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Q9BUN8

- DERL1_HUMAN

UniProt

Q9BUN8 - DERL1_HUMAN

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Protein

Derlin-1

Gene

DERL1

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

Functioni

Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class I heavy chains. Also participates in the degradation process of misfolded cytomegalovirus US2 protein.2 Publications

GO - Molecular functioni

  1. MHC class I protein binding Source: UniProtKB
  2. receptor activity Source: UniProtKB

GO - Biological processi

  1. endoplasmic reticulum unfolded protein response Source: UniProtKB
  2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. establishment of protein localization Source: UniProtKB
  4. intracellular transport of viral protein in host cell Source: UniProtKB
  5. response to unfolded protein Source: MGI
  6. retrograde protein transport, ER to cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport, Unfolded protein response

Protein family/group databases

TCDBi3.A.16.1.1. the endoplasmic reticular retrotranslocon (er-rt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Derlin-1
Alternative name(s):
Degradation in endoplasmic reticulum protein 1
Short name:
DERtrin-1
Der1-like protein 1
Gene namesi
Name:DERL1
Synonyms:DER1
ORF Names:UNQ243/PRO276
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:28454. DERL1.

Subcellular locationi

Endoplasmic reticulum membrane 4 Publications; Multi-pass membrane protein 4 Publications

GO - Cellular componenti

  1. early endosome Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB
  3. Hrd1p ubiquitin ligase complex Source: UniProt
  4. integral component of endoplasmic reticulum membrane Source: UniProtKB
  5. integral component of membrane Source: MGI
  6. late endosome Source: Ensembl
  7. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134926638.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 251250Derlin-1PRO_0000219042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei202 – 2021Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BUN8.
PaxDbiQ9BUN8.
PRIDEiQ9BUN8.

PTM databases

PhosphoSiteiQ9BUN8.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Inductioni

Up-regulated in response to endoplasmic reticulum stress via the ERN1-XBP1 pathway of the unfolded protein response (UPR).By similarity

Gene expression databases

BgeeiQ9BUN8.
CleanExiHS_DERL1.
ExpressionAtlasiQ9BUN8. baseline and differential.
GenevestigatoriQ9BUN8.

Organism-specific databases

HPAiHPA016562.

Interactioni

Subunit structurei

Forms homo- and heterooligomers with DERL2 and DERL3; binding to DERL3 is poorer than that between DERL2 and DERL3. Interacts with AMFR, VIMP/SELS, SEL1L, SELK, SYVN1 and VCP, as well as with SEL1L-SYVN1 and VCP-VIMP protein complexes; this interaction is weaker than that observed between DERL2 and these complexes. Interacts with the cytomegalovirus US11 protein. Interacts with NGLY1 and YOD1. Does not bind to EDEM1. Interacts with DNAJB9 and RNF103. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAP31P515723EBI-398977,EBI-77683
CFTRP135692EBI-398977,EBI-349854

Protein-protein interaction databases

BioGridi122559. 43 interactions.
IntActiQ9BUN8. 8 interactions.
STRINGi9606.ENSP00000259512.

Structurei

3D structure databases

ProteinModelPortaliQ9BUN8.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2221CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini44 – 5916LumenalSequence AnalysisAdd
BLAST
Topological domaini81 – 10525CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini127 – 15428LumenalSequence AnalysisAdd
BLAST
Topological domaini176 – 25176CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 4321Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei60 – 8021Helical; Name=2Sequence AnalysisAdd
BLAST
Transmembranei106 – 12621Helical; Name=3Sequence AnalysisAdd
BLAST
Transmembranei155 – 17521Helical; Name=4Sequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the derlin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5291.
GeneTreeiENSGT00530000063156.
HOGENOMiHOG000200949.
HOVERGENiHBG105143.
InParanoidiQ9BUN8.
KOiK11519.
OMAiYIWCQLN.
OrthoDBiEOG7353XM.
PhylomeDBiQ9BUN8.
TreeFamiTF354297.

Family and domain databases

InterProiIPR007599. DER1.
[Graphical view]
PANTHERiPTHR11009. PTHR11009. 1 hit.
PfamiPF04511. DER1. 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: Q9BUN8-1) [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
MSDIGDWFRS IPAITRYWFA ATVAVPLVGK LGLISPAYLF LWPEAFLYRF
60 70 80 90 100
QIWRPITATF YFPVGPGTGF LYLVNLYFLY QYSTRLETGA FDGRPADYLF
110 120 130 140 150
MLLFNWICIV ITGLAMDMQL LMIPLIMSVL YVWAQLNRDM IVSFWFGTRF
160 170 180 190 200
KACYLPWVIL GFNYIIGGSV INELIGNLVG HLYFFLMFRY PMDLGGRNFL
210 220 230 240 250
STPQFLYRWL PSRRGGVSGF GVPPASMRRA ADQNGGGGRH NWGQGFRLGD

Q
Length:251
Mass (Da):28,801
Last modified:June 1, 2001 - v1
Checksum:i4A6E0DB68D9AF244
GO
Isoform 2 (identifier: Q9BUN8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-189: Missing.

Show »
Length:231
Mass (Da):26,423
Checksum:iE0D0982FDD620F1F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711I → V.
Corresponds to variant rs2272722 [ dbSNP | Ensembl ].
VAR_019516

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 18920Missing in isoform 2. 1 PublicationVSP_041329Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY358818 mRNA. Translation: AAQ89177.1.
AC104316 Genomic DNA. No translation available.
BC002457 mRNA. Translation: AAH02457.1.
AK124086 mRNA. Translation: BAG54003.1.
CCDSiCCDS47915.1. [Q9BUN8-2]
CCDS6337.1. [Q9BUN8-1]
RefSeqiNP_001128143.1. NM_001134671.2. [Q9BUN8-2]
NP_077271.1. NM_024295.5. [Q9BUN8-1]
UniGeneiHs.241576.

Genome annotation databases

EnsembliENST00000259512; ENSP00000259512; ENSG00000136986. [Q9BUN8-1]
ENST00000405944; ENSP00000384289; ENSG00000136986. [Q9BUN8-2]
GeneIDi79139.
KEGGihsa:79139.
UCSCiuc003ypl.3. human. [Q9BUN8-1]
uc003ypm.3. human. [Q9BUN8-2]

Polymorphism databases

DMDMi50400630.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY358818 mRNA. Translation: AAQ89177.1 .
AC104316 Genomic DNA. No translation available.
BC002457 mRNA. Translation: AAH02457.1 .
AK124086 mRNA. Translation: BAG54003.1 .
CCDSi CCDS47915.1. [Q9BUN8-2 ]
CCDS6337.1. [Q9BUN8-1 ]
RefSeqi NP_001128143.1. NM_001134671.2. [Q9BUN8-2 ]
NP_077271.1. NM_024295.5. [Q9BUN8-1 ]
UniGenei Hs.241576.

3D structure databases

ProteinModelPortali Q9BUN8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122559. 43 interactions.
IntActi Q9BUN8. 8 interactions.
STRINGi 9606.ENSP00000259512.

Protein family/group databases

TCDBi 3.A.16.1.1. the endoplasmic reticular retrotranslocon (er-rt) family.

PTM databases

PhosphoSitei Q9BUN8.

Polymorphism databases

DMDMi 50400630.

Proteomic databases

MaxQBi Q9BUN8.
PaxDbi Q9BUN8.
PRIDEi Q9BUN8.

Protocols and materials databases

DNASUi 79139.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259512 ; ENSP00000259512 ; ENSG00000136986 . [Q9BUN8-1 ]
ENST00000405944 ; ENSP00000384289 ; ENSG00000136986 . [Q9BUN8-2 ]
GeneIDi 79139.
KEGGi hsa:79139.
UCSCi uc003ypl.3. human. [Q9BUN8-1 ]
uc003ypm.3. human. [Q9BUN8-2 ]

Organism-specific databases

CTDi 79139.
GeneCardsi GC08M124094.
HGNCi HGNC:28454. DERL1.
HPAi HPA016562.
MIMi 608813. gene.
neXtProti NX_Q9BUN8.
PharmGKBi PA134926638.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5291.
GeneTreei ENSGT00530000063156.
HOGENOMi HOG000200949.
HOVERGENi HBG105143.
InParanoidi Q9BUN8.
KOi K11519.
OMAi YIWCQLN.
OrthoDBi EOG7353XM.
PhylomeDBi Q9BUN8.
TreeFami TF354297.

Miscellaneous databases

GenomeRNAii 79139.
NextBioi 68017.
PROi Q9BUN8.
SOURCEi Search...

Gene expression databases

Bgeei Q9BUN8.
CleanExi HS_DERL1.
ExpressionAtlasi Q9BUN8. baseline and differential.
Genevestigatori Q9BUN8.

Family and domain databases

InterProi IPR007599. DER1.
[Graphical view ]
PANTHERi PTHR11009. PTHR11009. 1 hit.
Pfami PF04511. DER1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Lymph.
  4. "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] OF 47-131 (ISOFORM 2).
    Tissue: Esophagus.
  5. "A membrane protein required for dislocation of misfolded proteins from the ER."
    Lilley B.N., Ploegh H.L.
    Nature 429:834-840(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, TISSUE SPECIFICITY, INTERACTION WITH US11.
  6. "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol."
    Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.
    Nature 429:841-847(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH US11 AND VIMP.
  7. "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway."
    Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., Koning F., Kloetzel P.-M., Seeger M.
    J. Mol. Biol. 354:1021-1027(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCP AND SYVN1.
  8. "The retrotranslocation protein derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum."
    Katiyar S., Joshi S., Lennarz W.J.
    Mol. Biol. Cell 16:4584-4594(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NGLY1.
  9. "Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane."
    Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.
    Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMOOLIGOMERIZATION, INTERACTION WITH AMFR; SYVN1; VCP AND VIMP.
  10. "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane."
    Lilley B.N., Ploegh H.L.
    Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH VIMP; VCP; SEL1L AND SYVN1.
  11. "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation."
    Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.
    J. Cell Biol. 172:383-393(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH DERL3 AND VCP.
  12. "Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated degradation pathway."
    Maruyama Y., Yamada M., Takahashi K., Yamada M.
    Biochem. Biophys. Res. Commun. 374:737-741(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF103.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER."
    Ernst R., Mueller B., Ploegh H.L., Schlieker C.
    Mol. Cell 36:28-38(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YOD1.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
    Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SELK AND VIMP, IDENTIFICATION IN A COMPLEX WITH CANX; DERL2; DDOST; RPN1; RPN2; SELK; STT3A; VCP AND VIMP.
  17. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDERL1_HUMAN
AccessioniPrimary (citable) accession number: Q9BUN8
Secondary accession number(s): B3KW41, E9PH19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 115 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3