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Protein

Protein SEC13 homolog

Gene

SEC13

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

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 - Biological processi

Complete GO annotation...

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_355252. RHO GTPases Activate Formins.
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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10697. SEC13.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • ER to Golgi transport vesicle membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: GOC
  • nuclear envelope Source: UniProtKB
  • nuclear pore outer ring Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35620.

Polymorphism and mutation databases

DMDMi50403748.

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

BgeeiP55735.
CleanExiHS_SEC13.
ExpressionAtlasiP55735. baseline and differential.
GenevisibleiP55735. HS.

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.
SEC16BQ96JE7-25EBI-1046596,EBI-10215083
TRAF5O004633EBI-1046596,EBI-523498

Protein-protein interaction databases

BioGridi112296. 52 interactions.
DIPiDIP-39091N.
IntActiP55735. 21 interactions.
MINTiMINT-1154053.
STRINGi9606.ENSP00000312122.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000075049.
HOGENOMiHOG000216895.
HOVERGENiHBG057343.
InParanoidiP55735.
KOiK14004.
OMAiKSHEHAG.
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. AlignAdd to basket

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

        10         20         30         40         50
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI
60 70 80 90 100
ADLRGHEGPV WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA
110 120 130 140 150
GHDSSVNSVC WAPHDYGLIL ACGSSDGAIS LLTYTGEGQW EVKKINNAHT
160 170 180 190 200
IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK RFASGGCDNL IKLWKEEEDG
210 220 230 240 250
QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV FIWTCDDASS
260 270 280 290 300
NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI
310 320
SDVNKGQGSV SASVTEGQQN EQ
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. Curated

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:
EMBLi
GenBanki
DDBJi
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_006713351.1. XM_006713288.1. [P55735-2]
UniGeneiHs.166924.

Genome annotation databases

EnsembliENST00000350697; ENSP00000312122; ENSG00000157020. [P55735-1]
ENST00000383801; ENSP00000373312; ENSG00000157020. [P55735-3]
ENST00000397109; ENSP00000380298; ENSG00000157020. [P55735-2]
GeneIDi6396.
KEGGihsa:6396.
UCSCiuc003bvl.3. human. [P55735-1]
uc003bvo.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006713351.1. XM_006713288.1. [P55735-2]
UniGeneiHs.166924.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi112296. 52 interactions.
DIPiDIP-39091N.
IntActiP55735. 21 interactions.
MINTiMINT-1154053.
STRINGi9606.ENSP00000312122.

PTM databases

PhosphoSiteiP55735.

Polymorphism and mutation databases

DMDMi50403748.

Proteomic databases

MaxQBiP55735.
PaxDbiP55735.
PRIDEiP55735.

Protocols and materials databases

DNASUi6396.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350697; ENSP00000312122; ENSG00000157020. [P55735-1]
ENST00000383801; ENSP00000373312; ENSG00000157020. [P55735-3]
ENST00000397109; ENSP00000380298; ENSG00000157020. [P55735-2]
GeneIDi6396.
KEGGihsa:6396.
UCSCiuc003bvl.3. human. [P55735-1]
uc003bvo.3. human.

Organism-specific databases

CTDi6396.
GeneCardsiGC03M010350.
HGNCiHGNC:10697. SEC13.
HPAiHPA035292.
MIMi600152. gene.
neXtProtiNX_P55735.
PharmGKBiPA35620.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00550000075049.
HOGENOMiHOG000216895.
HOVERGENiHBG057343.
InParanoidiP55735.
KOiK14004.
OMAiKSHEHAG.
OrthoDBiEOG7966GP.
PhylomeDBiP55735.
TreeFamiTF300815.

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_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SignaLinkiP55735.

Miscellaneous databases

ChiTaRSiSEC13. human.
EvolutionaryTraceiP55735.
GeneWikiiSEC13.
GenomeRNAii6396.
NextBioi24846.
PROiP55735.
SOURCEiSearch...

Gene expression databases

BgeeiP55735.
CleanExiHS_SEC13.
ExpressionAtlasiP55735. baseline and differential.
GenevisibleiP55735. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: June 24, 2015
This is version 148 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

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.