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Protein

Protein SMG5

Gene

SMG5

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

Functioni

Plays a role in nonsense-mediated mRNA decay. Does not have RNase activity by itself. Promotes dephosphorylation of UPF1. Together with SMG7 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Necessary for TERT activity.1 Publication

GO - Molecular functioni

  • DNA polymerase binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • protein phosphatase 2A binding Source: HGNC
  • telomeric DNA binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  • gene expression Source: Reactome
  • mRNA export from nucleus Source: HGNC
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: HGNC
  • regulation of dephosphorylation Source: HGNC
  • regulation of telomere maintenance Source: BHF-UCL
  • regulation of telomere maintenance via telomerase Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Nonsense-mediated mRNA decay

Enzyme and pathway databases

ReactomeiR-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SMG5
Alternative name(s):
EST1-like protein B
LPTS-RP1
LPTS-interacting protein
SMG-5 homolog
Short name:
hSMG-5
Gene namesi
Name:SMG5
Synonyms:EST1B, KIAA1089
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24644. SMG5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi860 – 8601D → A: Abolishes stimulation of RENT1 dephosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA143485617.

Polymorphism and mutation databases

BioMutaiSMG5.
DMDMi84029494.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 10161015Protein SMG5PRO_0000076322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei423 – 4231PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UPR3.
MaxQBiQ9UPR3.
PaxDbiQ9UPR3.
PRIDEiQ9UPR3.

PTM databases

iPTMnetiQ9UPR3.
PhosphoSiteiQ9UPR3.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

BgeeiQ9UPR3.
CleanExiHS_SMG5.
GenevisibleiQ9UPR3. HS.

Interactioni

Subunit structurei

Interacts with TERT, PPP2CA and SMG1. Part of a complex that contains SMG1, SMG5, SMG7, PPP2CA, a short isoform of UPF3A (isoform UPF3AS, but not isoform UPF3AL) and phosphorylated UPF1. Not detected in complexes that contain unphosphorylated UPF1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMG7Q925405EBI-3400861,EBI-719830
UPF1Q92900-22EBI-3400861,EBI-373492

GO - Molecular functioni

  • DNA polymerase binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • protein phosphatase 2A binding Source: HGNC
  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116957. 16 interactions.
IntActiQ9UPR3. 8 interactions.
MINTiMINT-6783753.
STRINGi9606.ENSP00000355261.

Structurei

Secondary structure

1
1016
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi856 – 8594Combined sources
Helixi861 – 8666Combined sources
Helixi868 – 87710Combined sources
Beta strandi878 – 8847Combined sources
Helixi886 – 89510Combined sources
Helixi900 – 91516Combined sources
Beta strandi918 – 9225Combined sources
Helixi946 – 95510Combined sources
Beta strandi977 – 9804Combined sources
Helixi992 – 9965Combined sources
Beta strandi1000 – 10023Combined sources
Helixi1005 – 10117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HWYX-ray2.75A/B853-1016[»]
ProteinModelPortaliQ9UPR3.
SMRiQ9UPR3. Positions 56-408, 855-1012.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UPR3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini872 – 995124PINcAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili798 – 84144Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi460 – 4634Poly-Arg
Compositional biasi529 – 5324Poly-Glu

Sequence similaritiesi

Contains 1 PINc domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410INQY. Eukaryota.
ENOG410XPF4. LUCA.
GeneTreeiENSGT00560000077120.
HOVERGENiHBG082268.
InParanoidiQ9UPR3.
KOiK11125.
OMAiIIPFELS.
OrthoDBiEOG7GTT35.
PhylomeDBiQ9UPR3.
TreeFamiTF327119.

Family and domain databases

InterProiIPR018834. DNA/RNA-bd_Est1-type.
IPR019458. EST1.
IPR002716. PIN_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF10374. EST1. 1 hit.
PF10373. EST1_DNA_bind. 2 hits.
PF13638. PIN_4. 1 hit.
[Graphical view]
SMARTiSM00670. PINc. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q9UPR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQGPPTGES SEPEAKVLHT KRLYRAVVEA VHRLDLILCN KTAYQEVFKP
60 70 80 90 100
ENISLRNKLR ELCVKLMFLH PVDYGRKAEE LLWRKVYYEV IQLIKTNKKH
110 120 130 140 150
IHSRSTLECA YRTHLVAGIG FYQHLLLYIQ SHYQLELQCC IDWTHVTDPL
160 170 180 190 200
IGCKKPVSAS GKEMDWAQMA CHRCLVYLGD LSRYQNELAG VDTELLAERF
210 220 230 240 250
YYQALSVAPQ IGMPFNQLGT LAGSKYYNVE AMYCYLRCIQ SEVSFEGAYG
260 270 280 290 300
NLKRLYDKAA KMYHQLKKCE TRKLSPGKKR CKDIKRLLVN FMYLQSLLQP
310 320 330 340 350
KSSSVDSELT SLCQSVLEDF NLCLFYLPSS PNLSLASEDE EEYESGYAFL
360 370 380 390 400
PDLLIFQMVI ICLMCVHSLE RAGSKQYSAA IAFTLALFSH LVNHVNIRLQ
410 420 430 440 450
AELEEGENPV PAFQSDGTDE PESKEPVEKE EEPDPEPPPV TPQVGEGRKS
460 470 480 490 500
RKFSRLSCLR RRRHPPKVGD DSDLSEGFES DSSHDSARAS EGSDSGSDKS
510 520 530 540 550
LEGGGTAFDA ETDSEMNSQE SRSDLEDMEE EEGTRSPTLE PPRGRSEAPD
560 570 580 590 600
SLNGPLGPSE ASIASNLQAM STQMFQTKRC FRLAPTFSNL LLQPTTNPHT
610 620 630 640 650
SASHRPCVNG DVDKPSEPAS EEGSESEGSE SSGRSCRNER SIQEKLQVLM
660 670 680 690 700
AEGLLPAVKV FLDWLRTNPD LIIVCAQSSQ SLWNRLSVLL NLLPAAGELQ
710 720 730 740 750
ESGLALCPEV QDLLEGCELP DLPSSLLLPE DMALRNLPPL RAAHRRFNFD
760 770 780 790 800
TDRPLLSTLE ESVVRICCIR SFGHFIARLQ GSILQFNPEV GIFVSIAQSE
810 820 830 840 850
QESLLQQAQA QFRMAQEEAR RNRLMRDMAQ LRLQLEVSQL EGSLQQPKAQ
860 870 880 890 900
SAMSPYLVPD TQALCHHLPV IRQLATSGRF IVIIPRTVID GLDLLKKEHP
910 920 930 940 950
GARDGIRYLE AEFKKGNRYI RCQKEVGKSF ERHKLKRQDA DAWTLYKILD
960 970 980 990 1000
SCKQLTLAQG AGEEDPSGMV TIITGLPLDN PSVLSGPMQA ALQAAAHASV
1010
DIKNVLDFYK QWKEIG
Length:1,016
Mass (Da):113,928
Last modified:December 20, 2005 - v3
Checksum:iB6F8F9B53CF42195
GO

Sequence cautioni

The sequence BAA83041.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti372 – 3721A → S in AAQ84301 (Ref. 3) Curated
Sequence conflicti384 – 3841T → A in AAQ84301 (Ref. 3) Curated
Sequence conflicti496 – 4961G → R in AAQ84301 (Ref. 3) Curated
Sequence conflicti915 – 9151K → KK in CAH56374 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1004 – 10041N → D.1 Publication
Corresponds to variant rs17853821 [ dbSNP | Ensembl ].
VAR_030828

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB085691 mRNA. Translation: BAC53623.1.
AY168922 mRNA. Translation: AAO17582.1.
AY336728 mRNA. Translation: AAQ84301.1.
AB029012 mRNA. Translation: BAA83041.2. Different initiation.
AL589685, AL135927 Genomic DNA. Translation: CAI14160.1.
AL135927, AL589685 Genomic DNA. Translation: CAI15525.1.
CH471121 Genomic DNA. Translation: EAW52973.1.
CH471121 Genomic DNA. Translation: EAW52974.1.
BC007453 mRNA. Translation: AAH07453.2.
BC038296 mRNA. Translation: AAH38296.1.
AL137738 mRNA. Translation: CAH56374.1.
CCDSiCCDS1137.1.
RefSeqiNP_056142.2. NM_015327.2.
UniGeneiHs.516837.

Genome annotation databases

EnsembliENST00000361813; ENSP00000355261; ENSG00000198952.
GeneIDi23381.
KEGGihsa:23381.
UCSCiuc001foc.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB085691 mRNA. Translation: BAC53623.1.
AY168922 mRNA. Translation: AAO17582.1.
AY336728 mRNA. Translation: AAQ84301.1.
AB029012 mRNA. Translation: BAA83041.2. Different initiation.
AL589685, AL135927 Genomic DNA. Translation: CAI14160.1.
AL135927, AL589685 Genomic DNA. Translation: CAI15525.1.
CH471121 Genomic DNA. Translation: EAW52973.1.
CH471121 Genomic DNA. Translation: EAW52974.1.
BC007453 mRNA. Translation: AAH07453.2.
BC038296 mRNA. Translation: AAH38296.1.
AL137738 mRNA. Translation: CAH56374.1.
CCDSiCCDS1137.1.
RefSeqiNP_056142.2. NM_015327.2.
UniGeneiHs.516837.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HWYX-ray2.75A/B853-1016[»]
ProteinModelPortaliQ9UPR3.
SMRiQ9UPR3. Positions 56-408, 855-1012.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116957. 16 interactions.
IntActiQ9UPR3. 8 interactions.
MINTiMINT-6783753.
STRINGi9606.ENSP00000355261.

PTM databases

iPTMnetiQ9UPR3.
PhosphoSiteiQ9UPR3.

Polymorphism and mutation databases

BioMutaiSMG5.
DMDMi84029494.

Proteomic databases

EPDiQ9UPR3.
MaxQBiQ9UPR3.
PaxDbiQ9UPR3.
PRIDEiQ9UPR3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361813; ENSP00000355261; ENSG00000198952.
GeneIDi23381.
KEGGihsa:23381.
UCSCiuc001foc.5. human.

Organism-specific databases

CTDi23381.
GeneCardsiSMG5.
HGNCiHGNC:24644. SMG5.
MIMi610962. gene.
neXtProtiNX_Q9UPR3.
PharmGKBiPA143485617.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INQY. Eukaryota.
ENOG410XPF4. LUCA.
GeneTreeiENSGT00560000077120.
HOVERGENiHBG082268.
InParanoidiQ9UPR3.
KOiK11125.
OMAiIIPFELS.
OrthoDBiEOG7GTT35.
PhylomeDBiQ9UPR3.
TreeFamiTF327119.

Enzyme and pathway databases

ReactomeiR-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiSMG5. human.
EvolutionaryTraceiQ9UPR3.
GeneWikiiSMG5.
GenomeRNAii23381.
NextBioi45485.
PROiQ9UPR3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UPR3.
CleanExiHS_SMG5.
GenevisibleiQ9UPR3. HS.

Family and domain databases

InterProiIPR018834. DNA/RNA-bd_Est1-type.
IPR019458. EST1.
IPR002716. PIN_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF10374. EST1. 1 hit.
PF10373. EST1_DNA_bind. 2 hits.
PF13638. PIN_4. 1 hit.
[Graphical view]
SMARTiSM00670. PINc. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7."
    Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A., Hachiya T., Hentze M.W., Anderson P., Ohno S.
    Mol. Cell 12:1187-1200(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASP-860, INTERACTION WITH PPP2CA; SMG7 AND SMG1, IDENTIFICATION IN COMPLEXES WITH SMG7; PPP2CA AND PHOSPHORYLATED RENT1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "Functional conservation of the telomerase protein Est1p in humans."
    Snow B.E., Erdmann N., Cruickshank J., Goldman H., Gill R.M., Robinson M.O., Harrington L.
    Curr. Biol. 13:698-704(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TERT, TISSUE SPECIFICITY.
  3. "LPTS-RP1, a LPTS interacting protein."
    Song H., Zhao M., Li T.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 ASP-1004.
    Tissue: Muscle and Testis.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 584-1016.
    Tissue: Brain.
  10. "SMG7 acts as a molecular link between mRNA surveillance and mRNA decay."
    Unterholzner L., Izaurralde E.
    Mol. Cell 16:587-596(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH CYTOPLASMIC MRNA DECAY BODIES.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex."
    Glavan F., Behm-Ansmant I., Izaurralde E., Conti E.
    EMBO J. 25:5117-5125(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 853-1016, FUNCTION.

Entry informationi

Entry nameiSMG5_HUMAN
AccessioniPrimary (citable) accession number: Q9UPR3
Secondary accession number(s): D3DVB7
, Q5QJE7, Q659C7, Q8IXC0, Q8IY09, Q96IJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 11, 2016
This is version 129 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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 one 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.