Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BYC5 (FUT8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-(1,6)-fucosyltransferase

Short name=Alpha1-6FucT
EC=2.4.1.68
Alternative name(s):
Fucosyltransferase 8
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
GDP-fucose--glycoprotein fucosyltransferase
Glycoprotein 6-alpha-L-fucosyltransferase
Gene names
Name:FUT8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. Ref.1 Ref.9

Catalytic activity

GDP-beta-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->6))-N-acetyl-beta-D-glucosaminyl)asparagine. Ref.9

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein By similarity. Note: Membrane-bound form in trans cisternae of Golgi By similarity.

Sequence similarities

Belongs to the glycosyltransferase 23 family.

Contains 1 GT23 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3 domain
SH3-binding
Signal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGDP-L-fucose metabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

L-fucose catabolic process

Non-traceable author statement PubMed 11698403. Source: UniProtKB

N-glycan fucosylation

Inferred from direct assay Ref.9. Source: GOC

N-glycan processing

Traceable author statement PubMed 11698403. Source: UniProtKB

cell migration

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

in utero embryonic development

Non-traceable author statement PubMed 11698403. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

oligosaccharide biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation

Traceable author statement Ref.1. Source: ProtInc

protein N-linked glycosylation via asparagine

Inferred from direct assay Ref.9. Source: UniProtKB

protein glycosylation in Golgi

Inferred from electronic annotation. Source: InterPro

receptor metabolic process

Inferred from electronic annotation. Source: Ensembl

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Non-traceable author statement PubMed 11698403. Source: UniProtKB

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglycoprotein 6-alpha-L-fucosyltransferase activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BYC5-1)

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.
Isoform 2 (identifier: Q9BYC5-2)

Also known as: Retinal;

The sequence of this isoform differs from the canonical sequence as follows:
     280-329: EVKDKNVQVV...HGDPAVWWVS → TPIMNLLVITLFPGQLDCTIDTQKIHFVE
     330-575: Missing.
Isoform 3 (identifier: Q9BYC5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.
Isoform 4 (identifier: Q9BYC5-4)

Also known as: Retina-1; Retina-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MRPWTGSWRWIMLI → MHRQIWHLHWTLVR
     15-420: Missing.
Note: Seems to be only expressed in retina, inactive as a fucosyltransferase.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Alpha-(1,6)-fucosyltransferase
PRO_0000080526

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 575545Lumenal Potential
Domain206 – 493288GT23
Domain502 – 56362SH3
Region365 – 3662Important for donor substrate binding
Motif299 – 3057SH3-binding Potential

Amino acid modifications

Disulfide bond204 ↔ 266 Ref.9
Disulfide bond212 ↔ 230 Ref.9
Disulfide bond218 ↔ 222 Ref.9
Disulfide bond465 ↔ 472 Ref.9

Natural variations

Alternative sequence1 – 163163Missing in isoform 3.
VSP_046837
Alternative sequence1 – 1414MRPWT…WIMLI → MHRQIWHLHWTLVR in isoform 4.
VSP_053361
Alternative sequence15 – 420406Missing in isoform 4.
VSP_053362
Alternative sequence280 – 32950EVKDK…VWWVS → TPIMNLLVITLFPGQLDCTI DTQKIHFVE in isoform 2.
VSP_001807
Alternative sequence330 – 575246Missing in isoform 2.
VSP_001808
Natural variant1011K → Q.
Corresponds to variant rs2229678 [ dbSNP | Ensembl ].
VAR_054038
Natural variant2671T → K.
Corresponds to variant rs35949016 [ dbSNP | Ensembl ].
VAR_033537

Experimental info

Mutagenesis3651R → A or K: Complete loss of activity. Ref.8 Ref.9
Mutagenesis3661R → A or K: Decreases activity to 3%. Ref.8
Mutagenesis3681D → A: Loss of enzyme activity. Ref.9
Mutagenesis3691K → A: Loss of enzyme activity. Ref.9
Mutagenesis3731E → A: Loss of enzyme activity. Ref.9
Mutagenesis3821Y → A: Loss of enzyme activity. Ref.9
Mutagenesis4091D → A: Loss of enzyme activity. Ref.9
Mutagenesis4101D → A: No effect on enzyme activity. Ref.9
Mutagenesis4531D → A: Loss of enzyme activity. Ref.9
Mutagenesis4691S → A: Loss of enzyme activity. Ref.9
Sequence conflict2141I → T in BAG57538. Ref.5

Secondary structure

.............................................................. 575
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 5, 2002. Version 2.
Checksum: 5AE24A93881E18D0

FASTA57566,516
        10         20         30         40         50         60 
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL 

        70         80         90        100        110        120 
RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY KKQTRNGLGK DHEILRRRIE 

       130        140        150        160        170        180 
NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR 

       190        200        210        220        230        240 
EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT 

       250        260        270        280        290        300 
LILESQNWRY ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR 

       310        320        330        340        350        360 
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI 

       370        380        390        400        410        420 
GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PSLLKEAKTK 

       430        440        450        460        470        480 
YPNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ 

       490        500        510        520        530        540 
TLHPDASANF HSLDDIYYFG GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS 

       550        560        570 
KGVNRKLGRT GLYPSYKVRE KIETVKYPTY PEAEK 

« Hide

Isoform 2 (Retinal) [UniParc].

Checksum: FB52A33CFD91A366
Show »

FASTA30835,795
Isoform 3 [UniParc].

Checksum: 837F36AF48E7E4C3
Show »

FASTA41247,255
Isoform 4 (Retina-1) (Retina-2) [UniParc].

Checksum: 0ACD43AA0F56AB31
Show »

FASTA16919,520

References

« Hide 'large scale' references
[1]"Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells."
Yanagidani S., Uozumi N., Ihara Y., Miyoshi E., Yamaguchi N., Taniguchi N.
J. Biochem. 121:626-632(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]"Differential splice variants of human FUT8 embryonic cDNA."
Cailleau A., Balanzino L., Candelier J.J., Oriol R., Mollicone R.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryo.
[3]"Genomic structure and promoter analysis of the human alpha1,6-fucosyltransferase gene (FUT8)."
Yamaguchi Y., Ikeda Y., Takahashi T., Ihara H., Tanaka T., Sasho C., Uozumi N., Yanagidani S., Inoue S., Fujii J., Taniguchi N.
Glycobiology 10:637-643(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
[4]"Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis."
Martinez-Duncker I., Michalski J.C., Bauvy C., Candelier J.J., Mennesson B., Codogno P., Oriol R., Mollicone R.
Glycobiology 14:13-25(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING.
Tissue: Embryo.
[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. expand/collapse author list , 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 3).
Tissue: Amygdala.
[6]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [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 4).
Tissue: Lung.
[8]"A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues."
Takahashi T., Ikeda Y., Tateishi A., Yamaguchi Y., Ishikawa M., Taniguchi N.
Glycobiology 10:503-510(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DONOR SUBSTRATE-BINDING, MUTAGENESIS OF ARG-365 AND ARG-366.
[9]"Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8."
Ihara H., Ikeda Y., Toma S., Wang X., Suzuki T., Gu J., Miyoshi E., Tsukihara T., Honke K., Matsumoto A., Nakagawa A., Taniguchi N.
Glycobiology 17:455-466(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 68-575, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BOND, MUTAGENESIS OF ARG-365; ASP-368; LYS-369; GLU-373; TYR-382; ASP-409; ASP-410; ASP-453 AND SER-469.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89289 mRNA. Translation: BAA19764.1.
AH005745 Genomic DNA. Translation: AAB92372.2.
Y17979 mRNA. Translation: CAA76988.1.
Y17976 mRNA. Translation: CAA76985.1.
Y17977 mRNA. Translation: CAA76986.1.
Y17978 mRNA. Translation: CAA76987.1.
AB049828 Genomic DNA. Translation: BAB40975.1.
AB049740 mRNA. Translation: BAB40929.2.
AB032573 Genomic DNA. Translation: BAA92859.2.
AB032573 Genomic DNA. Translation: BAA92858.1.
AJ514324 mRNA. Translation: CAD55804.1.
AJ514325 mRNA. Translation: CAD55805.1.
AK294242 mRNA. Translation: BAG57538.1.
AL109847 Genomic DNA. No translation available.
AL161871 Genomic DNA. No translation available.
AL355840 Genomic DNA. No translation available.
AL359236 Genomic DNA. No translation available.
BC093889 mRNA. Translation: AAH93889.1.
BC101816 mRNA. Translation: AAI01817.1.
PIRJC5432.
RefSeqNP_004471.4. NM_004480.4.
NP_835368.1. NM_178155.2.
NP_835369.1. NM_178156.2.
UniGeneHs.597649.
Hs.654961.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DE0X-ray2.61X68-575[»]
ProteinModelPortalQ9BYC5.
SMRQ9BYC5. Positions 108-572.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108806. 6 interactions.
IntActQ9BYC5. 2 interactions.
STRING9606.ENSP00000353910.

Protein family/group databases

CAZyGT23. Glycosyltransferase Family 23.

PTM databases

PhosphoSiteQ9BYC5.

Polymorphism databases

DMDM20138326.

Proteomic databases

PaxDbQ9BYC5.
PRIDEQ9BYC5.

Protocols and materials databases

DNASU2530.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342677; ENSP00000345865; ENSG00000033170. [Q9BYC5-2]
ENST00000360689; ENSP00000353910; ENSG00000033170. [Q9BYC5-1]
ENST00000394585; ENSP00000378086; ENSG00000033170. [Q9BYC5-1]
ENST00000394586; ENSP00000378087; ENSG00000033170. [Q9BYC5-1]
ENST00000417683; ENSP00000396770; ENSG00000033170. [Q9BYC5-4]
ENST00000557164; ENSP00000452433; ENSG00000033170. [Q9BYC5-3]
GeneID2530.
KEGGhsa:2530.
UCSCuc001xin.3. human. [Q9BYC5-1]

Organism-specific databases

CTD2530.
GeneCardsGC14P065877.
HGNCHGNC:4019. FUT8.
HPACAB017129.
HPA040863.
HPA043410.
MIM602589. gene.
neXtProtNX_Q9BYC5.
PharmGKBPA28435.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251249.
HOGENOMHOG000007175.
HOVERGENHBG028260.
InParanoidQ9BYC5.
KOK00717.
OMAHNQIAVY.
OrthoDBEOG7N37C3.
PhylomeDBQ9BYC5.
TreeFamTF106108.

Enzyme and pathway databases

BRENDA2.4.1.68. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9BYC5.
BgeeQ9BYC5.
CleanExHS_FUT8.
GenevestigatorQ9BYC5.

Family and domain databases

InterProIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PIRSFPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51659. GT23. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFUT8. human.
EvolutionaryTraceQ9BYC5.
GeneWikiFUT8.
GenomeRNAi2530.
NextBio13637592.
PROQ9BYC5.
SOURCESearch...

Entry information

Entry nameFUT8_HUMAN
AccessionPrimary (citable) accession number: Q9BYC5
Secondary accession number(s): B4DFS7 expand/collapse secondary AC list , G3V5N0, O00235, Q8IUA5, Q9BYC6, Q9P2U5, Q9P2U6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM