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Q7L5Y1 (ENOF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial enolase superfamily member 1

EC=4.2.1.68
Alternative name(s):
Antisense RNA to thymidylate synthase
Short name=rTS
L-fuconate dehydratase
Gene names
Name:ENOSF1
Synonyms:RTS, TYMSAS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. May down-regulate thymidylate synthase activity, possibly already at the RNA level, by promoting the degradation of TYMS mRNA via an antisense RNA-based mechanism. Ref.7 Ref.8 Ref.9 Ref.13

Catalytic activity

L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O. Ref.13

Cofactor

Binds 1 Mg2+ per subunit. Ref.13

Subcellular location

Mitochondrion Ref.10.

Post-translational modification

Could be sumoylated. Ref.11

Sequence similarities

Belongs to the mandelate racemase/muconate lactonizing enzyme family. ENOSF1 subfamily.

Caution

Was originally (Ref.1) identified as a gene coding for an antisense RNA to thymidylate synthase.

Biophysicochemical properties

Kinetic parameters:

kcat is 0.5 sec(-1) for L-fuconate. kcat is 0.3 sec(-1) for L-galactonate. kcat is 0.3 sec(-1) for L-arabinonate. kcat is 0.04 sec(-1) for D-arabinonate. kcat is 0.002 sec(-1) for D-ribonate.

KM=0.2 mM for L-fuconate Ref.13

KM=3.0 mM for L-galactonate

KM=2.0 mM for D-arabinonate

KM=4.0 mM for L-arabinonate

KM=0.4 mM for D-ribonate

Sequence caution

The sequence AAG29537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA47471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
Lyase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular amino acid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionisomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7L5Y1-1)

Also known as: rTSgamma;

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: Q7L5Y1-2)

Also known as: rTSalpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.
     103-103: W → MQKMESRGVELPSLWEKALKL
Isoform 3 (identifier: Q7L5Y1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     65-117: VVCAVNALAH...KGVVHLATAA → DWSRKGRGAP...GILHRFQVHH
     118-443: Missing.
Isoform 4 (identifier: Q7L5Y1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MVRGRISRLSVRDVRFPTSLGGHG → MVSADAMVSADAMVSADAMVSADAMVSADAMVSADAMVSADAMVS
     293-306: Missing.
Note: Gene prediction based on EST data.
Isoform 5 (identifier: Q7L5Y1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MVRGRISRLSVRDVRFPTSLGGHG → MVSADAMVSA...AMVSADAMVS
     293-306: Missing.
Isoform 6 (identifier: Q7L5Y1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
Isoform 7 (identifier: Q7L5Y1-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-230: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Mitochondrial enolase superfamily member 1
PRO_0000331652

Regions

Region24 – 263Substrate binding By similarity
Region355 – 3573Substrate binding By similarity

Sites

Active site2221Proton donor/acceptor By similarity
Active site3551 Potential
Metal binding2501Magnesium
Metal binding2761Magnesium
Metal binding3051Magnesium
Binding site341Substrate By similarity
Binding site2201Substrate By similarity
Binding site2521Substrate By similarity
Binding site2761Substrate By similarity
Binding site3051Substrate By similarity
Binding site3861Substrate By similarity

Amino acid modifications

Modified residue1481Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 230230Missing in isoform 7.
VSP_055241
Alternative sequence1 – 181181Missing in isoform 6.
VSP_055242
Alternative sequence1 – 102102Missing in isoform 2.
VSP_033311
Alternative sequence1 – 2424MVRGR…LGGHG → MVSADAMVSADAMVSADAMV SADAMVSADAMVSADAMVSA DAMVS in isoform 4.
VSP_047153
Alternative sequence1 – 2424MVRGR…LGGHG → MVSADAMVSADAMVSADAMV SADAMVSADAMVSADAMVSA DAMVSADAMVSADAMVSADA MVSADAMVS in isoform 5.
VSP_055243
Alternative sequence65 – 11753VVCAV…LATAA → DWSRKGRGAPGDSGRPKRGV GLVGQAGGKACLEVTCGHGS QDAGILHRFQVHH in isoform 3.
VSP_033312
Alternative sequence1031W → MQKMESRGVELPSLWEKALK L in isoform 2.
VSP_033313
Alternative sequence118 – 443326Missing in isoform 3.
VSP_033314
Alternative sequence293 – 30614Missing in isoform 4 and isoform 5.
VSP_047154
Natural variant311D → E.
Corresponds to variant rs34724061 [ dbSNP | Ensembl ].
VAR_042933
Natural variant1451M → T. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs2612086 [ dbSNP | Ensembl ].
VAR_042934
Natural variant4281Y → S.
Corresponds to variant rs2847620 [ dbSNP | Ensembl ].
VAR_042935

Experimental info

Mutagenesis1 – 2727Missing: Impairs protein solubility. Abolishes catalytic activity. Ref.13

Secondary structure

.............................................................................. 443
Helix Strand Turn

Details...

Sequences

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

Last modified May 24, 2005. Version 1.
Checksum: 82BEDAC229D1A729

FASTA44349,786
        10         20         30         40         50         60 
MVRGRISRLS VRDVRFPTSL GGHGADAMHT DPDYSAAYVV IETDAEDGIK GCGITFTLGK 

        70         80         90        100        110        120 
GTEVVVCAVN ALAHHVLNKD LKDIVGDFRG FYRQLTSDGQ LRWIGPEKGV VHLATAAVLN 

       130        140        150        160        170        180 
AVWDLWAKQE GKPVWKLLVD MDPRMLVSCI DFRYITDVLT EEDALEILQK GQIGKKEREK 

       190        200        210        220        230        240 
QMLAQGYPAY TTSCAWLGYS DDTLKQLCAQ ALKDGWTRFK VKVGADLQDD MRRCQIIRDM 

       250        260        270        280        290        300 
IGPEKTLMMD ANQRWDVPEA VEWMSKLAKF KPLWIEEPTS PDDILGHATI SKALVPLGIG 

       310        320        330        340        350        360 
IATGEQCHNR VIFKQLLQAK ALQFLQIDSC RLGSVNENLS VLLMAKKFEI PVCPHAGGVG 

       370        380        390        400        410        420 
LCELVQHLII FDYISVSASL ENRVCEYVDH LHEHFKYPVM IQRASYMPPK DPGYSTEMKE 

       430        440 
ESVKKHQYPD GEVWKKLLPA QEN 

« Hide

Isoform 2 (rTSalpha) [UniParc].

Checksum: 73B469F1C9C7E144
Show »

FASTA36141,024
Isoform 3 [UniParc].

Checksum: B277BFA534E7DAF2
Show »

FASTA11712,286
Isoform 4 [UniParc].

Checksum: 7D6BD13DF0F12AD0
Show »

FASTA45050,170
Isoform 5 [UniParc].

Checksum: 97FA6018CAADF8CB
Show »

FASTA47452,468
Isoform 6 [UniParc].

Checksum: 5296CB2DCA806273
Show »

FASTA26229,710
Isoform 7 [UniParc].

Checksum: F2CF0580E05E10BA
Show »

FASTA21324,284

References

« Hide 'large scale' references
[1]"Cloning and characterization of a naturally occurring antisense RNA to human thymidylate synthase mRNA."
Dolnick B.J.
Nucleic Acids Res. 21:1747-1752(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANT THR-145.
Tissue: Cervix carcinoma.
[2]"Alternate splicing of the rTS gene product and its overexpression in a 5-fluorouracil-resistant cell line."
Dolnick B.J., Black A.R.
Cancer Res. 56:3207-3210(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 23-443 (ISOFORM 3), VARIANT THR-145.
Tissue: Cervix carcinoma.
[3]"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] (ISOFORMS 1; 5; 6 AND 7), VARIANT THR-145.
Tissue: Trachea.
[4]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-145.
[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] (ISOFORM 1).
Tissue: Placenta.
[7]"rTS gene expression is associated with altered cell sensitivity to thymidylate synthase inhibitors."
Dolnick B.J., Black A.R., Winkler P.M., Schindler K., Hsueh C.-T.
Adv. Enzyme Regul. 36:165-180(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Natural antisense (rTSalpha) RNA induces site-specific cleavage of thymidylate synthase mRNA."
Chu J., Dolnick B.J.
Biochim. Biophys. Acta 1587:183-193(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"A novel function for the rTS gene."
Dolnick B.J., Angelino N.J., Dolnick R., Sufrin J.R.
Cancer Biol. Ther. 2:364-369(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Comparative genomic analysis reveals a novel mitochondrial isoform of human rTS protein and unusual phylogenetic distribution of the rTS gene."
Liang P., Nair J.R., Song L., McGuire J.J., Dolnick B.J.
BMC Genomics 6:125-125(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Enhancement of 5-fluorouracil sensitivity by an rTS signaling mimic in H630 colon cancer cells."
Dolnick R., Wu Q., Angelino N.J., Stephanie L.V., Chow K.-C., Sufrin J.R., Dolnick B.J.
Cancer Res. 65:5917-5924(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-148, SUMOYLATION.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Enzymatic and structural characterization of rTSgamma provides insights into the function of rTSbeta."
Wichelecki D.J., Froese D.S., Kopec J., Muniz J.R., Yue W.W., Gerlt J.A.
Biochemistry 53:2732-2738(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-440 IN COMPLEX WITH MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 1-MET--HIS-27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF305057 Genomic DNA. Translation: AAG29536.1.
X67098 mRNA. Translation: CAA47472.1.
AF305057 Genomic DNA. Translation: AAG29537.1. Different initiation.
X67098 mRNA. Translation: CAA47471.1. Different initiation.
X89602 mRNA. Translation: CAA61761.1.
AK127818 mRNA. Translation: BAC87148.1.
AK093873 mRNA. Translation: BAG52778.1.
AK127219 mRNA. Translation: BAG54456.1.
AK292780 mRNA. Translation: BAF85469.1.
AP001178 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01713.1.
CH471113 Genomic DNA. Translation: EAX01714.1.
CH471113 Genomic DNA. Translation: EAX01715.1.
BC001285 mRNA. Translation: AAH01285.2.
CCDSCCDS11822.1. [Q7L5Y1-1]
CCDS11823.1. [Q7L5Y1-4]
CCDS45821.1. [Q7L5Y1-2]
RefSeqNP_001119595.1. NM_001126123.3. [Q7L5Y1-2]
NP_059982.2. NM_017512.5. [Q7L5Y1-1]
NP_974487.1. NM_202758.3. [Q7L5Y1-4]
UniGeneHs.658550.
Hs.731510.
Hs.732707.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A35X-ray1.74A1-440[»]
ProteinModelPortalQ7L5Y1.
SMRQ7L5Y1. Positions 1-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120716. 1 interaction.
IntActQ7L5Y1. 1 interaction.
STRING9606.ENSP00000345974.

PTM databases

PhosphoSiteQ7L5Y1.

Polymorphism databases

DMDM74739173.

Proteomic databases

MaxQBQ7L5Y1.
PaxDbQ7L5Y1.
PRIDEQ7L5Y1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251101; ENSP00000251101; ENSG00000132199. [Q7L5Y1-1]
ENST00000319815; ENSP00000313346; ENSG00000132199.
ENST00000340116; ENSP00000345974; ENSG00000132199. [Q7L5Y1-4]
ENST00000383578; ENSP00000373072; ENSG00000132199. [Q7L5Y1-2]
GeneID55556.
KEGGhsa:55556.
UCSCuc002kkt.4. human. [Q7L5Y1-2]
uc002kku.4. human. [Q7L5Y1-1]

Organism-specific databases

CTD55556.
GeneCardsGC18M000664.
HGNCHGNC:30365. ENOSF1.
HPAHPA047829.
MIM607427. gene.
neXtProtNX_Q7L5Y1.
PharmGKBPA134897613.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4948.
HOVERGENHBG053904.
OMAHEHFLYP.
OrthoDBEOG77DJ5S.
PhylomeDBQ7L5Y1.
TreeFamTF300529.

Gene expression databases

ArrayExpressQ7L5Y1.
BgeeQ7L5Y1.
CleanExHS_ENOSF1.
GenevestigatorQ7L5Y1.

Family and domain databases

Gene3D3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N.
IPR001354. MR_MLE.
[Graphical view]
PANTHERPTHR13794. PTHR13794. 1 hit.
PfamPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEPS00909. MR_MLE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENOSF1. human.
GenomeRNAi55556.
NextBio60026.
PROQ7L5Y1.
SOURCESearch...

Entry information

Entry nameENOF1_HUMAN
AccessionPrimary (citable) accession number: Q7L5Y1
Secondary accession number(s): A6NMP3 expand/collapse secondary AC list , A8K9R5, B3KSL6, B3KXE4, D3DUH0, Q15407, Q15594, Q15595, Q6ZS08, Q9HAS5, Q9HAS6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 24, 2005
Last modified: July 9, 2014
This is version 79 of the entry and version 1 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

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 18

Human chromosome 18: entries, gene names and cross-references to MIM