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Protein

Frizzled-5

Gene

FZD5

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

Functioni

Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Interacts specifically with Wnt5A to induce the beta-catenin pathway.1 Publication

GO - Molecular functioni

  • G-protein coupled receptor activity Source: GO_Central
  • protein kinase binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB
  • Wnt-activated receptor activity Source: BHF-UCL
  • Wnt-protein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_18372. Class B/2 (Secretin family receptors).
REACT_263982. Ca2+ pathway.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264378. RNF mutants show enhanced WNT signaling and proliferation.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264533. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
REACT_264580. regulation of FZD by ubiquitination.
SignaLinkiQ13467.

Protein family/group databases

MEROPSiI93.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-5
Short name:
Fz-5
Short name:
hFz5
Alternative name(s):
FzE5
Gene namesi
Name:FZD5
Synonyms:C2orf31
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4043. FZD5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 238212ExtracellularSequence AnalysisAdd
BLAST
Transmembranei239 – 25921Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini260 – 27011CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei271 – 29121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini292 – 31524ExtracellularSequence AnalysisAdd
BLAST
Transmembranei316 – 33621Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini337 – 35822CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei359 – 37921Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini380 – 40223ExtracellularSequence AnalysisAdd
BLAST
Transmembranei403 – 42321Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini424 – 44926CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei450 – 47021Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini471 – 50030ExtracellularSequence AnalysisAdd
BLAST
Transmembranei501 – 52121Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini522 – 58564CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28460.

Polymorphism and mutation databases

BioMutaiFZD5.
DMDMi116242481.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 585559Frizzled-5PRO_0000012990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 94PROSITE-ProRule annotation
Disulfide bondi41 ↔ 87PROSITE-ProRule annotation
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi78 ↔ 116PROSITE-ProRule annotation
Disulfide bondi105 ↔ 147PROSITE-ProRule annotation
Disulfide bondi109 ↔ 133PROSITE-ProRule annotation
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Ubiquitinated by RNF43 and ZNRF3, leading to its degradation by the proteasome.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13467.
PaxDbiQ13467.
PRIDEiQ13467.

PTM databases

PhosphoSiteiQ13467.

Expressioni

Gene expression databases

BgeeiQ13467.
CleanExiHS_FZD5.
GenevestigatoriQ13467.

Organism-specific databases

HPAiHPA052361.
HPA053811.

Interactioni

Subunit structurei

Interacts with GOPC.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SCYL2Q6P3W74EBI-3913027,EBI-1046810

Protein-protein interaction databases

BioGridi113609. 9 interactions.
IntActiQ13467. 11 interactions.
MINTiMINT-7005936.
STRINGi9606.ENSP00000354607.

Structurei

3D structure databases

ProteinModelPortaliQ13467.
SMRiQ13467. Positions 33-149, 197-536.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 150123FZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi525 – 5306Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity
Motifi583 – 5853PDZ-binding

Domaini

The PDZ-binding motif mediates interaction with GOPC.By similarity
Lys-Thr-X-X-X-Trp motif interacts with the PDZ doman of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.By similarity
The FZ domain is involved in binding with Wnt ligands.By similarity

Sequence similaritiesi

Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG257258.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233236.
HOVERGENiHBG006977.
InParanoidiQ13467.
KOiK02375.
OMAiAATYHKQ.
OrthoDBiEOG7M3J01.
PhylomeDBiQ13467.
TreeFamiTF317907.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026547. FZD5.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF29. PTHR11309:SF29. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARPDPSAPP SLLLLLLAQL VGRAAAASKA PVCQEITVPM CRGIGYNLTH
60 70 80 90 100
MPNQFNHDTQ DEAGLEVHQF WPLVEIQCSP DLRFFLCSMY TPICLPDYHK
110 120 130 140 150
PLPPCRSVCE RAKAGCSPLM RQYGFAWPER MSCDRLPVLG RDAEVLCMDY
160 170 180 190 200
NRSEATTAPP RPFPAKPTLP GPPGAPASGG ECPAGGPFVC KCREPFVPIL
210 220 230 240 250
KESHPLYNKV RTGQVPNCAV PCYQPSFSAD ERTFATFWIG LWSVLCFIST
260 270 280 290 300
STTVATFLID MERFRYPERP IIFLSACYLC VSLGFLVRLV VGHASVACSR
310 320 330 340 350
EHNHIHYETT GPALCTIVFL LVYFFGMASS IWWVILSLTW FLAAGMKWGN
360 370 380 390 400
EAIAGYAQYF HLAAWLIPSV KSITALALSS VDGDPVAGIC YVGNQNLNSL
410 420 430 440 450
RGFVLGPLVL YLLVGTLFLL AGFVSLFRIR SVIKQGGTKT DKLEKLMIRI
460 470 480 490 500
GIFTLLYTVP ASIVVACYLY EQHYRESWEA ALTCACPGHD TGQPRAKPEY
510 520 530 540 550
WVLMLKYFMC LVVGITSGVW IWSGKTVESW RRFTSRCCCR PRRGHKSGGA
560 570 580
MAAGDYPEAS AALTGRTGPP GPAATYHKQV SLSHV
Length:585
Mass (Da):64,507
Last modified:October 17, 2006 - v2
Checksum:iAC3AB2CD912C1B0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881S → T in AAC50385 (PubMed:8626800).Curated
Sequence conflicti262 – 2632ER → DT in AAC50385 (PubMed:8626800).Curated
Sequence conflicti345 – 3451G → A in AAC50385 (PubMed:8626800).Curated
Sequence conflicti357 – 3571A → G in AAC50385 (PubMed:8626800).Curated
Sequence conflicti384 – 3841D → G in BAF83075 (PubMed:15815621).Curated
Sequence conflicti402 – 4021G → R in AAC50385 (PubMed:8626800).Curated
Sequence conflicti504 – 5041M → V in BAG37738 (PubMed:15815621).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti216 – 2161P → L.
Corresponds to variant rs35994626 [ dbSNP | Ensembl ].
VAR_049291

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43318 mRNA. Translation: AAC50385.1.
AB043702 mRNA. Translation: BAB60959.1.
AK290386 mRNA. Translation: BAF83075.1.
AK315338 mRNA. Translation: BAG37738.1.
AC096772 Genomic DNA. Translation: AAY24058.1.
CCDSiCCDS33366.1.
RefSeqiNP_003459.2. NM_003468.3.
UniGeneiHs.17631.

Genome annotation databases

EnsembliENST00000295417; ENSP00000354607; ENSG00000163251.
GeneIDi7855.
KEGGihsa:7855.
UCSCiuc002vcj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43318 mRNA. Translation: AAC50385.1.
AB043702 mRNA. Translation: BAB60959.1.
AK290386 mRNA. Translation: BAF83075.1.
AK315338 mRNA. Translation: BAG37738.1.
AC096772 Genomic DNA. Translation: AAY24058.1.
CCDSiCCDS33366.1.
RefSeqiNP_003459.2. NM_003468.3.
UniGeneiHs.17631.

3D structure databases

ProteinModelPortaliQ13467.
SMRiQ13467. Positions 33-149, 197-536.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113609. 9 interactions.
IntActiQ13467. 11 interactions.
MINTiMINT-7005936.
STRINGi9606.ENSP00000354607.

Protein family/group databases

MEROPSiI93.001.
GPCRDBiSearch...

PTM databases

PhosphoSiteiQ13467.

Polymorphism and mutation databases

BioMutaiFZD5.
DMDMi116242481.

Proteomic databases

MaxQBiQ13467.
PaxDbiQ13467.
PRIDEiQ13467.

Protocols and materials databases

DNASUi7855.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295417; ENSP00000354607; ENSG00000163251.
GeneIDi7855.
KEGGihsa:7855.
UCSCiuc002vcj.3. human.

Organism-specific databases

CTDi7855.
GeneCardsiGC02M208628.
HGNCiHGNC:4043. FZD5.
HPAiHPA052361.
HPA053811.
MIMi601723. gene.
neXtProtiNX_Q13467.
PharmGKBiPA28460.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG257258.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233236.
HOVERGENiHBG006977.
InParanoidiQ13467.
KOiK02375.
OMAiAATYHKQ.
OrthoDBiEOG7M3J01.
PhylomeDBiQ13467.
TreeFamiTF317907.

Enzyme and pathway databases

ReactomeiREACT_18372. Class B/2 (Secretin family receptors).
REACT_263982. Ca2+ pathway.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264378. RNF mutants show enhanced WNT signaling and proliferation.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264533. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
REACT_264580. regulation of FZD by ubiquitination.
SignaLinkiQ13467.

Miscellaneous databases

ChiTaRSiFZD5. human.
GeneWikiiFZD5.
GenomeRNAii7855.
NextBioi30293.
PROiQ13467.
SOURCEiSearch...

Gene expression databases

BgeeiQ13467.
CleanExiHS_FZD5.
GenevestigatoriQ13467.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026547. FZD5.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF29. PTHR11309:SF29. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A large family of putative transmembrane receptors homologous to the product of the Drosophila tissue polarity gene frizzled."
    Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.
    J. Biol. Chem. 271:4468-4476(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "Molecular cloning and characterization of human Frizzled-5 gene on chromosome 2q33.3-q34 region."
    Saitoh T., Hirai M., Katoh M.
    Int. J. Oncol. 19:105-110(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
    , 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: Spleen and Umbilical cord blood.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "A novel frizzled gene identified in human esophageal carcinoma mediates APC/beta-catenin signals."
    Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.
    Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 273-331.
    Tissue: Esophageal carcinoma.
  6. "A member of the Frizzled protein family mediating axis induction by Wnt-5A."
    He X., Saint-Jeannet J.P., Wang Y., Nathans J., Dawid I., Varmus H.
    Science 275:1652-1654(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: COUPLING TO BETA-CATENIN PATHWAY.
  7. "Biochemical characterization of Wnt-frizzled interactions using a soluble, biologically active vertebrate Wnt protein."
    Hsieh J.C., Rattner A., Smallwood P.M., Nathans J.
    Proc. Natl. Acad. Sci. U.S.A. 96:3546-3551(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: UBIQUITINATION BY ZNRF3.
  9. "Tumour suppressor RNF43 is a stem-cell E3 ligase that induces endocytosis of Wnt receptors."
    Koo B.K., Spit M., Jordens I., Low T.Y., Stange D.E., van de Wetering M., van Es J.H., Mohammed S., Heck A.J., Maurice M.M., Clevers H.
    Nature 488:665-669(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY RNF43.

Entry informationi

Entry nameiFZD5_HUMAN
AccessioniPrimary (citable) accession number: Q13467
Secondary accession number(s): A8K2X1, B2RCZ1, Q53R22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 148 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.