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P35625 (TIMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metalloproteinase inhibitor 3
Alternative name(s):
Protein MIG-5
Tissue inhibitor of metalloproteinases 3
Short name=TIMP-3
Gene names
Name:TIMP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

Subunit structure

Interacts with EFEMP1. Ref.16

Subcellular location

Secretedextracellular spaceextracellular matrix.

Involvement in disease

Sorsby fundus dystrophy (SFD) [MIM:136900]: Rare autosomal dominant macular disorder with an age of onset in the fourth decade. It is characterized by loss of central vision from subretinal neovascularization and atrophy of the ocular tissues. Generally, macular disciform degeneration develops in the patients eye within 6 months to 6 years.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Sequence similarities

Belongs to the protease inhibitor I35 (TIMP) family. [View classification]

Contains 1 NTR domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AGTR2P500527EBI-1748085,EBI-1748067

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.14
Chain24 – 211188Metalloproteinase inhibitor 3
PRO_0000034341

Regions

Domain24 – 143120NTR
Region24 – 285Involved in metalloproteinase-binding
Region88 – 892Involved in metalloproteinase-binding
Region105 – 18884Mediates interaction with EFEMP1

Sites

Metal binding241Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner

Amino acid modifications

Disulfide bond24 ↔ 91 Ref.17
Disulfide bond26 ↔ 118 Ref.17
Disulfide bond36 ↔ 143 Ref.17
Disulfide bond145 ↔ 192 By similarity
Disulfide bond150 ↔ 155 By similarity
Disulfide bond163 ↔ 184 By similarity

Natural variations

Natural variant1791S → C in SFD. Ref.19
VAR_007508
Natural variant1891G → C in SFD. Ref.22
VAR_008290
Natural variant1901G → C in SFD. Ref.20
VAR_010901
Natural variant1911Y → C in SFD. Ref.18 Ref.21
VAR_007509
Natural variant2041S → C in SFD. Ref.18
VAR_007510

Experimental info

Sequence conflict16 – 238LGDWGAEA → WGTGAPR in CAA82918. Ref.4
Sequence conflict21 – 222AE → R in AAA21815. Ref.13

Secondary structure

........................... 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35625 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 15CF831028BABF7A

FASTA21124,145
        10         20         30         40         50         60 
MTPWLGLIVL LGSWSLGDWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK LVKEGPFGTL 

        70         80         90        100        110        120 
VYTIKQMKMY RGFTKMPHVQ YIHTEASESL CGLKLEVNKY QYLLTGRVYD GKMYTGLCNF 

       130        140        150        160        170        180 
VERWDQLTLS QRKGLNYRYH LGCNCKIKSC YYLPCFVTSK NECLWTDMLS NFGYPGYQSK 

       190        200        210 
HYACIRQKGG YCSWYRGWAP PDKSIINATD P 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression in breast tumors of human TIMP-3, a new member of the metalloproteinase inhibitor family."
Uria J.A., Ferrando A.A., Velasco G., Freije J.M., Lopez-Otin C.
Cancer Res. 54:2091-2094(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[2]"Cloning and characterization of human tissue inhibitor of metalloproteinases-3."
Wilde C.G., Hawkins P.R., Coleman R.T., Levine W.B., Delegeane A.M., Okamoto P.M., Ito L.Y., Scott R.W., Seilhamer J.J.
DNA Cell Biol. 13:711-718(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family."
Silbiger S.M., Jacobsen V.L., Cupples R.L., Koski R.A.
Gene 141:293-297(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[4]"A novel member of human tissue inhibitor of metalloproteinases (TIMP) gene family is regulated during G1 progression, mitogenic stimulation, differentiation, and senescence."
Wick M., Buerger C., Bruesselbach S., Lucibello F., Mueller R.
J. Biol. Chem. 269:18953-18960(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Genomic organization of the human tissue inhibitor of metalloproteinases-3 (TIMP3)."
Stoehr H., Roomp K., Felbor U., Weber B.H.F.
Genome Res. 5:483-487(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"TIMP-3 is expressed in the human retinal pigment epithelium."
Ruiz A.C., Brett P., Bok D.
Biochem. Biophys. Res. Commun. 226:467-474(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]"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].
Tissue: Placenta.
[10]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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: Pancreas.
[13]"Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22."
Apte S.S., Mattei M.-G., Olsen B.R.
Genomics 19:86-90(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-211.
Tissue: Placenta.
[14]"Identification and characterization of human tissue inhibitor of metalloproteinase-3 and detection of three additional metalloproteinase inhibitor activities in extracellular matrix."
Kishnani N.S., Staskus P.W., Yang T.-T., Masiarz F.R., Hawkes S.P.
Matrix Biol. 14:479-488(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-41.
[15]"Cloning and partial structure of the gene encoding human tissue inhibitor of metalloproteinases-3."
Hammani K., Henriet P.M., Silbiger S.M., DeClerck Y.A.
Gene 170:287-288(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-211.
Tissue: Placenta.
[16]"Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1). Implications for macular degenerations."
Klenotic P.A., Munier F.L., Marmorstein L.Y., Anand-Apte B.
J. Biol. Chem. 279:30469-30473(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EFEMP1.
[17]"Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex."
Wisniewska M., Goettig P., Maskos K., Belouski E., Winters D., Hecht R., Black R., Bode W.
J. Mol. Biol. 381:1307-1319(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 24-144 IN COMPLEX WITH TACE, DISULFIDE BONDS.
[18]"Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy."
Weber B.H.F., Vogt G., Pruett R.C., Stoehr H., Felbor U.
Nat. Genet. 8:352-356(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SFD CYS-191 AND CYS-204.
[19]"A novel Ser156Cys mutation in the tissue inhibitor of metalloproteinases-3 (TIMP3) in Sorsby's fundus dystrophy with unusual clinical features."
Felbor U., Stoehr H., Amann T., Schoenherr U., Weber B.H.F.
Hum. Mol. Genet. 4:2415-2416(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SFD CYS-179.
[20]"Night blindness in Sorsby's fundus dystrophy reversed by vitamin A."
Jacobson S.G., Cideciyan A.V., Regunath G., Rodriguez F.J., Vandenburgh K., Sheffield V.C., Stone E.M.
Nat. Genet. 11:27-32(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SFD CYS-190.
[21]"A second independent Tyr168Cys mutation in the tissue inhibitor of metalloproteinases-3 (TIMP3) in Sorsby's fundus dystrophy."
Felbor U., Stoehr H., Amann T., Schoenherr U., Apfelstedt-Sylla E., Weber B.H.F.
J. Med. Genet. 33:233-236(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SFD CYS-191.
[22]"Autosomal recessive Sorsby fundus dystrophy revisited: molecular evidence for dominant inheritance."
Felbor U., Suvanto E.A., Forsius H.R., Eriksson A.W., Weber B.H.
Am. J. Hum. Genet. 60:57-62(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SFD CYS-189.
+Additional computationally mapped references.

Web resources

Mutations of the TIMP3 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76227 mRNA. Translation: CAA53813.1.
S78453 mRNA. Translation: AAB34532.1.
U14394 mRNA. Translation: AAB60373.1.
U02571 mRNA. Translation: AAA17672.1.
Z30183 Genomic DNA. Translation: CAA82918.1.
U33114 expand/collapse EMBL AC list , U33110, U33111, U33112, U33113 Genomic DNA. Translation: AAC50393.1.
U67195 mRNA. Translation: AAB07547.1.
CR456593 mRNA. Translation: CAG30479.1.
BT006848 mRNA. Translation: AAP35494.1.
AK314871 mRNA. Translation: BAG37386.1.
AL023282, Z98256 Genomic DNA. Translation: CAI17996.1.
Z98256, AL023282 Genomic DNA. Translation: CAI20115.1.
CH471095 Genomic DNA. Translation: EAW60038.1.
BC014277 mRNA. Translation: AAH14277.1.
L15078 mRNA. Translation: AAA21815.1.
U38955 expand/collapse EMBL AC list , U38952, U38953, U38954 Genomic DNA. Translation: AAB17602.1.
PIRS45317.
RefSeqNP_000353.1. NM_000362.4.
UniGeneHs.644633.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CKIX-ray2.30B24-144[»]
ProteinModelPortalP35625.
SMRP35625. Positions 24-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112934. 3 interactions.
IntActP35625. 2 interactions.
STRING9606.ENSP00000266085.

PTM databases

PhosphoSiteP35625.

Polymorphism databases

DMDM730948.

Proteomic databases

PaxDbP35625.
PRIDEP35625.

Protocols and materials databases

DNASU7078.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266085; ENSP00000266085; ENSG00000100234.
GeneID7078.
KEGGhsa:7078.
UCSCuc003anb.3. human.

Organism-specific databases

CTD7078.
GeneCardsGC22P033196.
HGNCHGNC:11822. TIMP3.
HPACAB022187.
MIM136900. phenotype.
188826. gene.
neXtProtNX_P35625.
Orphanet59181. Sorsby's fundus dystrophy.
PharmGKBPA36528.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250837.
HOGENOMHOG000285981.
HOVERGENHBG068749.
InParanoidP35625.
KOK16866.
OMAKEGYCSW.
OrthoDBEOG79GT74.
PhylomeDBP35625.
TreeFamTF317409.

Gene expression databases

BgeeP35625.
CleanExHS_TIMP3.
GenevestigatorP35625.

Family and domain databases

Gene3D3.90.370.10. 1 hit.
InterProIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR027465. TIMP_C_dom.
IPR015612. Tissue_inhib_metalloprotease_3.
[Graphical view]
PANTHERPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF6. PTHR11844:SF6. 1 hit.
PfamPF00965. TIMP. 1 hit.
[Graphical view]
SMARTSM00206. NTR. 1 hit.
[Graphical view]
SUPFAMSSF50242. SSF50242. 1 hit.
PROSITEPS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP35625.
GeneWikiTIMP3.
GenomeRNAi7078.
NextBio27685.
PROP35625.
SOURCESearch...

Entry information

Entry nameTIMP3_HUMAN
AccessionPrimary (citable) accession number: P35625
Secondary accession number(s): B2RBY9 expand/collapse secondary AC list , Q5THV4, Q9UC74, Q9UGS2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 147 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

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 22

Human chromosome 22: entries, gene names and cross-references to MIM