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P55735

- SEC13_HUMAN

UniProt

P55735 - SEC13_HUMAN

Protein

Protein SEC13 homolog

Gene

SEC13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    3. cellular protein metabolic process Source: Reactome
    4. COPII vesicle coating Source: Reactome
    5. ER to Golgi vesicle-mediated transport Source: Reactome
    6. intracellular protein transport Source: UniProtKB
    7. membrane organization Source: Reactome
    8. mitotic cell cycle Source: Reactome
    9. mRNA transport Source: UniProtKB-KW
    10. post-translational protein modification Source: Reactome
    11. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Biological processi

    ER-Golgi transport, mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
    SignaLinkiP55735.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein SEC13 homolog
    Alternative name(s):
    SEC13-like protein 1
    SEC13-related protein
    Gene namesi
    Name:SEC13
    Synonyms:D3S1231E, SEC13L1, SEC13R
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10697. SEC13.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endoplasmic reticulum membrane Source: Reactome
    3. ER to Golgi transport vesicle membrane Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi membrane Source: GOC
    6. nuclear envelope Source: UniProtKB
    7. nuclear pore outer ring Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35620.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 322321Protein SEC13 homologPRO_0000051203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylvaline3 Publications
    Modified residuei309 – 3091Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP55735.
    PaxDbiP55735.
    PRIDEiP55735.

    PTM databases

    PhosphoSiteiP55735.

    Expressioni

    Gene expression databases

    ArrayExpressiP55735.
    BgeeiP55735.
    CleanExiHS_SEC13.
    GenevestigatoriP55735.

    Organism-specific databases

    HPAiHPA035292.

    Interactioni

    Subunit structurei

    At the nuclear pore: component of the Y-shaped Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13. At the COPII coat complex: interacts with SEC31A and SEC31B. Within the GATOR complex, component of the GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NUP145P496879EBI-1046596,EBI-11730From a different organism.

    Protein-protein interaction databases

    BioGridi112296. 32 interactions.
    DIPiDIP-39091N.
    IntActiP55735. 17 interactions.
    MINTiMINT-1154053.
    STRINGi9606.ENSP00000312122.

    Structurei

    Secondary structure

    1
    322
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 216
    Helixi23 – 253
    Beta strandi27 – 326
    Beta strandi35 – 439
    Beta strandi46 – 549
    Beta strandi60 – 656
    Helixi68 – 703
    Beta strandi74 – 785
    Beta strandi83 – 864
    Beta strandi89 – 913
    Beta strandi95 – 995
    Beta strandi108 – 1114
    Turni114 – 1163
    Beta strandi120 – 1234
    Beta strandi125 – 1273
    Beta strandi129 – 1346
    Beta strandi136 – 1383
    Beta strandi140 – 1423
    Beta strandi148 – 1514
    Beta strandi181 – 1833
    Beta strandi193 – 1964
    Beta strandi202 – 2065
    Beta strandi215 – 2195
    Beta strandi230 – 2356
    Beta strandi239 – 2446
    Beta strandi246 – 2494
    Beta strandi257 – 2604
    Beta strandi265 – 2706
    Turni272 – 2743
    Beta strandi277 – 2848
    Beta strandi286 – 2916
    Beta strandi297 – 3026

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BG0X-ray3.15A/D/E/H1-316[»]
    3BG1X-ray3.00A/D/E/H1-316[»]
    ProteinModelPortaliP55735.
    SMRiP55735. Positions 14-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55735.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati11 – 5040WD 1Add
    BLAST
    Repeati55 – 9642WD 2Add
    BLAST
    Repeati101 – 14444WD 3Add
    BLAST
    Repeati148 – 20457WD 4Add
    BLAST
    Repeati210 – 25344WD 5Add
    BLAST
    Repeati260 – 29940WD 6Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat SEC13 family.Curated
    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000216895.
    HOVERGENiHBG057343.
    InParanoidiP55735.
    KOiK14004.
    OrthoDBiEOG7966GP.
    PhylomeDBiP55735.
    TreeFamiTF300815.

    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. 6 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55735-1) [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

    MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI    50
    ADLRGHEGPV WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA 100
    GHDSSVNSVC WAPHDYGLIL ACGSSDGAIS LLTYTGEGQW EVKKINNAHT 150
    IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK RFASGGCDNL IKLWKEEEDG 200
    QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV FIWTCDDASS 250
    NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI 300
    SDVNKGQGSV SASVTEGQQN EQ 322
    Length:322
    Mass (Da):35,541
    Last modified:January 23, 2007 - v3
    Checksum:i18E29627D87FB3DD
    GO
    Isoform 2 (identifier: P55735-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:308
    Mass (Da):34,012
    Checksum:iF4D5BC3F757FE7BB
    GO
    Isoform 3 (identifier: P55735-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MREPVLTWCVPLELLCSHPLPLSAFLKSQVKLYTYRACAGKDEMGKM

    Note: No experimental confirmation available.

    Show »
    Length:368
    Mass (Da):40,747
    Checksum:iE738D9D307CF2308
    GO

    Sequence cautioni

    The sequence AAH02634.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511A → V in L09260. (PubMed:7987303)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721S → L.
    Corresponds to variant rs34078590 [ dbSNP | Ensembl ].
    VAR_053413

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1414Missing in isoform 2. 1 PublicationVSP_046191Add
    BLAST
    Alternative sequencei1 – 11M → MREPVLTWCVPLELLCSHPL PLSAFLKSQVKLYTYRACAG KDEMGKM in isoform 3. 1 PublicationVSP_054695

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09260 mRNA. No translation available.
    AF052155 mRNA. No translation available.
    AK301999 mRNA. Translation: BAG63403.1.
    AC022384 Genomic DNA. No translation available.
    BC002634 mRNA. Translation: AAH02634.2. Different initiation.
    BC006167 mRNA. Translation: AAH06167.1.
    BC091506 mRNA. Translation: AAH91506.1.
    CCDSiCCDS2599.1. [P55735-1]
    CCDS46751.1. [P55735-2]
    CCDS63540.1. [P55735-3]
    RefSeqiNP_001129498.1. NM_001136026.2. [P55735-3]
    NP_001129704.1. NM_001136232.2. [P55735-2]
    NP_109598.2. NM_030673.3.
    NP_899195.1. NM_183352.2. [P55735-1]
    XP_005265436.1. XM_005265379.1.
    XP_006713349.1. XM_006713286.1. [P55735-3]
    XP_006713351.1. XM_006713288.1. [P55735-2]
    UniGeneiHs.166924.

    Genome annotation databases

    EnsembliENST00000337354; ENSP00000336566; ENSG00000157020.
    ENST00000350697; ENSP00000312122; ENSG00000157020. [P55735-1]
    ENST00000383801; ENSP00000373312; ENSG00000157020. [P55735-3]
    ENST00000397109; ENSP00000380298; ENSG00000157020. [P55735-2]
    GeneIDi6396.
    KEGGihsa:6396.
    UCSCiuc003bvl.3. human. [P55735-1]

    Polymorphism databases

    DMDMi50403748.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09260 mRNA. No translation available.
    AF052155 mRNA. No translation available.
    AK301999 mRNA. Translation: BAG63403.1 .
    AC022384 Genomic DNA. No translation available.
    BC002634 mRNA. Translation: AAH02634.2 . Different initiation.
    BC006167 mRNA. Translation: AAH06167.1 .
    BC091506 mRNA. Translation: AAH91506.1 .
    CCDSi CCDS2599.1. [P55735-1 ]
    CCDS46751.1. [P55735-2 ]
    CCDS63540.1. [P55735-3 ]
    RefSeqi NP_001129498.1. NM_001136026.2. [P55735-3 ]
    NP_001129704.1. NM_001136232.2. [P55735-2 ]
    NP_109598.2. NM_030673.3.
    NP_899195.1. NM_183352.2. [P55735-1 ]
    XP_005265436.1. XM_005265379.1.
    XP_006713349.1. XM_006713286.1. [P55735-3 ]
    XP_006713351.1. XM_006713288.1. [P55735-2 ]
    UniGenei Hs.166924.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BG0 X-ray 3.15 A/D/E/H 1-316 [» ]
    3BG1 X-ray 3.00 A/D/E/H 1-316 [» ]
    ProteinModelPortali P55735.
    SMRi P55735. Positions 14-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112296. 32 interactions.
    DIPi DIP-39091N.
    IntActi P55735. 17 interactions.
    MINTi MINT-1154053.
    STRINGi 9606.ENSP00000312122.

    PTM databases

    PhosphoSitei P55735.

    Polymorphism databases

    DMDMi 50403748.

    Proteomic databases

    MaxQBi P55735.
    PaxDbi P55735.
    PRIDEi P55735.

    Protocols and materials databases

    DNASUi 6396.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337354 ; ENSP00000336566 ; ENSG00000157020 .
    ENST00000350697 ; ENSP00000312122 ; ENSG00000157020 . [P55735-1 ]
    ENST00000383801 ; ENSP00000373312 ; ENSG00000157020 . [P55735-3 ]
    ENST00000397109 ; ENSP00000380298 ; ENSG00000157020 . [P55735-2 ]
    GeneIDi 6396.
    KEGGi hsa:6396.
    UCSCi uc003bvl.3. human. [P55735-1 ]

    Organism-specific databases

    CTDi 6396.
    GeneCardsi GC03M010337.
    HGNCi HGNC:10697. SEC13.
    HPAi HPA035292.
    MIMi 600152. gene.
    neXtProti NX_P55735.
    PharmGKBi PA35620.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000216895.
    HOVERGENi HBG057343.
    InParanoidi P55735.
    KOi K14004.
    OrthoDBi EOG7966GP.
    PhylomeDBi P55735.
    TreeFami TF300815.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
    SignaLinki P55735.

    Miscellaneous databases

    EvolutionaryTracei P55735.
    GeneWikii SEC13.
    GenomeRNAii 6396.
    NextBioi 24846.
    PROi P55735.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55735.
    Bgeei P55735.
    CleanExi HS_SEC13.
    Genevestigatori P55735.

    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. 6 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of a novel human gene, SEC13R, related to the yeast secretory pathway gene SEC13, and mapping to a conserved linkage group on human chromosome 3p24-p25 and mouse chromosome 6."
      Swaroop A., Yang-Feng T.L., Liu W., Gieser L., Barrow L.L., Chen K.C., Agarwal N., Meisler M.H., Smith D.I.
      Hum. Mol. Genet. 3:1281-1286(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "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] (ISOFORM 3).
      Tissue: Testis.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Placenta and Uterus.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-27.
      Tissue: Platelet.
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-27; 44-54; 217-256 AND 291-322, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    8. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 182-192; 217-239 AND 291-322, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    9. "The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
      Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
      Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex."
      Enninga J., Levay A., Fontoura B.M.
      Mol. Cell. Biol. 23:7271-7284(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NUP96.
    11. "Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat."
      Stankewich M.C., Stabach P.R., Morrow J.S.
      J. Cell Sci. 119:958-969(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEC31B.
    12. "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: INTERACTION WITH SEC31A.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1."
      Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.
      Science 340:1100-1106(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN GATOR COMPLEX, INTERACTION WITH RRAG PROTEINS.
    18. "Architecture of a coat for the nuclear pore membrane."
      Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.
      Cell 131:1313-1326(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST NUP145C, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSEC13_HUMAN
    AccessioniPrimary (citable) accession number: P55735
    Secondary accession number(s): A8MV37
    , B4DXJ1, Q5BJF0, Q9BRM6, Q9BUG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 140 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3