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Protein

Beta-sarcoglycan

Gene

SGCB

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

Functioni

Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-sarcoglycan
Short name:
Beta-SG
Alternative name(s):
43 kDa dystrophin-associated glycoprotein
Short name:
43DAG
A3b
Gene namesi
Name:SGCB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10806. SGCB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6565CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei66 – 8621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini87 – 318232ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • dystrophin-associated glycoprotein complex Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • sarcoglycan complex Source: ProtInc
  • sarcolemma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Limb-girdle muscular dystrophy 2E (LGMD2E)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive degenerative myopathy characterized by pelvic and shoulder muscle wasting, onset usually in childhood and variable progression rate.

See also OMIM:604286
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911R → C in LGMD2E. 1 Publication
VAR_010422
Natural varianti91 – 911R → L in LGMD2E. 1 Publication
VAR_010391
Natural varianti91 – 911R → P in LGMD2E. 1 Publication
Corresponds to variant rs28936384 [ dbSNP | Ensembl ].
VAR_010392
Natural varianti100 – 1001M → K in LGMD2E. 1 Publication
Corresponds to variant rs28936386 [ dbSNP | Ensembl ].
VAR_010393
Natural varianti108 – 1081L → R in LGMD2E. 1 Publication
VAR_010394
Natural varianti114 – 1141S → F in LGMD2E or DMD-like. 1 Publication
VAR_010423
Natural varianti119 – 1191I → F in LGMD2E. 1 Publication
VAR_010424
Natural varianti151 – 1511T → R in LGMD2E. 1 Publication
Corresponds to variant rs28936383 [ dbSNP | Ensembl ].
VAR_010395
Natural varianti167 – 1671G → S in LGMD2E.
VAR_010426

Keywords - Diseasei

Disease mutation, Limb-girdle muscular dystrophy

Organism-specific databases

MIMi604286. phenotype.
Orphaneti119. Autosomal recessive limb-girdle muscular dystrophy type 2E.
PharmGKBiPA35717.

Polymorphism and mutation databases

BioMutaiSGCB.
DMDMi13431857.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Beta-sarcoglycanPRO_0000175242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi158 – 1581N-linked (GlcNAc...)1 Publication
Glycosylationi211 – 2111N-linked (GlcNAc...)1 Publication
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi288 ↔ 314Sequence Analysis
Disulfide bondi290 ↔ 307Sequence Analysis

Post-translational modificationi

Disulfide bonds are present.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ16585.
PaxDbiQ16585.
PRIDEiQ16585.

PTM databases

PhosphoSiteiQ16585.

Miscellaneous databases

PMAP-CutDBQ16585.

Expressioni

Tissue specificityi

Highest expression in heart and skeletal muscle. Low expression in brain, kidney, placenta, pancreas and lung. High expression in fetal brain. Also found in fetal lung, kidney and liver.

Gene expression databases

BgeeiQ16585.
CleanExiHS_SGCB.
ExpressionAtlasiQ16585. baseline and differential.
GenevisibleiQ16585. HS.

Organism-specific databases

HPAiHPA011422.
HPA058656.

Interactioni

Subunit structurei

Cross-link to form 2 major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The association between SGCB and SGCG is particularly strong while SGCA is loosely associated with the other sarcoglycans (By similarity).By similarity

Protein-protein interaction databases

BioGridi112341. 3 interactions.
IntActiQ16585. 1 interaction.
STRINGi9606.ENSP00000370839.

Structurei

3D structure databases

ProteinModelPortaliQ16585.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi97 – 314218Cys-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG84633.
GeneTreeiENSGT00390000008110.
HOGENOMiHOG000133159.
HOVERGENiHBG004508.
InParanoidiQ16585.
KOiK12566.
OMAiNMGCQTS.
OrthoDBiEOG74R1R4.
PhylomeDBiQ16585.
TreeFamiTF313538.

Family and domain databases

InterProiIPR006875. Sarcoglycan.
IPR027659. Sgcb.
[Graphical view]
PANTHERiPTHR21142. PTHR21142. 1 hit.
PfamiPF04790. Sarcoglycan_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16585-1) [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
MAAAAAAAAE QQSSNGPVKK SMREKAVERR SVNKEHNSNF KAGYIPIDED
60 70 80 90 100
RLHKTGLRGR KGNLAICVII LLFILAVINL IITLVIWAVI RIGPNGCDSM
110 120 130 140 150
EFHESGLLRF KQVSDMGVIH PLYKSTVGGR RNENLVITGN NQPIVFQQGT
160 170 180 190 200
TKLSVENNKT SITSDIGMQF FDPRTQNILF STDYETHEFH LPSGVKSLNV
210 220 230 240 250
QKASTERITS NATSDLNIKV DGRAIVRGNE GVFIMGKTIE FHMGGNMELK
260 270 280 290 300
AENSIILNGS VMVSTTRLPS SSSGDQLGSG DWVRYKLCMC ADGTLFKVQV
310
TSQNMGCQIS DNPCGNTH
Length:318
Mass (Da):34,777
Last modified:November 1, 1996 - v1
Checksum:iDAC5E93D1AB6C80C
GO
Isoform 2 (identifier: Q16585-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     12-81: Missing.

Note: No experimental confirmation available.
Show »
Length:248
Mass (Da):26,924
Checksum:i8ADEB947A629AC43
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111Q → E in DMD-like. 1 Publication
VAR_010421
Natural varianti91 – 911R → C in LGMD2E. 1 Publication
VAR_010422
Natural varianti91 – 911R → L in LGMD2E. 1 Publication
VAR_010391
Natural varianti91 – 911R → P in LGMD2E. 1 Publication
Corresponds to variant rs28936384 [ dbSNP | Ensembl ].
VAR_010392
Natural varianti100 – 1001M → K in LGMD2E. 1 Publication
Corresponds to variant rs28936386 [ dbSNP | Ensembl ].
VAR_010393
Natural varianti108 – 1081L → R in LGMD2E. 1 Publication
VAR_010394
Natural varianti114 – 1141S → F in LGMD2E or DMD-like. 1 Publication
VAR_010423
Natural varianti119 – 1191I → F in LGMD2E. 1 Publication
VAR_010424
Natural varianti139 – 1391G → D in DMD-like. 1 Publication
VAR_010425
Natural varianti151 – 1511T → R in LGMD2E. 1 Publication
Corresponds to variant rs28936383 [ dbSNP | Ensembl ].
VAR_010395
Natural varianti167 – 1671G → S in LGMD2E.
VAR_010426
Natural varianti182 – 1821T → A in DMD-like. 1 Publication
VAR_010427
Natural varianti184 – 1841Y → C in DMD-like. 1 Publication
VAR_010428

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei12 – 8170Missing in isoform 2. 1 PublicationVSP_056894Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31116 mRNA. Translation: AAA87034.1.
U29586 mRNA. Translation: AAB41291.1.
U63801
, U63796, U63797, U63798, U63800 Genomic DNA. Translation: AAB46956.1.
Y09781 Genomic DNA. Translation: CAA70920.1.
AK299765 mRNA. Translation: BAH13121.1.
AC093858 Genomic DNA. No translation available.
BC020709 mRNA. Translation: AAH20709.1.
CCDSiCCDS3488.1. [Q16585-1]
PIRiI39151.
RefSeqiNP_000223.1. NM_000232.4. [Q16585-1]
XP_011532705.1. XM_011534403.1. [Q16585-2]
UniGeneiHs.438953.

Genome annotation databases

EnsembliENST00000381431; ENSP00000370839; ENSG00000163069.
GeneIDi6443.
KEGGihsa:6443.
UCSCiuc003gzj.2. human. [Q16585-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Leiden Muscular Dystrophy pages

SGCB mutations in LGMD2E

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31116 mRNA. Translation: AAA87034.1.
U29586 mRNA. Translation: AAB41291.1.
U63801
, U63796, U63797, U63798, U63800 Genomic DNA. Translation: AAB46956.1.
Y09781 Genomic DNA. Translation: CAA70920.1.
AK299765 mRNA. Translation: BAH13121.1.
AC093858 Genomic DNA. No translation available.
BC020709 mRNA. Translation: AAH20709.1.
CCDSiCCDS3488.1. [Q16585-1]
PIRiI39151.
RefSeqiNP_000223.1. NM_000232.4. [Q16585-1]
XP_011532705.1. XM_011534403.1. [Q16585-2]
UniGeneiHs.438953.

3D structure databases

ProteinModelPortaliQ16585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112341. 3 interactions.
IntActiQ16585. 1 interaction.
STRINGi9606.ENSP00000370839.

PTM databases

PhosphoSiteiQ16585.

Polymorphism and mutation databases

BioMutaiSGCB.
DMDMi13431857.

Proteomic databases

MaxQBiQ16585.
PaxDbiQ16585.
PRIDEiQ16585.

Protocols and materials databases

DNASUi6443.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381431; ENSP00000370839; ENSG00000163069.
GeneIDi6443.
KEGGihsa:6443.
UCSCiuc003gzj.2. human. [Q16585-1]

Organism-specific databases

CTDi6443.
GeneCardsiGC04M052886.
GeneReviewsiSGCB.
HGNCiHGNC:10806. SGCB.
HPAiHPA011422.
HPA058656.
MIMi600900. gene.
604286. phenotype.
neXtProtiNX_Q16585.
Orphaneti119. Autosomal recessive limb-girdle muscular dystrophy type 2E.
PharmGKBiPA35717.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG84633.
GeneTreeiENSGT00390000008110.
HOGENOMiHOG000133159.
HOVERGENiHBG004508.
InParanoidiQ16585.
KOiK12566.
OMAiNMGCQTS.
OrthoDBiEOG74R1R4.
PhylomeDBiQ16585.
TreeFamiTF313538.

Miscellaneous databases

ChiTaRSiSGCB. human.
GeneWikiiSGCB.
GenomeRNAii6443.
NextBioi25039.
PMAP-CutDBQ16585.
PROiQ16585.
SOURCEiSearch...

Gene expression databases

BgeeiQ16585.
CleanExiHS_SGCB.
ExpressionAtlasiQ16585. baseline and differential.
GenevisibleiQ16585. HS.

Family and domain databases

InterProiIPR006875. Sarcoglycan.
IPR027659. Sgcb.
[Graphical view]
PANTHERiPTHR21142. PTHR21142. 1 hit.
PfamiPF04790. Sarcoglycan_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Beta-sarcoglycan (A3b) mutations cause autosomal recessive muscular dystrophy with loss of the sarcoglycan complex."
    Boennemann C.G., Modi R., Noguchi S., Mizuno Y., Yoshida M., Gussoni E., McNally E.M., Duggan D.J., Angelini C., Hoffman E.P., Ozawa E., Kunkel L.M.
    Nat. Genet. 11:266-273(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 42-54; 112-173; 175-192 AND 228-253, DISEASE.
    Tissue: Skeletal muscle.
  3. "Genomic screening for beta-sarcoglycan gene mutations: missense mutations may cause severe limb-girdle muscular dystrophy type 2E (LGMD 2E)."
    Bonnemann C.G., Passos-Bueno M.R., McNally E.M., Vainzof M., de Sa Moreira E., Marie S.K., Pavanello R.C., Noguchi S., Ozawa E., Zatz M., Kunkel L.M.
    Hum. Mol. Genet. 5:1953-1961(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS LGMD2E PRO-91; LYS-100 AND ARG-108.
  4. Bourg N.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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 2).
    Tissue: Brain.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Placenta.
  8. "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-158 AND ASN-211.
    Tissue: Liver.
  9. "LGMD 2E in Tunisia is caused by a homozygous missense mutation in beta-sarcoglycan exon 3."
    Bonnemann C.G., Wong J., Ben-Hamida C., Ben-Hamida M., Hentati F., Kunkel L.M.
    Neuromuscul. Disord. 8:193-197(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LGMD2E LEU-91.
  10. "Mutations in the sarcoglycan genes in patients with myopathy."
    Duggan D.J., Gorospe J.R., Fanin M., Hoffman E.P., Angelini C.
    N. Engl. J. Med. 336:618-624(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DMD-LIKE GLU-11; PHE-114; ASP-139 AND ALA-182.
  11. "Novel mutation (Y184C) in exon 4 of the beta-sarcoglycan gene identified in a Portuguese patient."
    dos Santos M.R., Jorge P., Ribeiro E.M., Pires M.M., Guimaraes A.
    Hum. Mutat. 12:214-215(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DMD-LIKE CYS-184.
  12. "Beta-sarcoglycan: genomic analysis and identification of a novel missense mutation in the LGMD2E Amish isolate."
    Duclos F., Broux O., Bourg N., Straub V., Feldman G.L., Sunada Y., Lim L.E., Piccolo F., Cutshall S., Gary F., Quetier F., Kaplan J.C., Jackson C.E., Beckmann J.S., Campbell K.P.
    Neuromuscul. Disord. 8:30-38(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LGMD2E CYS-91; PHE-119 AND ARG-151.

Entry informationi

Entry nameiSGCB_HUMAN
AccessioniPrimary (citable) accession number: Q16585
Secondary accession number(s): B7Z635, O00661
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 136 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.