Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BZQ6

- EDEM3_HUMAN

UniProt

Q9BZQ6 - EDEM3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ER degradation-enhancing alpha-mannosidase-like protein 3

Gene

EDEM3

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

Functioni

Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity).By similarity

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei146 – 1461Proton donorBy similarity
Active sitei293 – 2931By similarity
Active sitei405 – 4051By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. glycoprotein endo-alpha-1,2-mannosidase activity Source: Ensembl
  3. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. glycoprotein catabolic process Source: Ensembl
  3. post-translational protein modification Source: Reactome
  4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  5. protein folding Source: Reactome
  6. protein N-linked glycosylation via asparagine Source: Reactome
  7. response to unfolded protein Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Unfolded protein response

Enzyme and pathway databases

ReactomeiREACT_25091. ER Quality Control Compartment (ERQC).

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended name:
ER degradation-enhancing alpha-mannosidase-like protein 3 (EC:3.2.1.113)
Alternative name(s):
Alpha-1,2-mannosidase EDEM3
Gene namesi
Name:EDEM3
Synonyms:C1orf22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16787. EDEM3.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Ensembl
  2. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Sequence AnalysisAdd
BLAST
Chaini42 – 932891ER degradation-enhancing alpha-mannosidase-like protein 3PRO_0000210323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)1 Publication
Glycosylationi504 – 5041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi814 – 8141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi900 – 9001N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9BZQ6.
PaxDbiQ9BZQ6.
PRIDEiQ9BZQ6.

PTM databases

PhosphoSiteiQ9BZQ6.

Expressioni

Gene expression databases

BgeeiQ9BZQ6.
CleanExiHS_EDEM3.
ExpressionAtlasiQ9BZQ6. baseline and differential.
GenevestigatoriQ9BZQ6.

Organism-specific databases

HPAiHPA025754.
HPA025755.

Interactioni

Protein-protein interaction databases

BioGridi123207. 4 interactions.
IntActiQ9BZQ6. 2 interactions.
STRINGi9606.ENSP00000318147.

Structurei

3D structure databases

ProteinModelPortaliQ9BZQ6.
SMRiQ9BZQ6. Positions 56-499, 674-737.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini674 – 779106PAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi929 – 9324Prevents secretion from ERPROSITE-ProRule annotation

Domaini

Contains a protease-associated domain (PA) of unknown function.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG307610.
GeneTreeiENSGT00530000063069.
HOGENOMiHOG000007735.
HOVERGENiHBG107835.
InParanoidiQ9BZQ6.
KOiK10086.
OMAiDRDPEME.
OrthoDBiEOG79W94G.
PhylomeDBiQ9BZQ6.
TreeFamiTF300807.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
IPR003137. Protease-assoc_domain.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
PF02225. PA. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 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: Q9BZQ6) [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
MSEAGGRGCG SPVPQRARWR LVAATAAFCL VSATSVWTAG AEPMSREEKQ
60 70 80 90 100
KLGNQVLEMF DHAYGNYMEH AYPADELMPL TCRGRVRGQE PSRGDVDDAL
110 120 130 140 150
GKFSLTLIDS LDTLVVLNKT KEFEDAVRKV LRDVNLDNDV VVSVFETNIR
160 170 180 190 200
VLGGLLGGHS LAIMLKEKGE YMQWYNDELL QMAKQLGYKL LPAFNTTSGL
210 220 230 240 250
PYPRINLKFG IRKPEARTGT ETDTCTACAG TLILEFAALS RFTGATIFEE
260 270 280 290 300
YARKALDFLW EKRQRSSNLV GVTINIHTGD WVRKDSGVGA GIDSYYEYLL
310 320 330 340 350
KAYVLLGDDS FLERFNTHYD AIMRYISQPP LLLDVHIHKP MLNARTWMDA
360 370 380 390 400
LLAFFPGLQV LKGDIRPAIE THEMLYQVIK KHNFLPEAFT TDFRVHWAQH
410 420 430 440 450
PLRPEFAEST YFLYKATGDP YYLEVGKTLI ENLNKYARVP CGFAAMKDVR
460 470 480 490 500
TGSHEDRMDS FFLAEMFKYL YLLFADKEDI IFDIEDYIFT TEAHLLPLWL
510 520 530 540 550
STTNQSISKK NTTSEYTELD DSNFDWTCPN TQILFPNDPL YAQSIREPLK
560 570 580 590 600
NVVDKSCPRG IIRVEESFRS GAKPPLRARD FMATNPEHLE ILKKMGVSLI
610 620 630 640 650
HLKDGRVQLV QHAIQAASSI DAEDGLRFMQ EMIELSSQQQ KEQQLPPRAV
660 670 680 690 700
QIVSHPFFGR VVLTAGPAQF GLDLSKHKET RGFVASSKPS NGCSELTNPE
710 720 730 740 750
AVMGKIALIQ RGQCMFAEKA RNIQNAGAIG GIVIDDNEGS SSDTAPLFQM
760 770 780 790 800
AGDGKDTDDI KIPMLFLFSK EGSIILDAIR EYEEVEVLLS DKAKDRDPEM
810 820 830 840 850
ENEEQPSSEN DSQNQSGEQI SSSSQEVDLV DQESSEENSL NSHPESLSLA
860 870 880 890 900
DMDNAASISP SEQTSNPTEN HETTNLNGEC TDLDNQLQEQ SETEEDSNPN
910 920 930
VSWGKKVQPI DSILADWNED IEAFEMMEKD EL
Length:932
Mass (Da):104,664
Last modified:February 5, 2008 - v2
Checksum:i3C040FDF48284D36
GO
Isoform 2 (identifier: Q9BZQ6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.
     796-797: RD → RAAILKGKMIPSYIINSN

Note: No experimental confirmation available.

Show »
Length:905
Mass (Da):102,005
Checksum:iA774AE3B184729A4
GO

Sequence cautioni

The sequence AAG60613.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAG37573.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti276 – 2761I → T in BAG37573. (PubMed:14702039)Curated
Sequence conflicti318 – 3192HY → VS in AAI05587. (PubMed:11318611)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti820 – 8201I → S.1 Publication
Corresponds to variant rs9425343 [ dbSNP | Ensembl ].
VAR_059306

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform 2. 1 PublicationVSP_056375Add
BLAST
Alternative sequencei796 – 7972RD → RAAILKGKMIPSYIINSN in isoform 2. 1 PublicationVSP_056376

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK315118 mRNA. Translation: BAG37573.1. Different initiation.
AL096819 Genomic DNA. Translation: CAI21741.1.
BC105586 mRNA. Translation: AAI05587.1.
BC144149 mRNA. Translation: AAI44150.1.
AF288393 mRNA. Translation: AAG60613.1. Different initiation.
AL117441 mRNA. Translation: CAB55926.1.
CCDSiCCDS1363.2. [Q9BZQ6-1]
PIRiT17236.
RefSeqiNP_079467.3. NM_025191.3.
UniGeneiHs.523811.

Genome annotation databases

EnsembliENST00000318130; ENSP00000318147; ENSG00000116406. [Q9BZQ6-1]
ENST00000367512; ENSP00000356482; ENSG00000116406. [Q9BZQ6-2]
GeneIDi80267.
KEGGihsa:80267.
UCSCiuc010pok.2. human. [Q9BZQ6-1]

Polymorphism databases

DMDMi166897965.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK315118 mRNA. Translation: BAG37573.1 . Different initiation.
AL096819 Genomic DNA. Translation: CAI21741.1 .
BC105586 mRNA. Translation: AAI05587.1 .
BC144149 mRNA. Translation: AAI44150.1 .
AF288393 mRNA. Translation: AAG60613.1 . Different initiation.
AL117441 mRNA. Translation: CAB55926.1 .
CCDSi CCDS1363.2. [Q9BZQ6-1 ]
PIRi T17236.
RefSeqi NP_079467.3. NM_025191.3.
UniGenei Hs.523811.

3D structure databases

ProteinModelPortali Q9BZQ6.
SMRi Q9BZQ6. Positions 56-499, 674-737.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123207. 4 interactions.
IntActi Q9BZQ6. 2 interactions.
STRINGi 9606.ENSP00000318147.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSitei Q9BZQ6.

Polymorphism databases

DMDMi 166897965.

Proteomic databases

MaxQBi Q9BZQ6.
PaxDbi Q9BZQ6.
PRIDEi Q9BZQ6.

Protocols and materials databases

DNASUi 80267.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318130 ; ENSP00000318147 ; ENSG00000116406 . [Q9BZQ6-1 ]
ENST00000367512 ; ENSP00000356482 ; ENSG00000116406 . [Q9BZQ6-2 ]
GeneIDi 80267.
KEGGi hsa:80267.
UCSCi uc010pok.2. human. [Q9BZQ6-1 ]

Organism-specific databases

CTDi 80267.
GeneCardsi GC01M184659.
H-InvDB HIX0001417.
HGNCi HGNC:16787. EDEM3.
HPAi HPA025754.
HPA025755.
MIMi 610214. gene.
neXtProti NX_Q9BZQ6.
PharmGKBi PA38186.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307610.
GeneTreei ENSGT00530000063069.
HOGENOMi HOG000007735.
HOVERGENi HBG107835.
InParanoidi Q9BZQ6.
KOi K10086.
OMAi DRDPEME.
OrthoDBi EOG79W94G.
PhylomeDBi Q9BZQ6.
TreeFami TF300807.

Enzyme and pathway databases

Reactomei REACT_25091. ER Quality Control Compartment (ERQC).

Miscellaneous databases

ChiTaRSi EDEM3. human.
GeneWikii EDEM3.
GenomeRNAii 80267.
NextBioi 35481352.
PROi Q9BZQ6.
SOURCEi Search...

Gene expression databases

Bgeei Q9BZQ6.
CleanExi HS_EDEM3.
ExpressionAtlasi Q9BZQ6. baseline and differential.
Genevestigatori Q9BZQ6.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
IPR003137. Protease-assoc_domain.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
PF02225. PA. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Tissue: Placenta.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-319 (ISOFORM 1).
    Tissue: Brain and Lung.
  4. "Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus."
    Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., Carpten J.D.
    Genomics 73:211-222(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-932 (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 553-932 (ISOFORM 1), VARIANT SER-820.
    Tissue: Testis.
  6. "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-195.
    Tissue: Liver.

Entry informationi

Entry nameiEDEM3_HUMAN
AccessioniPrimary (citable) accession number: Q9BZQ6
Secondary accession number(s): B2RCH6
, B7ZLZ2, Q0VGM5, Q5TEZ0, Q9HCW1, Q9UFV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: February 5, 2008
Last modified: October 29, 2014
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3