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P14625

- ENPL_HUMAN

UniProt

P14625 - ENPL_HUMAN

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Protein

Endoplasmin

Gene

HSP90B1

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

Functioni

Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071ATPBy similarity
Binding sitei149 – 1491ATPBy similarity
Binding sitei162 – 1621ATPBy similarity
Binding sitei168 – 1681ATPBy similarity
Binding sitei199 – 1991ATP; via amide nitrogenBy similarity
Binding sitei448 – 4481ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: UniProtKB
  3. low-density lipoprotein particle receptor binding Source: MGI
  4. protein phosphatase binding Source: MGI
  5. RNA binding Source: UniProtKB
  6. virion binding Source: UniProtKB

GO - Biological processi

  1. actin rod assembly Source: MGI
  2. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. cellular response to ATP Source: MGI
  5. endoplasmic reticulum unfolded protein response Source: Reactome
  6. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. innate immune response Source: Reactome
  8. negative regulation of apoptotic process Source: UniProtKB
  9. protein folding Source: InterPro
  10. protein transport Source: UniProtKB
  11. regulation of phosphoprotein phosphatase activity Source: MGI
  12. response to hypoxia Source: UniProtKB
  13. sequestering of calcium ion Source: UniProtKB
  14. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118632. Trafficking and processing of endosomal TLR.
REACT_163699. Scavenging by Class A Receptors.
REACT_18423. ATF6-alpha activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmin
Alternative name(s):
94 kDa glucose-regulated protein
Short name:
GRP-94
Heat shock protein 90 kDa beta member 1
Tumor rejection antigen 1
gp96 homolog
Gene namesi
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:12028. HSP90B1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. endocytic vesicle lumen Source: Reactome
  3. endoplasmic reticulum Source: UniProtKB
  4. endoplasmic reticulum lumen Source: UniProtKB
  5. endoplasmic reticulum membrane Source: UniProtKB
  6. extracellular matrix Source: UniProtKB
  7. extracellular region Source: Reactome
  8. extracellular vesicular exosome Source: UniProt
  9. focal adhesion Source: UniProtKB
  10. membrane Source: UniProtKB
  11. midbody Source: UniProtKB
  12. nucleus Source: UniProt
  13. perinuclear region of cytoplasm Source: UniProtKB
  14. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36705.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 803782EndoplasminPRO_0000013598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)1 Publication
Glycosylationi107 – 1071N-linked (GlcNAc...)2 Publications
Disulfide bondi138 – 138InterchainBy similarity
Glycosylationi217 – 2171N-linked (GlcNAc...)2 Publications
Modified residuei306 – 3061Phosphoserine2 Publications
Modified residuei404 – 4041N6-succinyllysineBy similarity
Glycosylationi445 – 4451N-linked (GlcNAc...)2 Publications
Modified residuei479 – 4791N6-acetyllysineBy similarity
Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
Modified residuei633 – 6331N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP14625.
PaxDbiP14625.
PeptideAtlasiP14625.
PRIDEiP14625.

2D gel databases

DOSAC-COBS-2DPAGEP14625.
OGPiP14625.
REPRODUCTION-2DPAGEIPI00027230.

PTM databases

PhosphoSiteiP14625.

Miscellaneous databases

PMAP-CutDBP14625.

Expressioni

Gene expression databases

BgeeiP14625.
CleanExiHS_HSP90B1.
ExpressionAtlasiP14625. baseline and differential.
GenevestigatoriP14625.

Organism-specific databases

HPAiCAB005224.
HPA003901.
HPA008424.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9. Interacts with CNPY3. This interaction is disrupted in the presence of ATP (By similarity). Interacts with TLR4 and TLR9, but not with TLR3. Interacts with MZB1 in a calcium-dependent manner (By similarity). Interacts with METTL23.By similarity3 Publications

Protein-protein interaction databases

BioGridi113036. 81 interactions.
DIPiDIP-36060N.
IntActiP14625. 43 interactions.
MINTiMINT-210408.
STRINGi9606.ENSP00000299767.

Structurei

Secondary structure

1
803
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi80 – 9213Combined sources
Helixi99 – 11820Combined sources
Turni119 – 1213Combined sources
Turni123 – 1286Combined sources
Beta strandi134 – 1396Combined sources
Turni140 – 1434Combined sources
Beta strandi144 – 1496Combined sources
Helixi156 – 1605Combined sources
Helixi175 – 18410Combined sources
Helixi189 – 1946Combined sources
Helixi198 – 2047Combined sources
Beta strandi206 – 2149Combined sources
Beta strandi221 – 2255Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi241 – 25111Combined sources
Helixi256 – 2594Combined sources
Helixi261 – 27111Combined sources
Beta strandi279 – 2846Combined sources
Beta strandi331 – 3355Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NH9X-ray2.77A69-337[»]
ProteinModelPortaliP14625.
SMRiP14625. Positions 72-755.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi800 – 8034Prevents secretion from ER

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0326.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP14625.
KOiK09487.
OMAiQSSHHPS.
OrthoDBiEOG780RM0.
PhylomeDBiP14625.
TreeFamiTF105969.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14625-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ
60 70 80 90 100
REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF
110 120 130 140 150
LRELISNASD ALDKIRLISL TDENALSGNE ELTVKIKCDK EKNLLHVTDT
160 170 180 190 200
GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY
210 220 230 240 250
SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV
260 270 280 290 300
LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
310 320 330 340 350
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV
360 370 380 390 400
EEDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE
410 420 430 440 450
YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET
460 470 480 490 500
LQQHKLLKVI RKKLVRKTLD MIKKIADDKY NDTFWKEFGT NIKLGVIEDH
510 520 530 540 550
SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE
560 570 580 590 600
SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
610 620 630 640 650
SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS
660 670 680 690 700
QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR
710 720 730 740 750
IKEDEDDKTV LDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID
760 770 780 790 800
PDAKVEEEPE EEPEETAEDT TEDTEQDEDE EMDVGTDEEE ETAKESTAEK

DEL
Length:803
Mass (Da):92,469
Last modified:April 1, 1990 - v1
Checksum:i9BF6705A7A2ED0D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881T → S in AAK74072. 1 PublicationCurated
Sequence conflicti419 – 4191T → P in AAK74072. 1 PublicationCurated
Sequence conflicti803 – 8031L → F in AAK74072. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15187 mRNA. Translation: CAA33261.1.
M33716 Genomic DNA. Translation: AAA68201.1.
BC066656 mRNA. Translation: AAH66656.1.
M26596 Genomic DNA. Translation: AAA58621.1.
AY040226 mRNA. Translation: AAK74072.1.
CCDSiCCDS9094.1.
PIRiA35954.
RefSeqiNP_003290.1. NM_003299.2.
UniGeneiHs.192374.

Genome annotation databases

EnsembliENST00000299767; ENSP00000299767; ENSG00000166598.
GeneIDi7184.
KEGGihsa:7184.
UCSCiuc001tkb.2. human.

Polymorphism databases

DMDMi119360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15187 mRNA. Translation: CAA33261.1 .
M33716 Genomic DNA. Translation: AAA68201.1 .
BC066656 mRNA. Translation: AAH66656.1 .
M26596 Genomic DNA. Translation: AAA58621.1 .
AY040226 mRNA. Translation: AAK74072.1 .
CCDSi CCDS9094.1.
PIRi A35954.
RefSeqi NP_003290.1. NM_003299.2.
UniGenei Hs.192374.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NH9 X-ray 2.77 A 69-337 [» ]
ProteinModelPortali P14625.
SMRi P14625. Positions 72-755.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113036. 81 interactions.
DIPi DIP-36060N.
IntActi P14625. 43 interactions.
MINTi MINT-210408.
STRINGi 9606.ENSP00000299767.

Chemistry

BindingDBi P14625.
ChEMBLi CHEMBL1075323.
DrugBanki DB00615. Rifabutin.

PTM databases

PhosphoSitei P14625.

Polymorphism databases

DMDMi 119360.

2D gel databases

DOSAC-COBS-2DPAGE P14625.
OGPi P14625.
REPRODUCTION-2DPAGE IPI00027230.

Proteomic databases

MaxQBi P14625.
PaxDbi P14625.
PeptideAtlasi P14625.
PRIDEi P14625.

Protocols and materials databases

DNASUi 7184.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299767 ; ENSP00000299767 ; ENSG00000166598 .
GeneIDi 7184.
KEGGi hsa:7184.
UCSCi uc001tkb.2. human.

Organism-specific databases

CTDi 7184.
GeneCardsi GC12P104324.
H-InvDB HIX0056796.
HGNCi HGNC:12028. HSP90B1.
HPAi CAB005224.
HPA003901.
HPA008424.
MIMi 191175. gene.
neXtProti NX_P14625.
PharmGKBi PA36705.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0326.
HOGENOMi HOG000031988.
HOVERGENi HBG007374.
InParanoidi P14625.
KOi K09487.
OMAi QSSHHPS.
OrthoDBi EOG780RM0.
PhylomeDBi P14625.
TreeFami TF105969.

Enzyme and pathway databases

Reactomei REACT_118632. Trafficking and processing of endosomal TLR.
REACT_163699. Scavenging by Class A Receptors.
REACT_18423. ATF6-alpha activates chaperone genes.

Miscellaneous databases

ChiTaRSi HSP90B1. human.
GeneWikii HSP90B1.
GenomeRNAii 7184.
NextBioi 28164.
PMAP-CutDB P14625.
PROi P14625.
SOURCEi Search...

Gene expression databases

Bgeei P14625.
CleanExi HS_HSP90B1.
ExpressionAtlasi P14625. baseline and differential.
Genevestigatori P14625.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF00183. HSP90. 1 hit.
[Graphical view ]
PIRSFi PIRSF002583. Hsp90. 1 hit.
PRINTSi PR00775. HEATSHOCK90.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins."
    Maki R.G., Old L.J., Srivastava P.K.
    Proc. Natl. Acad. Sci. U.S.A. 87:5658-5662(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    Tissue: Blood.
  2. "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].
    Tissue: Skin.
  3. "Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors."
    Chang S.C., Erwin A.E., Lee A.S.
    Mol. Cell. Biol. 9:2153-2162(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    Tissue: Liver.
  4. "The association of heat shock protein gp96 with HBV-derived peptides in vitro."
    Meng S., Tien P.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-803.
    Tissue: Liver.
  5. "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 22-39.
    Tissue: Platelet.
  6. "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.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  8. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-217 AND ASN-445.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone."
    Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
    Nat. Commun. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNPY3; TLR4 AND TLR9.
  11. Erratum
    Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
    Nat. Commun. 3:653-653(2012)
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  13. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
    Tissue: Platelet.
  14. "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."
    Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.
    Nat. Cell Biol. 10:272-282(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH OS9.
  15. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-107; ASN-217 AND ASN-445.
    Tissue: Liver.
  16. "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-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
    Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
    PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH METTL23.

Entry informationi

Entry nameiENPL_HUMAN
AccessioniPrimary (citable) accession number: P14625
Secondary accession number(s): Q96A97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 26, 2014
This is version 177 of the entry and version 1 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
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3