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Protein

GPI mannosyltransferase 2

Gene

PIGV

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

Functioni

Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.2 Publications

Pathway:iglycosylphosphatidylinositol-anchor biosynthesis

This protein is involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis, which is part of Glycolipid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis and in Glycolipid biosynthesis.

GO - Molecular functioni

  • mannosyltransferase activity Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • C-terminal protein lipidation Source: Reactome
  • GPI anchor biosynthetic process Source: UniProtKB
  • mannosylation Source: GOC
  • post-translational protein modification Source: Reactome
  • preassembly of GPI anchor in ER membrane Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Protein family/group databases

CAZyiGT76. Glycosyltransferase Family 76.

Names & Taxonomyi

Protein namesi
Recommended name:
GPI mannosyltransferase 2 (EC:2.4.1.-)
Alternative name(s):
GPI mannosyltransferase II
Short name:
GPI-MT-II
Phosphatidylinositol-glycan biosynthesis class V protein
Short name:
PIG-V
Gene namesi
Name:PIGV
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:26031. PIGV.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei14 – 3421HelicalSequence AnalysisAdd
BLAST
Topological domaini35 – 7743LumenalSequence AnalysisAdd
BLAST
Transmembranei78 – 9821HelicalSequence AnalysisAdd
BLAST
Topological domaini99 – 11315CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei114 – 13421HelicalSequence AnalysisAdd
BLAST
Topological domaini135 – 1362LumenalSequence Analysis
Transmembranei137 – 15721HelicalSequence AnalysisAdd
BLAST
Topological domaini158 – 1614CytoplasmicSequence Analysis
Transmembranei162 – 18221HelicalSequence AnalysisAdd
BLAST
Topological domaini183 – 19210LumenalSequence Analysis
Transmembranei193 – 21321HelicalSequence AnalysisAdd
BLAST
Topological domaini214 – 23421CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei235 – 25521HelicalSequence AnalysisAdd
BLAST
Topological domaini256 – 32772LumenalSequence AnalysisAdd
BLAST
Transmembranei328 – 34821HelicalSequence AnalysisAdd
BLAST
Topological domaini349 – 37830CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei379 – 39921HelicalSequence AnalysisAdd
BLAST
Topological domaini400 – 46970LumenalSequence AnalysisAdd
BLAST
Transmembranei470 – 49021HelicalSequence AnalysisAdd
BLAST
Topological domaini491 – 4933CytoplasmicSequence Analysis

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Hyperphosphatasia with mental retardation syndrome 1 (HPMRS1)1 Publication

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

Disease descriptionA severe syndrome characterized by elevated serum alkaline phosphatase, severe mental retardation, seizures, hypotonia, facial dysmorphism, and hypoplastic terminal phalanges.

See also OMIM:239300
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561Q → K in HPMRS1. 1 Publication
VAR_064190
Natural varianti341 – 3411A → E in HPMRS1. 1 Publication
VAR_064191
Natural varianti341 – 3411A → V in HPMRS1. 1 Publication
VAR_064192
Natural varianti385 – 3851H → P in HPMRS1. 1 Publication
VAR_064193

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661W → L: Loss of function. 1 Publication
Mutagenesisi67 – 671D → A: Loss of function. 1 Publication
Mutagenesisi293 – 2942PP → TA: N-glycosylated due to the creation of an acceptor site for N-glycosylation. 1 Publication
Mutagenesisi308 – 3081Q → A: Induces a reduces enzyme activity. 1 Publication
Mutagenesisi312 – 3121W → L: Loss of function. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi239300. phenotype.
Orphaneti247262. Hyperphosphatasia-intellectual disability syndrome.
PharmGKBiPA134952230.

Polymorphism and mutation databases

BioMutaiPIGV.
DMDMi74752975.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493GPI mannosyltransferase 2PRO_0000246234Add
BLAST

Post-translational modificationi

Not N-glycosylated.1 Publication

Proteomic databases

MaxQBiQ9NUD9.
PaxDbiQ9NUD9.
PRIDEiQ9NUD9.

PTM databases

PhosphoSiteiQ9NUD9.

Expressioni

Gene expression databases

BgeeiQ9NUD9.
CleanExiHS_PIGV.
ExpressionAtlasiQ9NUD9. baseline and differential.
GenevisibleiQ9NUD9. HS.

Interactioni

Protein-protein interaction databases

BioGridi120782. 1 interaction.
STRINGi9606.ENSP00000078527.

Structurei

3D structure databases

ProteinModelPortaliQ9NUD9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGV family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5542.
GeneTreeiENSGT00390000013174.
HOGENOMiHOG000232162.
HOVERGENiHBG080592.
InParanoidiQ9NUD9.
KOiK07542.
OMAiVGFLKYY.
OrthoDBiEOG7VDXPB.
PhylomeDBiQ9NUD9.
TreeFamiTF314515.

Family and domain databases

InterProiIPR007315. GPI_Mannosyltransferase_2.
[Graphical view]
PANTHERiPTHR12468. PTHR12468. 1 hit.
PfamiPF04188. Mannosyl_trans2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NUD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWPQDPSRKE VLRFAVSCRI LTLMLQALFN AIIPDHHAEA FSPPRLAPSG
60 70 80 90 100
FVDQLVEGLL GGLSHWDAEH FLFIAEHGYL YEHNFAFFPG FPLALLVGTE
110 120 130 140 150
LLRPLRGLLS LRSCLLISVA SLNFLFFMLA AVALHDLGCL VLHCPHQSFY
160 170 180 190 200
AALLFCLSPA NVFLAAGYSE ALFALLTFSA MGQLERGRVW TSVLLFAFAT
210 220 230 240 250
GVRSNGLVSV GFLMHSQCQG FFSSLTMLNP LRQLFKLMAS LFLSVFTLGL
260 270 280 290 300
PFALFQYYAY TQFCLPGSAR PIPEPLVQLA VDKGYRIAEG NEPPWCFWDV
310 320 330 340 350
PLIYSYIQDV YWNVGFLKYY ELKQVPNFLL AAPVAILVAW ATWTYVTTHP
360 370 380 390 400
WLCLTLGLQR SKNNKTLEKP DLGFLSPQVF VYVVHAAVLL LFGGLCMHVQ
410 420 430 440 450
VLTRFLGSST PIMYWFPAHL LQDQEPLLRS LKTVPWKPLA EDSPPGQKVP
460 470 480 490
RNPIMGLLYH WKTCSPVTRY ILGYFLTYWL LGLLLHCNFL PWT
Length:493
Mass (Da):55,713
Last modified:October 1, 2000 - v1
Checksum:i087AE31E51BDD519
GO

Sequence cautioni

The sequence CAI21625.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI21626.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI21627.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331I → T in BAA91196 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561Q → K in HPMRS1. 1 Publication
VAR_064190
Natural varianti341 – 3411A → E in HPMRS1. 1 Publication
VAR_064191
Natural varianti341 – 3411A → V in HPMRS1. 1 Publication
VAR_064192
Natural varianti385 – 3851H → P in HPMRS1. 1 Publication
VAR_064193

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000484 mRNA. Translation: BAA91196.1.
AL034380 Genomic DNA. Translation: CAB92120.1.
AL034380 Genomic DNA. Translation: CAI21625.1. Sequence problems.
AL034380 Genomic DNA. Translation: CAI21626.1. Sequence problems.
AL034380 Genomic DNA. Translation: CAI21627.1. Sequence problems.
CH471059 Genomic DNA. Translation: EAX07790.1.
CH471059 Genomic DNA. Translation: EAX07791.1.
CH471059 Genomic DNA. Translation: EAX07792.1.
BC013568 mRNA. Translation: AAH13568.1.
CCDSiCCDS287.1.
RefSeqiNP_001189483.1. NM_001202554.1.
NP_060307.2. NM_017837.3.
UniGeneiHs.259605.
Hs.732254.

Genome annotation databases

EnsembliENST00000078527; ENSP00000078527; ENSG00000060642.
ENST00000374145; ENSP00000363260; ENSG00000060642.
GeneIDi55650.
KEGGihsa:55650.
UCSCiuc001bmz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000484 mRNA. Translation: BAA91196.1.
AL034380 Genomic DNA. Translation: CAB92120.1.
AL034380 Genomic DNA. Translation: CAI21625.1. Sequence problems.
AL034380 Genomic DNA. Translation: CAI21626.1. Sequence problems.
AL034380 Genomic DNA. Translation: CAI21627.1. Sequence problems.
CH471059 Genomic DNA. Translation: EAX07790.1.
CH471059 Genomic DNA. Translation: EAX07791.1.
CH471059 Genomic DNA. Translation: EAX07792.1.
BC013568 mRNA. Translation: AAH13568.1.
CCDSiCCDS287.1.
RefSeqiNP_001189483.1. NM_001202554.1.
NP_060307.2. NM_017837.3.
UniGeneiHs.259605.
Hs.732254.

3D structure databases

ProteinModelPortaliQ9NUD9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120782. 1 interaction.
STRINGi9606.ENSP00000078527.

Protein family/group databases

CAZyiGT76. Glycosyltransferase Family 76.

PTM databases

PhosphoSiteiQ9NUD9.

Polymorphism and mutation databases

BioMutaiPIGV.
DMDMi74752975.

Proteomic databases

MaxQBiQ9NUD9.
PaxDbiQ9NUD9.
PRIDEiQ9NUD9.

Protocols and materials databases

DNASUi55650.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000078527; ENSP00000078527; ENSG00000060642.
ENST00000374145; ENSP00000363260; ENSG00000060642.
GeneIDi55650.
KEGGihsa:55650.
UCSCiuc001bmz.3. human.

Organism-specific databases

CTDi55650.
GeneCardsiGC01P027113.
H-InvDBHIX0159960.
HGNCiHGNC:26031. PIGV.
MIMi239300. phenotype.
610274. gene.
neXtProtiNX_Q9NUD9.
Orphaneti247262. Hyperphosphatasia-intellectual disability syndrome.
PharmGKBiPA134952230.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5542.
GeneTreeiENSGT00390000013174.
HOGENOMiHOG000232162.
HOVERGENiHBG080592.
InParanoidiQ9NUD9.
KOiK07542.
OMAiVGFLKYY.
OrthoDBiEOG7VDXPB.
PhylomeDBiQ9NUD9.
TreeFamiTF314515.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

GeneWikiiPIGV.
GenomeRNAii55650.
NextBioi60346.
PROiQ9NUD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUD9.
CleanExiHS_PIGV.
ExpressionAtlasiQ9NUD9. baseline and differential.
GenevisibleiQ9NUD9. HS.

Family and domain databases

InterProiIPR007315. GPI_Mannosyltransferase_2.
[Graphical view]
PANTHERiPTHR12468. PTHR12468. 1 hit.
PfamiPF04188. Mannosyl_trans2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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].
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Lung.
  5. "Familial hyperphosphatase with mental retardation, seizures, and neurologic deficits."
    Mabry C.C., Bautista A., Kirk R.F., Dubilier L.D., Braunstein H., Koepke J.A.
    J. Pediatr. 77:74-85(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: DESCRIPTION OF HYPERPHOSPHATASIA WITH MENTAL RETARDATION SYNDROME.
  6. "Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly."
    Fabre A.-L., Orlean P., Taron C.H.
    FEBS J. 272:1160-1168(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol."
    Kang J.Y., Hong Y., Ashida H., Shishioh N., Murakami Y., Morita Y.S., Maeda Y., Kinoshita T.
    J. Biol. Chem. 280:9489-9497(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, LACK OF GLYCOSYLATION, MUTAGENESIS OF TRP-66; ASP-67; 293-PRO-PRO-294; GLN-308 AND TRP-312.
  8. "Hyperphosphatasia with seizures, neurologic deficit, and characteristic facial features: Five new patients with Mabry syndrome."
    Thompson M.D., Nezarati M.M., Gillessen-Kaesbach G., Meinecke P., Mendoza R., Mornet E., Brun-Heath I., Squarcioni C.P., Legeai-Mallet L., Munnich A., Cole D.E.
    Am. J. Med. Genet. A 152:1661-1669(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DESCRIPTION OF HYPERPHOSPHATASIA WITH MENTAL RETARDATION SYNDROME.
  9. Cited for: VARIANTS HPMRS1 LYS-256; VAL-341; GLU-341 AND PRO-385.

Entry informationi

Entry nameiPIGV_HUMAN
AccessioniPrimary (citable) accession number: Q9NUD9
Secondary accession number(s): D3DPL2
, Q5JYG7, Q5JYG8, Q5JYG9, Q9NX26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 107 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 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.