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P49257

- LMAN1_HUMAN

UniProt

P49257 - LMAN1_HUMAN

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Protein

Protein ERGIC-53

Gene

LMAN1

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

Functioni

Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881CarbohydratePROSITE-ProRule annotation
Binding sitei121 – 1211CarbohydratePROSITE-ProRule annotation
Metal bindingi152 – 1521Calcium
Metal bindingi154 – 1541Calcium; via carbonyl oxygen
Metal bindingi156 – 1561Calcium
Binding sitei156 – 1561CarbohydratePROSITE-ProRule annotation
Binding sitei178 – 1781CarbohydratePROSITE-ProRule annotation
Metal bindingi181 – 1811Calcium
Sitei501 – 5011Required for ER export

GO - Molecular functioni

  1. mannose binding Source: ProtInc
  2. metal ion binding Source: UniProtKB-KW
  3. unfolded protein binding Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: ProtInc
  2. cellular protein metabolic process Source: Reactome
  3. endoplasmic reticulum organization Source: Ensembl
  4. ER to Golgi vesicle-mediated transport Source: ProtInc
  5. Golgi organization Source: UniProtKB
  6. positive regulation of organelle organization Source: UniProtKB
  7. post-translational protein modification Source: Reactome
  8. protein folding Source: ProtInc
  9. protein N-linked glycosylation via asparagine Source: Reactome
  10. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_25046. Transport to the Golgi and subsequent modification.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ERGIC-53
Alternative name(s):
ER-Golgi intermediate compartment 53 kDa protein
Gp58
Intracellular mannose-specific lectin MR60
Lectin mannose-binding 1
Gene namesi
Name:LMAN1
Synonyms:ERGIC53, F5F8D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:6631. LMAN1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  2. endoplasmic reticulum membrane Source: ProtInc
  3. ER to Golgi transport vesicle membrane Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. Golgi membrane Source: ProtInc
  6. integral component of membrane Source: ProtInc
  7. membrane Source: UniProtKB
  8. sarcomere Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Factor V and factor VIII combined deficiency 1 (F5F8D1) [MIM:227300]: A blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi227300. phenotype.
Orphaneti35909. Combined deficiency of factor V and factor VIII.
PharmGKBiPA30399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30303 PublicationsAdd
BLAST
Chaini31 – 510480Protein ERGIC-53PRO_0000017660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi190 ↔ 230
Disulfide bondi466 – 466Interchain
Disulfide bondi475 – 475Interchain

Post-translational modificationi

The N-terminal may be partly blocked.

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP49257.
PaxDbiP49257.
PeptideAtlasiP49257.
PRIDEiP49257.

PTM databases

PhosphoSiteiP49257.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiP49257.
GenevestigatoriP49257.

Organism-specific databases

HPAiCAB037163.
HPA002320.

Interactioni

Subunit structurei

Exists both as a covalent disulfide-linked homohexamer, and a complex of three disulfide-linked dimers non-covalently kept together. Interacts with MCFD2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERP44Q9BS263EBI-1057738,EBI-541644
SURF4O152603EBI-1057738,EBI-1044848

Protein-protein interaction databases

BioGridi110185. 31 interactions.
DIPiDIP-42188N.
IntActiP49257. 8 interactions.
MINTiMINT-4999949.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 464Combined sources
Helixi48 – 503Combined sources
Beta strandi52 – 565Combined sources
Beta strandi67 – 715Combined sources
Beta strandi80 – 834Combined sources
Beta strandi85 – 884Combined sources
Beta strandi90 – 978Combined sources
Beta strandi102 – 11312Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi122 – 1309Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi164 – 17310Combined sources
Helixi178 – 1803Combined sources
Helixi183 – 1853Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi201 – 2088Combined sources
Beta strandi211 – 2177Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi240 – 24910Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi256 – 26611Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A4UX-ray1.84A31-285[»]
3LCPX-ray2.45A/B32-277[»]
3WHTX-ray1.80A31-269[»]
3WHUX-ray2.60A31-269[»]
3WNXX-ray2.75A31-269[»]
4GKXX-ray2.70A/B/C/D/E/F31-270[»]
4GKYX-ray2.42A31-270[»]
ProteinModelPortaliP49257.
SMRiP49257. Positions 41-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49257.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 477447LumenalSequence AnalysisAdd
BLAST
Topological domaini499 – 51012CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei478 – 49821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 267224L-type lectin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2533Carbohydrate bindingPROSITE-ProRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi509 – 5102ER export motif

Domaini

The FF ER export motif at the C-terminus is not sufficient to support endoplasmic reticulum exit, and needs assistance of Gln-501 for proper recognition of COPII coat components.

Sequence similaritiesi

Contains 1 L-type lectin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292314.
GeneTreeiENSGT00530000062977.
HOVERGENiHBG052332.
InParanoidiP49257.
KOiK10080.
OMAiGTVPFWA.
OrthoDBiEOG7QC7VR.
PhylomeDBiP49257.
TreeFamiTF313311.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR005052. Lectin_leg.
[Graphical view]
PANTHERiPTHR12223. PTHR12223. 1 hit.
PfamiPF03388. Lectin_leg-like. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49257-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGSRQRGLR ARVRPLFCAL LLSLGRFVRG DGVGGDPAVA LPHRRFEYKY
60 70 80 90 100
SFKGPHLVQS DGTVPFWAHA GNAIPSSDQI RVAPSLKSQR GSVWTKTKAA
110 120 130 140 150
FENWEVEVTF RVTGRGRIGA DGLAIWYAEN QGLEGPVFGS ADLWNGVGIF
160 170 180 190 200
FDSFDNDGKK NNPAIVIIGN NGQIHYDHQN DGASQALASC QRDFRNKPYP
210 220 230 240 250
VRAKITYYQN TLTVMINNGF TPDKNDYEFC AKVENMIIPA QGHFGISAAT
260 270 280 290 300
GGLADDHDVL SFLTFQLTEP GKEPPTPDKE ISEKEKEKYQ EEFEHFQQEL
310 320 330 340 350
DKKKEEFQKG HPDLQGQPAE EIFESVGDRE LRQVFEGQNR IHLEIKQLNR
360 370 380 390 400
QLDMILDEQR RYVSSLTEEI SKRGAGMPGQ HGQITQQELD TVVKTQHEIL
410 420 430 440 450
RQVNEMKNSM SETVRLVSGM QHPGSAGGVY ETTQHFIDIK EHLHIVKRDI
460 470 480 490 500
DNLVQRNMPS NEKPKCPELP PFPSCLSTVH FIIFVVVQTV LFIGYIMYRS
510
QQEAAAKKFF
Length:510
Mass (Da):57,549
Last modified:August 13, 2002 - v2
Checksum:iB87EF117C0CD386C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531S → T in CAA50653. (PubMed:8223692)Curated

Mass spectrometryi

Molecular mass is 54222.91 Da from positions 31 - 510. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141R → Q.1 Publication
Corresponds to variant rs1043302 [ dbSNP | Ensembl ].
VAR_013703
Natural varianti39 – 391V → A.1 Publication
Corresponds to variant rs33926449 [ dbSNP | Ensembl ].
VAR_013704
Natural varianti355 – 3551I → T.
Corresponds to variant rs3737392 [ dbSNP | Ensembl ].
VAR_049770
Natural varianti410 – 4101M → L.2 Publications
Corresponds to variant rs2298711 [ dbSNP | Ensembl ].
VAR_013705

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71661 mRNA. Translation: CAA50653.1.
U09716 mRNA. Translation: AAA95960.1.
AF081866, AF081865 Genomic DNA. Translation: AAD32479.1.
AF081867 Genomic DNA. Translation: AAD32480.1.
AF081869, AF081868 Genomic DNA. Translation: AAD32481.1.
AF081871, AF081870 Genomic DNA. Translation: AAD32482.1.
AF081873, AF081872 Genomic DNA. Translation: AAD32483.1.
AF081875, AF081874 Genomic DNA. Translation: AAD32484.1.
AF081877, AF081876 Genomic DNA. Translation: AAD32485.1.
AF081879, AF081878 Genomic DNA. Translation: AAD32486.1.
AF081880 Genomic DNA. Translation: AAD32487.1.
AF081882, AF081881 Genomic DNA. Translation: AAD32488.1.
AF081884, AF081883 Genomic DNA. Translation: AAD32489.1.
AF081885 Genomic DNA. Translation: AAD32490.1.
BC032330 mRNA. Translation: AAH32330.1.
CCDSiCCDS11974.1.
PIRiS42626.
RefSeqiNP_005561.1. NM_005570.3.
UniGeneiHs.465295.

Genome annotation databases

EnsembliENST00000251047; ENSP00000251047; ENSG00000074695.
GeneIDi3998.
KEGGihsa:3998.
UCSCiuc002lhz.3. human.

Polymorphism databases

DMDMi22261801.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71661 mRNA. Translation: CAA50653.1 .
U09716 mRNA. Translation: AAA95960.1 .
AF081866 , AF081865 Genomic DNA. Translation: AAD32479.1 .
AF081867 Genomic DNA. Translation: AAD32480.1 .
AF081869 , AF081868 Genomic DNA. Translation: AAD32481.1 .
AF081871 , AF081870 Genomic DNA. Translation: AAD32482.1 .
AF081873 , AF081872 Genomic DNA. Translation: AAD32483.1 .
AF081875 , AF081874 Genomic DNA. Translation: AAD32484.1 .
AF081877 , AF081876 Genomic DNA. Translation: AAD32485.1 .
AF081879 , AF081878 Genomic DNA. Translation: AAD32486.1 .
AF081880 Genomic DNA. Translation: AAD32487.1 .
AF081882 , AF081881 Genomic DNA. Translation: AAD32488.1 .
AF081884 , AF081883 Genomic DNA. Translation: AAD32489.1 .
AF081885 Genomic DNA. Translation: AAD32490.1 .
BC032330 mRNA. Translation: AAH32330.1 .
CCDSi CCDS11974.1.
PIRi S42626.
RefSeqi NP_005561.1. NM_005570.3.
UniGenei Hs.465295.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3A4U X-ray 1.84 A 31-285 [» ]
3LCP X-ray 2.45 A/B 32-277 [» ]
3WHT X-ray 1.80 A 31-269 [» ]
3WHU X-ray 2.60 A 31-269 [» ]
3WNX X-ray 2.75 A 31-269 [» ]
4GKX X-ray 2.70 A/B/C/D/E/F 31-270 [» ]
4GKY X-ray 2.42 A 31-270 [» ]
ProteinModelPortali P49257.
SMRi P49257. Positions 41-269.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110185. 31 interactions.
DIPi DIP-42188N.
IntActi P49257. 8 interactions.
MINTi MINT-4999949.

Chemistry

DrugBanki DB00025. Antihemophilic Factor.

PTM databases

PhosphoSitei P49257.

Polymorphism databases

DMDMi 22261801.

Proteomic databases

MaxQBi P49257.
PaxDbi P49257.
PeptideAtlasi P49257.
PRIDEi P49257.

Protocols and materials databases

DNASUi 3998.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251047 ; ENSP00000251047 ; ENSG00000074695 .
GeneIDi 3998.
KEGGi hsa:3998.
UCSCi uc002lhz.3. human.

Organism-specific databases

CTDi 3998.
GeneCardsi GC18M056969.
HGNCi HGNC:6631. LMAN1.
HPAi CAB037163.
HPA002320.
MIMi 227300. phenotype.
601567. gene.
neXtProti NX_P49257.
Orphaneti 35909. Combined deficiency of factor V and factor VIII.
PharmGKBi PA30399.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292314.
GeneTreei ENSGT00530000062977.
HOVERGENi HBG052332.
InParanoidi P49257.
KOi K10080.
OMAi GTVPFWA.
OrthoDBi EOG7QC7VR.
PhylomeDBi P49257.
TreeFami TF313311.

Enzyme and pathway databases

Reactomei REACT_25046. Transport to the Golgi and subsequent modification.

Miscellaneous databases

EvolutionaryTracei P49257.
GeneWikii LMAN1.
GenomeRNAii 3998.
NextBioi 15688.
PROi P49257.
SOURCEi Search...

Gene expression databases

Bgeei P49257.
Genevestigatori P49257.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR005052. Lectin_leg.
[Graphical view ]
PANTHERi PTHR12223. PTHR12223. 1 hit.
Pfami PF03388. Lectin_leg-like. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif."
    Schindler R., Itin C., Zerial M., Lottspeich F., Hauri H.-P.
    Eur. J. Cell Biol. 61:1-9(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-59 AND 418-432.
    Tissue: Liver and Placenta.
  2. "ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells."
    Arar C., Carpentier V., Le Caer J.-P., Monsigny M., Legrand A., Roche A.-C.
    J. Biol. Chem. 270:3551-3553(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-41.
    Tissue: Peripheral blood.
  3. "ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families."
    Nichols W.C., Terry V.H., Wheatley M.A., Yang A., Zivelin A., Ciavarella N., Stefanile C., Matsushita T., Saito H., de Bosch N.B., Ruiz-Saez A., Torres A., Thompson A.R., Feinstein D.I., White G.C., Negrier C., Vinciguerra C., Aktan M.
    , Kaufman R.J., Ginsburg D., Seligsohn U.
    Blood 93:2261-2266(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-14; ALA-39 AND LEU-410, INVOLVEMENT IN F5F8D1.
  4. "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], VARIANT LEU-410.
    Tissue: Brain.
  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 31-44.
    Tissue: Platelet.
  6. "A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins."
    Fiedler K., Simons K.
    Cell 77:625-626(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO LEGUMINOUS LECTINS.
  7. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  8. "ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains."
    Nufer O., Kappeler F., Guldbrandsen S., Hauri H.-P.
    J. Cell Sci. 116:4429-4440(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MOTIF ER EXPORT, DISULFIDE BOND.
  9. Cited for: INTERACTION WITH MCFD2, FUNCTION.
  10. "Oligomerization and intracellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds."
    Neve E.P., Lahtinen U., Pettersson R.F.
    J. Mol. Biol. 354:556-568(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERCHAIN DISULFIDE BONDS.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII."
    Wigren E., Bourhis J.M., Kursula I., Guy J.E., Lindqvist Y.
    FEBS Lett. 584:878-882(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 32-277 IN COMPLEX WITH MCFD2 AND CALCIUM IONS, SUBUNIT, DISULFIDE BOND.
  13. "Structural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiency."
    Nishio M., Kamiya Y., Mizushima T., Wakatsuki S., Sasakawa H., Yamamoto K., Uchiyama S., Noda M., McKay A.R., Fukui K., Hauri H.P., Kato K.
    Proc. Natl. Acad. Sci. U.S.A. 107:4034-4039(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 31-285 IN COMPLEX WITH CALCIUM IONS, SUBUNIT, DISULFIDE BOND.

Entry informationi

Entry nameiLMAN1_HUMAN
AccessioniPrimary (citable) accession number: P49257
Secondary accession number(s): Q12895
, Q8N5I7, Q9UQG1, Q9UQG2, Q9UQG3, Q9UQG4, Q9UQG5, Q9UQG6, Q9UQG7, Q9UQG8, Q9UQG9, Q9UQH0, Q9UQH1, Q9UQH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 13, 2002
Last modified: October 29, 2014
This is version 151 of the entry and version 2 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 18
    Human chromosome 18: 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