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Protein

Endoplasmic reticulum resident protein 29

Gene

ERP29

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

Functioni

Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: ProtInc

GO - Biological processi

  1. intracellular protein transport Source: ProtInc
  2. protein folding Source: ProtInc
  3. protein secretion Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum resident protein 29
Short name:
ERp29
Alternative name(s):
Endoplasmic reticulum resident protein 28
Short name:
ERp28
Endoplasmic reticulum resident protein 31
Short name:
ERp31
Gene namesi
Name:ERP29
Synonyms:C12orf8, ERP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:13799. ERP29.

Subcellular locationi

Endoplasmic reticulum lumen. Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: ProtInc
  3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProtKB
  5. melanosome Source: UniProtKB-SubCell
  6. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25509.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 261229Endoplasmic reticulum resident protein 29PRO_0000021197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphotyrosine; by PKDCC1 Publication
Modified residuei66 – 661Phosphotyrosine; by PKDCC1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP30040.
PaxDbiP30040.
PeptideAtlasiP30040.
PRIDEiP30040.

2D gel databases

OGPiP30040.
REPRODUCTION-2DPAGEIPI00024911.
SWISS-2DPAGEP30040.

PTM databases

PhosphoSiteiP30040.

Expressioni

Tissue specificityi

Ubiquitous. Mostly expressed in secretory tissues.

Gene expression databases

BgeeiP30040.
CleanExiHS_ERP29.
ExpressionAtlasiP30040. baseline and differential.
GenevestigatoriP30040.

Organism-specific databases

HPAiHPA039363.
HPA039456.

Interactioni

Subunit structurei

Homodimer. Part of a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.

Binary interactionsi

WithEntry#Exp.IntActNotes
Erp29P525552EBI-8762218,EBI-917740From a different organism.

Protein-protein interaction databases

BioGridi116160. 8 interactions.
IntActiP30040. 6 interactions.
MINTiMINT-5002525.
STRINGi9606.ENSP00000261735.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 495Combined sources
Helixi50 – 523Combined sources
Beta strandi54 – 607Combined sources
Helixi68 – 8013Combined sources
Beta strandi86 – 916Combined sources
Beta strandi96 – 983Combined sources
Helixi102 – 1076Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1227Combined sources
Helixi138 – 14710Combined sources
Helixi159 – 17012Combined sources
Helixi174 – 1807Combined sources
Helixi183 – 1875Combined sources
Helixi193 – 21119Combined sources
Helixi217 – 23014Combined sources
Helixi235 – 24814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QC7X-ray2.90A/B34-261[»]
ProteinModelPortaliP30040.
SMRiP30040. Positions 33-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30040.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi258 – 2614Prevents secretion from ERPROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG82861.
GeneTreeiENSGT00390000018566.
HOGENOMiHOG000046371.
HOVERGENiHBG051508.
InParanoidiP30040.
KOiK09586.
OMAiGEKYKLD.
OrthoDBiEOG7XH6RH.
PhylomeDBiP30040.
TreeFamiTF324701.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]
PIRSFiPIRSF027352. ER_p29. 1 hit.
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P30040-1) [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
MAAAVPRAAF LSPLLPLLLG FLLLSAPHGG SGLHTKGALP LDTVTFYKVI
60 70 80 90 100
PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL
110 120 130 140 150
NMELSEKYKL DKESYPVFYL FRDGDFENPV PYTGAVKVGA IQRWLKGQGV
160 170 180 190 200
YLGMPGCLPV YDALAGEFIR ASGVEARQAL LKQGQDNLSS VKETQKKWAE
210 220 230 240 250
QYLKIMGKIL DQGEDFPASE MTRIARLIEK NKMSDGKKEE LQKSLNILTA
260
FQKKGAEKEE L
Length:261
Mass (Da):28,993
Last modified:December 15, 1998 - v4
Checksum:i76145006433A1983
GO
Isoform 2 (identifier: P30040-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-53: VIPKS → IMVTS
     54-261: Missing.

Note: No experimental confirmation available.

Show »
Length:53
Mass (Da):5,477
Checksum:i67DE41DE8CA1F165
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 535VIPKS → IMVTS in isoform 2. 1 PublicationVSP_045680
Alternative sequencei54 – 261208Missing in isoform 2. 1 PublicationVSP_045681Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94910 mRNA. Translation: CAA64397.1.
AA412124 mRNA. No translation available.
CR541667 mRNA. Translation: CAG46468.1.
AC073575 Genomic DNA. No translation available.
BC101493 mRNA. Translation: AAI01494.1.
BC101495 mRNA. Translation: AAI01496.1.
CCDSiCCDS44977.1. [P30040-2]
CCDS9158.1. [P30040-1]
PIRiT09549.
RefSeqiNP_001029197.1. NM_001034025.1. [P30040-2]
NP_006808.1. NM_006817.3. [P30040-1]
UniGeneiHs.75841.

Genome annotation databases

EnsembliENST00000261735; ENSP00000261735; ENSG00000089248. [P30040-1]
ENST00000455836; ENSP00000412083; ENSG00000089248. [P30040-2]
GeneIDi10961.
KEGGihsa:10961.
UCSCiuc001ttk.1. human. [P30040-1]

Polymorphism databases

DMDMi6015110.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94910 mRNA. Translation: CAA64397.1.
AA412124 mRNA. No translation available.
CR541667 mRNA. Translation: CAG46468.1.
AC073575 Genomic DNA. No translation available.
BC101493 mRNA. Translation: AAI01494.1.
BC101495 mRNA. Translation: AAI01496.1.
CCDSiCCDS44977.1. [P30040-2]
CCDS9158.1. [P30040-1]
PIRiT09549.
RefSeqiNP_001029197.1. NM_001034025.1. [P30040-2]
NP_006808.1. NM_006817.3. [P30040-1]
UniGeneiHs.75841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QC7X-ray2.90A/B34-261[»]
ProteinModelPortaliP30040.
SMRiP30040. Positions 33-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116160. 8 interactions.
IntActiP30040. 6 interactions.
MINTiMINT-5002525.
STRINGi9606.ENSP00000261735.

PTM databases

PhosphoSiteiP30040.

Polymorphism databases

DMDMi6015110.

2D gel databases

OGPiP30040.
REPRODUCTION-2DPAGEIPI00024911.
SWISS-2DPAGEP30040.

Proteomic databases

MaxQBiP30040.
PaxDbiP30040.
PeptideAtlasiP30040.
PRIDEiP30040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261735; ENSP00000261735; ENSG00000089248. [P30040-1]
ENST00000455836; ENSP00000412083; ENSG00000089248. [P30040-2]
GeneIDi10961.
KEGGihsa:10961.
UCSCiuc001ttk.1. human. [P30040-1]

Organism-specific databases

CTDi10961.
GeneCardsiGC12P112451.
HGNCiHGNC:13799. ERP29.
HPAiHPA039363.
HPA039456.
MIMi602287. gene.
neXtProtiNX_P30040.
PharmGKBiPA25509.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG82861.
GeneTreeiENSGT00390000018566.
HOGENOMiHOG000046371.
HOVERGENiHBG051508.
InParanoidiP30040.
KOiK09586.
OMAiGEKYKLD.
OrthoDBiEOG7XH6RH.
PhylomeDBiP30040.
TreeFamiTF324701.

Miscellaneous databases

ChiTaRSiERP29. human.
EvolutionaryTraceiP30040.
GeneWikiiERP29.
GenomeRNAii10961.
NextBioi41652.
PROiP30040.
SOURCEiSearch...

Gene expression databases

BgeeiP30040.
CleanExiHS_ERP29.
ExpressionAtlasiP30040. baseline and differential.
GenevestigatoriP30040.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]
PIRSFiPIRSF027352. ER_p29. 1 hit.
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif."
    Ferrari D.M., van Nguyen P., Kratzin H.D., Soeling H.D.
    Eur. J. Biochem. 255:570-579(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(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: Lung.
  6. Cited for: PROTEIN SEQUENCE OF 33-52.
    Tissue: Liver.
  7. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 33-42.
    Tissue: Liver.
  8. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 113-122, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  9. Hubbard M.J.
    Submitted (DEC-1998) to UniProtKB
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  10. "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
    Hubbard M.J., McHugh N.J.
    Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    Tissue: Liver.
  11. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
    Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
    Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: PHOSPHORYLATION AT TYR-64 AND TYR-66.

Entry informationi

Entry nameiERP29_HUMAN
AccessioniPrimary (citable) accession number: P30040
Secondary accession number(s): C9J183, Q3MJC3, Q6FHT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 15, 1998
Last modified: January 7, 2015
This is version 156 of the entry and version 4 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.