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P14625

- ENPL_HUMAN

UniProt

P14625 - ENPL_HUMAN

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Protein
Endoplasmin
Gene
HSP90B1, GRP94, TRA1
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.1 Publication

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. actin rod assembly Source: MGI
  3. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  4. cellular protein metabolic process Source: Reactome
  5. cellular response to ATP Source: MGI
  6. endoplasmic reticulum unfolded protein response Source: Reactome
  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.2 Publications

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 region Source: Reactome
  7. extracellular vesicular exosome Source: UniProt
  8. melanosome Source: UniProtKB-SubCell
  9. midbody Source: UniProtKB
  10. nucleus Source: UniProt
  11. perinuclear region of cytoplasm Source: UniProtKB
  12. 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 Publication
Add
BLAST
Chaini22 – 803782EndoplasminUniRule annotation
PRO_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 – 138Interchain By similarity
Glycosylationi217 – 2171N-linked (GlcNAc...)2 Publications
Modified residuei306 – 3061Phosphoserine2 Publications
Modified residuei404 – 4041N6-succinyllysine By similarity
Glycosylationi445 – 4451N-linked (GlcNAc...)2 Publications
Modified residuei479 – 4791N6-acetyllysine By similarity
Glycosylationi481 – 4811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi502 – 5021N-linked (GlcNAc...) Reviewed prediction
Modified residuei633 – 6331N6-succinyllysine By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP14625.
PaxDbiP14625.
PeptideAtlasiP14625.
PRIDEiP14625.

2D gel databases

DOSAC-COBS-2DPAGEiP14625.
OGPiP14625.
REPRODUCTION-2DPAGEiIPI00027230.

PTM databases

PhosphoSiteiP14625.

Miscellaneous databases

PMAP-CutDBiP14625.

Expressioni

Gene expression databases

ArrayExpressiP14625.
BgeeiP14625.
CleanExiHS_HSP90B1.
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 METTL23.3 Publications

Protein-protein interaction databases

BioGridi113036. 79 interactions.
DIPiDIP-36060N.
IntActiP14625. 40 interactions.
MINTiMINT-210408.
STRINGi9606.ENSP00000299767.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NH9X-ray2.77A69-337[»]
ProteinModelPortaliP14625.
SMRiP14625. Positions 72-755.

Family & Domainsi

Motif

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

Sequence similaritiesi

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_ATP-bd.
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

MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ    50
REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF 100
LRELISNASD ALDKIRLISL TDENALSGNE ELTVKIKCDK EKNLLHVTDT 150
GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY 200
SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV 250
LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK 300
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV 350
EEDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE 400
YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET 450
LQQHKLLKVI RKKLVRKTLD MIKKIADDKY NDTFWKEFGT NIKLGVIEDH 500
SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE 550
SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE 600
SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS 650
QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR 700
IKEDEDDKTV LDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID 750
PDAKVEEEPE EEPEETAEDT TEDTEQDEDE EMDVGTDEEE ETAKESTAEK 800
DEL 803
Length:803
Mass (Da):92,469
Last modified:April 1, 1990 - v1
Checksum:i9BF6705A7A2ED0D0
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

Protein-protein interaction databases

BioGridi 113036. 79 interactions.
DIPi DIP-36060N.
IntActi P14625. 40 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-2DPAGEi P14625.
OGPi P14625.
REPRODUCTION-2DPAGEi 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-InvDBi 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-CutDBi P14625.
PROi P14625.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14625.
Bgeei P14625.
CleanExi HS_HSP90B1.
Genevestigatori P14625.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_ATP-bd.
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: September 3, 2014
This is version 174 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

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