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Protein

Solute carrier family 2, facilitated glucose transporter member 3

Gene

SLC2A3

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

Functioni

Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane (PubMed:9477959, PubMed:26176916). Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate (PubMed:9477959, PubMed:26176916). Does not mediate fructose transport (PubMed:9477959, PubMed:26176916).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei315 – 3151Monosaccharide1 Publication
Binding sitei378 – 3781Monosaccharide1 Publication
Binding sitei386 – 3861Monosaccharide1 Publication

GO - Molecular functioni

GO - Biological processi

  • carbohydrate metabolic process Source: ProtInc
  • dehydroascorbic acid transport Source: GOC
  • glucose transmembrane transport Source: UniProtKB
  • glucose transport Source: Reactome
  • L-ascorbic acid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-196836. Vitamin C (ascorbate) metabolism.
R-HSA-428790. Facilitative Na+-independent glucose transporters.
R-HSA-70153. Glucose transport.

Protein family/group databases

TCDBi2.A.1.1.91. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 2, facilitated glucose transporter member 3
Alternative name(s):
Glucose transporter type 3, brain
Short name:
GLUT-3
Gene namesi
Name:SLC2A3
Synonyms:GLUT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:11007. SLC2A3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicCurated
Transmembranei11 – 3222Helical; Name=1Sequence analysis1 PublicationAdd
BLAST
Topological domaini33 – 6432ExtracellularCuratedAdd
BLAST
Transmembranei65 – 8521Helical; Name=2Sequence analysis1 PublicationAdd
BLAST
Topological domaini86 – 905CytoplasmicCurated
Transmembranei91 – 11121Helical; Name=3Sequence analysis1 PublicationAdd
BLAST
Topological domaini112 – 1187ExtracellularCurated
Transmembranei119 – 14224Helical; Name=4Sequence analysis1 PublicationAdd
BLAST
Topological domaini143 – 15311CytoplasmicCuratedAdd
BLAST
Transmembranei154 – 17421Helical; Name=5Sequence analysis1 PublicationAdd
BLAST
Topological domaini175 – 1839ExtracellularCurated
Transmembranei184 – 20421Helical; Name=6Sequence analysis1 PublicationAdd
BLAST
Topological domaini205 – 26965CytoplasmicCuratedAdd
BLAST
Transmembranei270 – 29021Helical; Name=7Sequence analysis1 PublicationAdd
BLAST
Topological domaini291 – 30414ExtracellularCuratedAdd
BLAST
Transmembranei305 – 32521Helical; Name=8Sequence analysis1 PublicationAdd
BLAST
Topological domaini326 – 3316CytoplasmicCurated
Transmembranei332 – 35221Helical; Name=9Sequence analysis1 PublicationAdd
BLAST
Topological domaini353 – 36311ExtracellularCuratedAdd
BLAST
Transmembranei364 – 38926Helical; Name=10Sequence analysis1 PublicationAdd
BLAST
Topological domaini390 – 39910CytoplasmicCurated
Transmembranei400 – 42021Helical; Name=11Sequence analysis1 PublicationAdd
BLAST
Topological domaini421 – 4299ExtracellularCurated
Transmembranei430 – 45021Helical; Name=12Sequence analysis1 PublicationAdd
BLAST
Topological domaini451 – 49646CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi277 – 2793QLS → HVA: Confers moderate fructose trasnport activity. 1 Publication

Organism-specific databases

MalaCardsiSLC2A3.
Orphaneti399. Huntington disease.
PharmGKBiPA35877.

Chemistry

ChEMBLiCHEMBL5215.

Polymorphism and mutation databases

BioMutaiSLC2A3.
DMDMi121760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Solute carrier family 2, facilitated glucose transporter member 3PRO_0000050353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence analysis
Modified residuei232 – 2321PhosphothreonineBy similarity
Modified residuei475 – 4751PhosphoserineBy similarity
Modified residuei485 – 4851PhosphoserineBy similarity
Modified residuei492 – 4921PhosphothreonineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP11169.
MaxQBiP11169.
PaxDbiP11169.
PRIDEiP11169.

PTM databases

iPTMnetiP11169.
PhosphoSiteiP11169.

Expressioni

Tissue specificityi

Highly expressed in brain. Expressed in many tissues.1 Publication

Gene expression databases

BgeeiP11169.
CleanExiHS_SLC2A3.
ExpressionAtlasiP11169. baseline and differential.
GenevisibleiP11169. HS.

Organism-specific databases

HPAiCAB002763.
HPA006539.

Interactioni

Protein-protein interaction databases

BioGridi112406. 4 interactions.
IntActiP11169. 6 interactions.
MINTiMINT-4999361.
STRINGi9606.ENSP00000075120.

Structurei

Secondary structure

1
496
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2922Combined sources
Beta strandi30 – 323Combined sources
Helixi35 – 4814Combined sources
Beta strandi50 – 523Combined sources
Helixi56 – 7924Combined sources
Helixi81 – 888Combined sources
Helixi90 – 967Combined sources
Helixi98 – 11013Combined sources
Turni111 – 1155Combined sources
Helixi117 – 14529Combined sources
Helixi148 – 1503Combined sources
Helixi151 – 17323Combined sources
Turni175 – 1784Combined sources
Turni181 – 1833Combined sources
Helixi184 – 1896Combined sources
Helixi192 – 20110Combined sources
Helixi202 – 2043Combined sources
Helixi209 – 2146Combined sources
Helixi219 – 23012Combined sources
Helixi236 – 25116Combined sources
Helixi259 – 2624Combined sources
Helixi264 – 28118Combined sources
Turni282 – 2843Combined sources
Helixi285 – 29915Combined sources
Helixi304 – 35552Combined sources
Turni356 – 3583Combined sources
Helixi362 – 37918Combined sources
Turni380 – 3823Combined sources
Helixi383 – 3919Combined sources
Turni395 – 3973Combined sources
Helixi398 – 42730Combined sources
Helixi428 – 4303Combined sources
Helixi431 – 44919Combined sources
Helixi458 – 46912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZW9X-ray1.50A1-496[»]
4ZWBX-ray2.40A1-496[»]
4ZWCX-ray2.60A/B1-496[»]
5C65X-ray2.65A/B1-474[»]
ProteinModelPortaliP11169.
SMRiP11169. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni277 – 2793Important for selectivity against fructose1 Publication
Regioni280 – 2867Monosaccharide binding1 Publication

Domaini

Transport is mediated via a series of conformation changes, switching between a conformation where the substrate-binding cavity is accessible from the outside, and a another conformation where it is accessible from the cytoplasm.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0569. Eukaryota.
COG0477. LUCA.
GeneTreeiENSGT00760000119022.
HOGENOMiHOG000202871.
HOVERGENiHBG014816.
InParanoidiP11169.
KOiK08142.
OMAiXLFLVER.
OrthoDBiEOG7QVM2R.
PhylomeDBiP11169.
TreeFamiTF313762.

Family and domain databases

InterProiIPR002945. Glc_transpt_3.
IPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR01192. GLUCTRSPORT3.
PR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 2 hits.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTQKVTPAL IFAITVATIG SFQFGYNTGV INAPEKIIKE FINKTLTDKG
60 70 80 90 100
NAPPSEVLLT SLWSLSVAIF SVGGMIGSFS VGLFVNRFGR RNSMLIVNLL
110 120 130 140 150
AVTGGCFMGL CKVAKSVEML ILGRLVIGLF CGLCTGFVPM YIGEISPTAL
160 170 180 190 200
RGAFGTLNQL GIVVGILVAQ IFGLEFILGS EELWPLLLGF TILPAILQSA
210 220 230 240 250
ALPFCPESPR FLLINRKEEE NAKQILQRLW GTQDVSQDIQ EMKDESARMS
260 270 280 290 300
QEKQVTVLEL FRVSSYRQPI IISIVLQLSQ QLSGINAVFY YSTGIFKDAG
310 320 330 340 350
VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAFCSTLMT
360 370 380 390 400
VSLLLKDNYN GMSFVCIGAI LVFVAFFEIG PGPIPWFIVA ELFSQGPRPA
410 420 430 440 450
AMAVAGCSNW TSNFLVGLLF PSAAHYLGAY VFIIFTGFLI TFLAFTFFKV
460 470 480 490
PETRGRTFED ITRAFEGQAH GADRSGKDGV MEMNSIEPAK ETTTNV
Length:496
Mass (Da):53,924
Last modified:July 1, 1989 - v1
Checksum:iF601CD6892F16516
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851V → L.
Corresponds to variant rs17728193 [ dbSNP | Ensembl ].
VAR_052502

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20681 mRNA. Translation: AAB61083.1.
AF274892
, AF274889, AF274890, AF274891 Genomic DNA. Translation: AAF82116.1.
CR457413 mRNA. Translation: CAG33694.1.
AK312386 mRNA. Translation: BAG35303.1.
CH471116 Genomic DNA. Translation: EAW88644.1.
CH471116 Genomic DNA. Translation: EAW88645.1.
BC039196 mRNA. Translation: AAH39196.1.
AY034634 mRNA. Translation: AAK56796.1.
CCDSiCCDS8586.1.
PIRiA31986.
T14798.
RefSeqiNP_008862.1. NM_006931.2.
UniGeneiHs.419240.

Genome annotation databases

EnsembliENST00000075120; ENSP00000075120; ENSG00000059804.
GeneIDi6515.
KEGGihsa:6515.
UCSCiuc001qtr.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20681 mRNA. Translation: AAB61083.1.
AF274892
, AF274889, AF274890, AF274891 Genomic DNA. Translation: AAF82116.1.
CR457413 mRNA. Translation: CAG33694.1.
AK312386 mRNA. Translation: BAG35303.1.
CH471116 Genomic DNA. Translation: EAW88644.1.
CH471116 Genomic DNA. Translation: EAW88645.1.
BC039196 mRNA. Translation: AAH39196.1.
AY034634 mRNA. Translation: AAK56796.1.
CCDSiCCDS8586.1.
PIRiA31986.
T14798.
RefSeqiNP_008862.1. NM_006931.2.
UniGeneiHs.419240.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZW9X-ray1.50A1-496[»]
4ZWBX-ray2.40A1-496[»]
4ZWCX-ray2.60A/B1-496[»]
5C65X-ray2.65A/B1-474[»]
ProteinModelPortaliP11169.
SMRiP11169. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112406. 4 interactions.
IntActiP11169. 6 interactions.
MINTiMINT-4999361.
STRINGi9606.ENSP00000075120.

Chemistry

ChEMBLiCHEMBL5215.

Protein family/group databases

TCDBi2.A.1.1.91. the major facilitator superfamily (mfs).

PTM databases

iPTMnetiP11169.
PhosphoSiteiP11169.

Polymorphism and mutation databases

BioMutaiSLC2A3.
DMDMi121760.

Proteomic databases

EPDiP11169.
MaxQBiP11169.
PaxDbiP11169.
PRIDEiP11169.

Protocols and materials databases

DNASUi6515.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000075120; ENSP00000075120; ENSG00000059804.
GeneIDi6515.
KEGGihsa:6515.
UCSCiuc001qtr.4. human.

Organism-specific databases

CTDi6515.
GeneCardsiSLC2A3.
HGNCiHGNC:11007. SLC2A3.
HPAiCAB002763.
HPA006539.
MalaCardsiSLC2A3.
MIMi138170. gene.
neXtProtiNX_P11169.
Orphaneti399. Huntington disease.
PharmGKBiPA35877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0569. Eukaryota.
COG0477. LUCA.
GeneTreeiENSGT00760000119022.
HOGENOMiHOG000202871.
HOVERGENiHBG014816.
InParanoidiP11169.
KOiK08142.
OMAiXLFLVER.
OrthoDBiEOG7QVM2R.
PhylomeDBiP11169.
TreeFamiTF313762.

Enzyme and pathway databases

ReactomeiR-HSA-196836. Vitamin C (ascorbate) metabolism.
R-HSA-428790. Facilitative Na+-independent glucose transporters.
R-HSA-70153. Glucose transport.

Miscellaneous databases

ChiTaRSiSLC2A3. human.
GenomeRNAii6515.
PROiP11169.
SOURCEiSearch...

Gene expression databases

BgeeiP11169.
CleanExiHS_SLC2A3.
ExpressionAtlasiP11169. baseline and differential.
GenevisibleiP11169. HS.

Family and domain databases

InterProiIPR002945. Glc_transpt_3.
IPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR01192. GLUCTRSPORT3.
PR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 2 hits.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues."
    Kayano T., Fukumoto H., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I.
    J. Biol. Chem. 263:15245-15248(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Fetal skeletal muscle.
  2. "Resistance and expression of glucose transporters in human skeletal muscle."
    Stuart C.A., Wen K.G., Acosta M., Wood T.G.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Amygdala.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Duodenum.
  7. "Molecular characterization and cloning of glucose transporters in human articular chondrocytes."
    Neama G., Richardson S., Bell S., Carter S., Mobasheri A.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-453.
    Tissue: Articular cartilage.
  8. "QLS motif in transmembrane helix VII of the glucose transporter family interacts with the C-1 (position) of D-glucose and is involved in substrate selection at the exofacial binding site."
    Seatter M.J., de la Rue S.A., Porter L.M., Gould G.W.
    Biochemistry 37:1322-1326(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY, REGION, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 277-GLN--SER-279.
  9. "Molecular basis of ligand recognition and transport by glucose transporters."
    Deng D., Sun P., Yan C., Ke M., Jiang X., Xiong L., Ren W., Hirata K., Yamamoto M., Fan S., Yan N.
    Nature 526:391-396(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH GLUCOSE, SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, DOMAIN.

Entry informationi

Entry nameiGTR3_HUMAN
AccessioniPrimary (citable) accession number: P11169
Secondary accession number(s): B2R606
, D3DUU6, Q6I9U2, Q9UG15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 169 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

3D-structure, 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. 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.