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O94979

- SC31A_HUMAN

UniProt

O94979 - SC31A_HUMAN

Protein

Protein transport protein Sec31A

Gene

SEC31A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (10 Jul 2007)
      Previous versions | rss
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    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
    2. 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

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:17052. SEC31A.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmic vesicleCOPII-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 membrane Source: Reactome
    6. ER to Golgi transport vesicle Source: UniProtKB
    7. ER to Golgi transport vesicle membrane Source: Reactome
    8. Golgi membrane Source: GOC
    9. intracellular membrane-bounded organelle Source: HPA
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. vesicle coat Source: MGI

    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

    ArrayExpressiO94979.
    BgeeiO94979.
    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. 15 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.
    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

    MKLKEVDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL     50
    SDPSLDMKSC ATFSSSHRYH KLIWGPYKMD SKGDVSGVLI AGGENGNIIL 100
    YDPSKIIAGD KEVVIAQNDK HTGPVRALDV NIFQTNLVAS GANESEIYIW 150
    DLNNFATPMT PGAKTQPPED ISCIAWNRQV QHILASASPS GRATVWDLRK 200
    NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV IQMWDLRFAS 250
    SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP 300
    TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSTDG LRQKQVDKLS 350
    SSFGNLDPFG TGQPLPPLQI PQQTAQHSIV LPLKKPPKWI RRPVGASFSF 400
    GGKLVTFENV RMPSHQGAEQ QQQQHHVFIS QVVTEKEFLS RSDQLQQAVQ 450
    SQGFINYCQK KIDASQTEFE KNVWSFLKVN FEDDSRGKYL ELLGYRKEDL 500
    GKKIALALNK VDGANVALKD SDQVAQSDGE ESPAAEEQLL GEHIKEEKEE 550
    SEFLPSSGGT FNISVSGDID GLITQALLTG NFESAVDLCL HDNRMADAII 600
    LAIAGGQELL ARTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR 650
    EALAAVLTYA KPDEFSALCD LLGTRLENEG DSLLQTQACL CYICAGNVEK 700
    LVACWTKAQD GSHPLSLQDL IEKVVILRKA VQLTQAMDTS TVGVLLAAKM 750
    SQYANLLAAQ GSIAAALAFL PDNTNQPNIM QLRDRLCRAQ GEPVAGHESP 800
    KIPYEKQQLP KGRPGPVAGH HQMPRVQTQQ YYPHGENPPP PGFIMHGNVN 850
    PNAAGQLPTS PGHMHTQVPP YPQPQPYQPA QPYPFGTGGS AMYRPQQPVA 900
    PPTSNAYPNT PYISSASSYT GQSQLYAAQH QASSPTSSPA TSFPPPPSSG 950
    ASFQHGGPGA PPSSSAYALP PGTTGTLPAA SELPASQRTG PQNGWNDPPA 1000
    LNRVPKKKKM PENFMPPVPI TSPIMNPLGD PQSQMLQQQP SAPVPLSSQS 1050
    SFPQPHLPGG QPFHGVQQPL GQTGMPPSFS KPNIEGAPGA PIGNTFQHVQ 1100
    SLPTKKITKK PIPDEHLILK TTFEDLIQRC LSSATDPQTK RKLDDASKRL 1150
    EFLYDKLREQ TLSPTITSGL HNIARSIETR NYSEGLTMHT HIVSTSNFSE 1200
    TSAFMPVLKV VLTQANKLGV 1220
    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.
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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_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]
    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]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS3596.1. [O94979-1 ]
    CCDS3597.1. [O94979-4 ]
    CCDS43244.1. [O94979-3 ]
    CCDS47088.1. [O94979-2 ]
    CCDS54773.1. [O94979-9 ]
    RefSeqi NP_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 ]
    UniGenei Hs.370024.

    3D structure databases

    ProteinModelPortali O94979.
    SMRi O94979. Positions 4-770.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116539. 15 interactions.
    DIPi DIP-40438N.
    IntActi O94979. 32 interactions.
    MINTi MINT-3002555.

    PTM databases

    PhosphoSitei O94979.

    Proteomic databases

    MaxQBi O94979.
    PaxDbi O94979.
    PRIDEi O94979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311785 ; 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 ]
    GeneIDi 22872.
    KEGGi hsa:22872.
    UCSCi uc003hnf.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

    CTDi 22872.
    GeneCardsi GC04M083739.
    HGNCi HGNC:17052. SEC31A.
    HPAi HPA005457.
    MIMi 610257. gene.
    neXtProti NX_O94979.
    PharmGKBi PA162402737.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248389.
    HOVERGENi HBG055626.
    InParanoidi O94979.
    KOi K14005.
    OrthoDBi EOG7B31M1.
    PhylomeDBi O94979.
    TreeFami TF313842.

    Enzyme and pathway databases

    Reactomei REACT_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.
    SignaLinki O94979.

    Miscellaneous databases

    ChiTaRSi SEC31A. human.
    GeneWikii SEC31A.
    GenomeRNAii 22872.
    NextBioi 35481219.
    PROi O94979.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94979.
    Bgeei O94979.
    Genevestigatori O94979.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 1 hit.
    [Graphical view ]
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 118 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