
ExpressionAtlasiO94979. baseline and differential.
GenevestigatoriO94979.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Entry informationi

Entry nameiSC31A_HUMAN
AccessioniPrimary (citable) accession number: O94979
Secondary accession number(s): B4DIW6
, B7ZKZ7, B7ZL00, H7C2W3, Q17RR5, Q5H9P6, Q5XG74, Q659G7, Q6ZU90, Q7LCX9, Q86TJ0, Q8IZH4, Q9P048, Q9P0A6, Q9UM05, Q9UM06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: February 4, 2015
This is version 122 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 4
    Human chromosome 4: 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

External Data

Dasty 3

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 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.