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Protein

Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C

Gene

MGAT4C

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

Functioni

Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Does not catalyze the transfer of GlcNAc to the Manalpha1-6 arm to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI' activity).By similarity1 Publication

Catalytic activityi

UDP-N-acetyl-D-glucosamine + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2,4-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.

Cofactori

Pathwayi

GO - Molecular functioni

  1. alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. post-translational protein modification Source: Reactome
  3. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00017-MONOMER.
ReactomeiREACT_25085. N-Glycan antennae elongation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT54. Glycosyltransferase Family 54.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C (EC:2.4.1.145)
Alternative name(s):
N-acetylglucosaminyltransferase IV homolog
Short name:
hGnT-IV-H
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVc
Short name:
GlcNAc-T IVc
Short name:
GnT-IVc
Short name:
N-acetylglucosaminyltransferase IVc
UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVc
Gene namesi
Name:MGAT4C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30871. MGAT4C.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2323CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei24 – 4421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini45 – 478434LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485535.

Polymorphism and mutation databases

BioMutaiMGAT4C.
DMDMi296437368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase CPRO_0000288596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9UBM8.
PRIDEiQ9UBM8.

PTM databases

PhosphoSiteiQ9UBM8.

Expressioni

Tissue specificityi

Expressed in heart, adrenal gland, testis, liver, brain and fetal brain. Not expressed in pancreas.1 Publication

Gene expression databases

BgeeiQ9UBM8.
CleanExiHS_MGAT4C.
ExpressionAtlasiQ9UBM8. baseline and differential.
GenevestigatoriQ9UBM8.

Organism-specific databases

HPAiHPA016418.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000331664.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 54 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG69242.
GeneTreeiENSGT00550000074578.
HOGENOMiHOG000070065.
HOVERGENiHBG103174.
InParanoidiQ9UBM8.
KOiK13748.
OMAiVMVQDIT.
OrthoDBiEOG7F24TD.
PhylomeDBiQ9UBM8.
TreeFamiTF324570.

Family and domain databases

InterProiIPR006759. Glyco_transf_54.
[Graphical view]
PANTHERiPTHR12062. PTHR12062. 1 hit.
PfamiPF04666. Glyco_transf_54. 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: Q9UBM8-1) [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
MFKFHQMKHI FEILDKMRCL RKRSTVSFLG VLVIFLLFMN LYIEDSYVLE
60 70 80 90 100
GDKQLIRETS THQLNSERYV HTFKDLSNFS GAINVTYRYL AATPLQRKRY
110 120 130 140 150
LTIGLSSVKR KKGNYLLETI KSIFEQSSYE ELKEISVVVH LADFNSSWRD
160 170 180 190 200
AMVQDITQKF AHHIIAGRLM VIHAPEEYYP ILDGLKRNYN DPEDRVKFRS
210 220 230 240 250
KQNVDYAFLL NFCANTSDYY VMLEDDVRCS KNFLTAIKKV IASLEGTYWV
260 270 280 290 300
TLEFSKLGYI GKLYHSHDLP RLAHFLLMFY QEMPCDWLLT HFRGLLAQKN
310 320 330 340 350
VIRFKPSLFQ HMGYYSSYKG TENKLKDDDF EEESFDIPDN PPASLYTNMN
360 370 380 390 400
VFENYEASKA YSSVDEYFWG KPPSTGDVFV IVFENPIIIK KIKVNTGTED
410 420 430 440 450
RQNDILHHGA LDVGENVMPS KQRRQCSTYL RLGEFKNGNF EMSGVNQKIP
460 470
FDIHCMRIYV TKTQKEWLII RSISIWTS
Length:478
Mass (Da):56,061
Last modified:May 18, 2010 - v2
Checksum:i7D09A1BB6B6800C6
GO
Isoform 2 (identifier: Q9UBM8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLGKDMVRFVVRKTVQRSVAKGSRRCKKRM

Note: No experimental confirmation available.

Show »
Length:507
Mass (Da):59,465
Checksum:iA73FDA660E5A71C3
GO

Sequence cautioni

The sequence AAH26068.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti428 – 4281T → S.2 Publications
Corresponds to variant rs17855890 [ dbSNP | Ensembl ].
VAR_032447

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLGKDMVRFVVRKTVQRSVA KGSRRCKKRM in isoform 2. 1 PublicationVSP_056096

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024729 mRNA. Translation: BAA83074.1.
AB024730 mRNA. Translation: BAA83075.1.
AB024911 Genomic DNA. Translation: BAA83087.1.
AK299253 mRNA. Translation: BAG61284.1.
AC010196 Genomic DNA. No translation available.
AC016993 Genomic DNA. No translation available.
AC025157 Genomic DNA. No translation available.
AC079596 Genomic DNA. No translation available.
AC079865 Genomic DNA. No translation available.
AC087887 Genomic DNA. No translation available.
AC093122 Genomic DNA. No translation available.
AC128681 Genomic DNA. No translation available.
AC139663 Genomic DNA. No translation available.
AC139697 Genomic DNA. No translation available.
BC026068 mRNA. Translation: AAH26068.1. Sequence problems.
BC064141 mRNA. Translation: AAH64141.1.
CCDSiCCDS9030.1. [Q9UBM8-1]
RefSeqiNP_037376.2. NM_013244.3. [Q9UBM8-1]
XP_005268833.1. XM_005268776.3. [Q9UBM8-2]
XP_005268836.1. XM_005268779.2. [Q9UBM8-1]
UniGeneiHs.589093.

Genome annotation databases

EnsembliENST00000548651; ENSP00000447253; ENSG00000182050. [Q9UBM8-1]
ENST00000552808; ENSP00000446647; ENSG00000182050. [Q9UBM8-1]
ENST00000611864; ENSP00000481096; ENSG00000182050. [Q9UBM8-1]
ENST00000620241; ENSP00000477650; ENSG00000182050. [Q9UBM8-1]
ENST00000621808; ENSP00000478300; ENSG00000182050. [Q9UBM8-1]
GeneIDi25834.
KEGGihsa:25834.
UCSCiuc001tah.4. human. [Q9UBM8-1]

Polymorphism and mutation databases

BioMutaiMGAT4C.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024729 mRNA. Translation: BAA83074.1.
AB024730 mRNA. Translation: BAA83075.1.
AB024911 Genomic DNA. Translation: BAA83087.1.
AK299253 mRNA. Translation: BAG61284.1.
AC010196 Genomic DNA. No translation available.
AC016993 Genomic DNA. No translation available.
AC025157 Genomic DNA. No translation available.
AC079596 Genomic DNA. No translation available.
AC079865 Genomic DNA. No translation available.
AC087887 Genomic DNA. No translation available.
AC093122 Genomic DNA. No translation available.
AC128681 Genomic DNA. No translation available.
AC139663 Genomic DNA. No translation available.
AC139697 Genomic DNA. No translation available.
BC026068 mRNA. Translation: AAH26068.1. Sequence problems.
BC064141 mRNA. Translation: AAH64141.1.
CCDSiCCDS9030.1. [Q9UBM8-1]
RefSeqiNP_037376.2. NM_013244.3. [Q9UBM8-1]
XP_005268833.1. XM_005268776.3. [Q9UBM8-2]
XP_005268836.1. XM_005268779.2. [Q9UBM8-1]
UniGeneiHs.589093.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000331664.

Protein family/group databases

CAZyiGT54. Glycosyltransferase Family 54.

PTM databases

PhosphoSiteiQ9UBM8.

Polymorphism and mutation databases

BioMutaiMGAT4C.
DMDMi296437368.

Proteomic databases

PaxDbiQ9UBM8.
PRIDEiQ9UBM8.

Protocols and materials databases

DNASUi25834.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000548651; ENSP00000447253; ENSG00000182050. [Q9UBM8-1]
ENST00000552808; ENSP00000446647; ENSG00000182050. [Q9UBM8-1]
ENST00000611864; ENSP00000481096; ENSG00000182050. [Q9UBM8-1]
ENST00000620241; ENSP00000477650; ENSG00000182050. [Q9UBM8-1]
ENST00000621808; ENSP00000478300; ENSG00000182050. [Q9UBM8-1]
GeneIDi25834.
KEGGihsa:25834.
UCSCiuc001tah.4. human. [Q9UBM8-1]

Organism-specific databases

CTDi25834.
GeneCardsiGC12M086372.
H-InvDBHIX0026328.
HGNCiHGNC:30871. MGAT4C.
HPAiHPA016418.
MIMi607385. gene.
neXtProtiNX_Q9UBM8.
PharmGKBiPA143485535.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG69242.
GeneTreeiENSGT00550000074578.
HOGENOMiHOG000070065.
HOVERGENiHBG103174.
InParanoidiQ9UBM8.
KOiK13748.
OMAiVMVQDIT.
OrthoDBiEOG7F24TD.
PhylomeDBiQ9UBM8.
TreeFamiTF324570.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS00017-MONOMER.
ReactomeiREACT_25085. N-Glycan antennae elongation.

Miscellaneous databases

ChiTaRSiMGAT4C. human.
GenomeRNAii25834.
NextBioi35474390.
PROiQ9UBM8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBM8.
CleanExiHS_MGAT4C.
ExpressionAtlasiQ9UBM8. baseline and differential.
GenevestigatoriQ9UBM8.

Family and domain databases

InterProiIPR006759. Glyco_transf_54.
[Graphical view]
PANTHERiPTHR12062. PTHR12062. 1 hit.
PfamiPF04666. Glyco_transf_54. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the human UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IV-homologue (hGnT-IV-H) gene."
    Furukawa T., Youssef E.M., Yatsuoka T., Yokoyama T., Makino N., Inoue H., Fukushige S., Hoshi M., Hayashi Y., Sunamura M., Horii A.
    J. Hum. Genet. 44:397-401(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-428.
  2. "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).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1), VARIANT SER-428.
    Tissue: Testis.
  5. "Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcbeta 1-6(GlcNAcbeta 1-2)-manalpha 1-R[GlcNAc to man]beta 1,4N-acetylglucosaminyltransferase VI."
    Sakamoto Y., Taguchi T., Honke K., Korekane H., Watanabe H., Tano Y., Dohmae N., Takio K., Horii A., Taniguchi N.
    J. Biol. Chem. 275:36029-36034(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMGT4C_HUMAN
AccessioniPrimary (citable) accession number: Q9UBM8
Secondary accession number(s): B4DRH2, Q4G199, Q9UIU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 18, 2010
Last modified: April 29, 2015
This is version 109 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. Human chromosome 12
    Human chromosome 12: 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.