UniProtKB/Swiss-Prot P08603: Variant p.Tyr402His

Complement factor H
Gene: CFH
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Variant information Variant position:

402 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Tyrosine (Y) to Histidine (H) at position 402 (Y402H, p.Tyr402His). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Change from large size and aromatic (Y) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Variant description:

Associated with ARMD4. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1061170 [ dbSNP | Ensembl ]

Sequence information Variant position:

402 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1231 The length of the canonical sequence.
Location on the sequence:

AVPCLRKCYFPYLENGYNQN Y GRKFVQGKSIDVACHPGYAL The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         AVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYAL

Mouse                         EVPCVRKCVFHYVENGDSAYWEKVYVQGQSLKVQCYNGYSL

Bovine                        EEPCLRQCIFNYLENGHTPYREEKYLQGETVRVRCYEGYSL

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	19 – 1231	Complement factor H
Domain	387 – 444	Sushi 7
Disulfide bond	389 – 431
Turn	400 – 403

Literature citations
The complete amino acid sequence of human complement factor H.
Ripoche J.; Day A.J.; Harris T.J.R.; Sim R.B.;
Biochem. J. 249:593-602(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2); GLYCOSYLATION AT ASN-529; VARIANTS HIS-402 AND ARG-493; The DNA sequence and biological annotation of human chromosome 1.
Gregory S.G.; Barlow K.F.; McLay K.E.; Kaul R.; Swarbreck D.; Dunham A.; Scott C.E.; Howe K.L.; Woodfine K.; Spencer C.C.A.; Jones M.C.; Gillson C.; Searle S.; Zhou Y.; Kokocinski F.; McDonald L.; Evans R.; Phillips K.; Atkinson A.; Cooper R.; Jones C.; Hall R.E.; Andrews T.D.; Lloyd C.; Ainscough R.; Almeida J.P.; Ambrose K.D.; Anderson F.; Andrew R.W.; Ashwell R.I.S.; Aubin K.; Babbage A.K.; Bagguley C.L.; Bailey J.; Beasley H.; Bethel G.; Bird C.P.; Bray-Allen S.; Brown J.Y.; Brown A.J.; Buckley D.; Burton J.; Bye J.; Carder C.; Chapman J.C.; Clark S.Y.; Clarke G.; Clee C.; Cobley V.; Collier R.E.; Corby N.; Coville G.J.; Davies J.; Deadman R.; Dunn M.; Earthrowl M.; Ellington A.G.; Errington H.; Frankish A.; Frankland J.; French L.; Garner P.; Garnett J.; Gay L.; Ghori M.R.J.; Gibson R.; Gilby L.M.; Gillett W.; Glithero R.J.; Grafham D.V.; Griffiths C.; Griffiths-Jones S.; Grocock R.; Hammond S.; Harrison E.S.I.; Hart E.; Haugen E.; Heath P.D.; Holmes S.; Holt K.; Howden P.J.; Hunt A.R.; Hunt S.E.; Hunter G.; Isherwood J.; James R.; Johnson C.; Johnson D.; Joy A.; Kay M.; Kershaw J.K.; Kibukawa M.; Kimberley A.M.; King A.; Knights A.J.; Lad H.; Laird G.; Lawlor S.; Leongamornlert D.A.; Lloyd D.M.; Loveland J.; Lovell J.; Lush M.J.; Lyne R.; Martin S.; Mashreghi-Mohammadi M.; Matthews L.; Matthews N.S.W.; McLaren S.; Milne S.; Mistry S.; Moore M.J.F.; Nickerson T.; O'Dell C.N.; Oliver K.; Palmeiri A.; Palmer S.A.; Parker A.; Patel D.; Pearce A.V.; Peck A.I.; Pelan S.; Phelps K.; Phillimore B.J.; Plumb R.; Rajan J.; Raymond C.; Rouse G.; Saenphimmachak C.; Sehra H.K.; Sheridan E.; Shownkeen R.; Sims S.; Skuce C.D.; Smith M.; Steward C.; Subramanian S.; Sycamore N.; Tracey A.; Tromans A.; Van Helmond Z.; Wall M.; Wallis J.M.; White S.; Whitehead S.L.; Wilkinson J.E.; Willey D.L.; Williams H.; Wilming L.; Wray P.W.; Wu Z.; Coulson A.; Vaudin M.; Sulston J.E.; Durbin R.M.; Hubbard T.; Wooster R.; Dunham I.; Carter N.P.; McVean G.; Ross M.T.; Harrow J.; Olson M.V.; Beck S.; Rogers J.; Bentley D.R.;
Nature 441:315-321(2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT HIS-402; Strong association of the Y402H variant in complement factor H at 1q32 with susceptibility to age-related macular degeneration.
Zareparsi S.; Branham K.E.H.; Li M.; Shah S.; Klein R.J.; Ott J.; Hoh J.; Abecasis G.R.; Swaroop A.;
Am. J. Hum. Genet. 77:149-153(2005)
Cited for: VARIANT HIS-402; A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration.
Hageman G.S.; Anderson D.H.; Johnson L.V.; Hancox L.S.; Taiber A.J.; Hardisty L.I.; Hageman J.L.; Stockman H.A.; Borchardt J.D.; Gehrs K.M.; Smith R.J.H.; Silvestri G.; Russell S.R.; Klaver C.C.W.; Barbazetto I.; Chang S.; Yannuzzi L.A.; Barile G.R.; Merriam J.C.; Smith R.T.; Olsh A.K.; Bergeron J.; Zernant J.; Merriam J.E.; Gold B.; Dean M.; Allikmets R.;
Proc. Natl. Acad. Sci. U.S.A. 102:7227-7232(2005)
Cited for: VARIANTS ILE-62 AND HIS-402; ASSOCIATION WITH ARMD; Complement factor H polymorphism in age-related macular degeneration.
Klein R.J.; Zeiss C.; Chew E.Y.; Tsai J.-Y.; Sackler R.S.; Haynes C.; Henning A.K.; SanGiovanni J.P.; Mane S.M.; Mayne S.T.; Bracken M.B.; Ferris F.L.; Ott J.; Barnstable C.; Hoh J.;
Science 308:385-389(2005)
Cited for: ASSOCIATION OF VARIANT HIS-402 WITH ARMD; Complement factor H variant increases the risk of age-related macular degeneration.
Haines J.L.; Hauser M.A.; Schmidt S.; Scott W.K.; Olson L.M.; Gallins P.; Spencer K.L.; Kwan S.Y.; Noureddine M.; Gilbert J.R.; Schnetz-Boutaud N.; Agarwal A.; Postel E.A.; Pericak-Vance M.A.;
Science 308:419-421(2005)
Cited for: ASSOCIATION OF VARIANT HIS-402 WITH ARMD; Complement factor H polymorphism and age-related macular degeneration.
Edwards A.O.; Ritter R. III; Abel K.J.; Manning A.; Panhuysen C.; Farrer L.A.;
Science 308:421-424(2005)
Cited for: ASSOCIATION OF VARIANT HIS-402 WITH ARMD; Basal laminar drusen caused by compound heterozygous variants in the CFH gene.
Boon C.J.F.; Klevering B.J.; Hoyng C.B.; Zonneveld-Vrieling M.N.; Nabuurs S.B.; Blokland E.; Cremers F.P.M.; den Hollander A.I.;
Am. J. Hum. Genet. 82:516-523(2008)
Cited for: INVOLVEMENT IN BASAL LAMINAR DRUSEN; VARIANTS HIS-402; GLY-567; ASP-936; TYR-1050 AND SER-1078;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.