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Protein

Short transient receptor potential channel 5

Gene

TRPC5

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

Functioni

Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective (By similarity). May also be activated by intracellular calcium store depletion.By similarity1 Publication

Enzyme regulationi

Calcium channel activity is enhanced by MYLK, that promotes its subcellular localization at the plasma membrane.1 Publication

GO - Molecular functioni

  • calcium channel activity Source: UniProtKB
  • inositol 1,4,5 trisphosphate binding Source: GO_Central
  • store-operated calcium channel activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.
REACT_22228. Role of second messengers in netrin-1 signaling.

Protein family/group databases

TCDBi1.A.4.1.7. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Short transient receptor potential channel 5
Short name:
TrpC5
Alternative name(s):
Transient receptor protein 5
Short name:
TRP-5
Short name:
hTRP-5
Short name:
hTRP5
Gene namesi
Name:TRPC5
Synonyms:TRP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12337. TRPC5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 330330CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei331 – 35121HelicalSequence AnalysisAdd
BLAST
Topological domaini352 – 39847ExtracellularSequence AnalysisAdd
BLAST
Transmembranei399 – 41921HelicalSequence AnalysisAdd
BLAST
Topological domaini420 – 43718CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei438 – 45821HelicalSequence AnalysisAdd
BLAST
Topological domaini459 – 47012ExtracellularSequence AnalysisAdd
BLAST
Transmembranei471 – 49121HelicalSequence AnalysisAdd
BLAST
Topological domaini492 – 51221CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei513 – 53321HelicalSequence AnalysisAdd
BLAST
Topological domaini534 – 60370ExtracellularSequence AnalysisAdd
BLAST
Transmembranei604 – 62421HelicalSequence AnalysisAdd
BLAST
Topological domaini625 – 973349CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • calcium channel complex Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37010.

Polymorphism and mutation databases

BioMutaiTRPC5.
DMDMi10720321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 973973Short transient receptor potential channel 5PRO_0000215318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9UL62.
PaxDbiQ9UL62.
PRIDEiQ9UL62.

PTM databases

PhosphoSiteiQ9UL62.

Expressioni

Tissue specificityi

Expressed in brain with higher levels in fetal brain. Found in cerebellum and occipital pole.1 Publication

Gene expression databases

BgeeiQ9UL62.
CleanExiHS_TRPC5.
GenevestigatoriQ9UL62.

Organism-specific databases

HPAiHPA000510.

Interactioni

Subunit structurei

Interacts with TRPC4AP (By similarity). Homotetramer and heterotetramer with TRPC1 and/or TRPC4. Interacts with NHERF (By similarity). Interacts with MX1 and RNF24. Interacts (via C-terminus) with CABP1. Interacts with SESTD1 (via the spectrin 1 repeat).By similarity5 Publications

Protein-protein interaction databases

BioGridi113075. 17 interactions.
IntActiQ9UL62. 1 interaction.
STRINGi9606.ENSP00000262839.

Structurei

3D structure databases

ProteinModelPortaliQ9UL62.
SMRiQ9UL62. Positions 60-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati31 – 6030ANK 1Add
BLAST
Repeati69 – 9729ANK 2Add
BLAST
Repeati98 – 12427ANK 3Add
BLAST
Repeati141 – 17030ANK 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni971 – 9733Essential for binding to NHERF PDZ domainBy similarity

Sequence similaritiesi

Contains 4 ANK repeats.Curated

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG254238.
GeneTreeiENSGT00760000119180.
HOGENOMiHOG000020589.
HOVERGENiHBG068337.
InParanoidiQ9UL62.
KOiK04968.
OMAiHPRRSFS.
OrthoDBiEOG72G17P.
PhylomeDBiQ9UL62.
TreeFamiTF313147.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR005461. TRPC5_channel.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERiPTHR10117. PTHR10117. 1 hit.
PTHR10117:SF24. PTHR10117:SF24. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSiPR01097. TRNSRECEPTRP.
PR01646. TRPCHANNEL5.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UL62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ
60 70 80 90 100
ALQEAEIYYN VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL
110 120 130 140 150
LYAIRKEVVG AVELLLSYRR PSGEKQVPTL MMDTQFSEFT PDITPIMLAA
160 170 180 190 200
HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE CVSSSEVDSL RHSRSRLNIY
210 220 230 240 250
KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE YEELSQQCKL
260 270 280 290 300
FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE
310 320 330 340 350
FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI
360 370 380 390 400
SPRSNLGLFI KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP
410 420 430 440 450
TVVEWMILPW VLGFIWGEIK EMWDGGFTEY IHDWWNLMDF AMNSLYLATI
460 470 480 490 500
SLKIVAYVKY NGSRPREEWE MWHPTLIAEA LFAISNILSS LRLISLFTAN
510 520 530 540 550
SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF YYETRAIDEP
560 570 580 590 600
NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV
610 620 630 640 650
GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY
660 670 680 690 700
FDEGGTLPPP FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRRNLRSFT
710 720 730 740 750
ERNADSLIQN QHYQEVIRNL VKRYVAAMIR NSKTHEGLTE ENFKELKQDI
760 770 780 790 800
SSFRYEVLDL LGNRKHPRSF STSSTELSQR DDNNDGSGGA RAKSKSVSFN
810 820 830 840 850
LGCKKKTCHG PPLIRTMPRS SGAQGKSKAE SSSKRSFMGP SLKKLGLLFS
860 870 880 890 900
KFNGHMSEPS SEPMYTISDG IVQQHCMWQD IRYSQMEKGK AEACSQSEIN
910 920 930 940 950
LSEVELGEVQ GAAQSSECPL ACSSSLHCAS SICSSNSKLL DSSEDVFETW
960 970
GEACDLLMHK WGDGQEEQVT TRL
Length:973
Mass (Da):111,412
Last modified:May 1, 2000 - v1
Checksum:iFBC8CBF17BE42166
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti667 – 6671P → T Found in a patient with severe delayed speech, autism spectrum and Gilles de la Tourette disorders. 1 Publication
VAR_069415
Natural varianti702 – 7021R → H.
Corresponds to variant rs36047478 [ dbSNP | Ensembl ].
VAR_052369

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054568 mRNA. Translation: AAF00002.1.
AC005191 Genomic DNA. Translation: AAC24563.1.
AL049563, AC005191 Genomic DNA. Translation: CAI43017.1.
CH471120 Genomic DNA. Translation: EAX02630.1.
BC137271 mRNA. Translation: AAI37272.1.
BC137274 mRNA. Translation: AAI37275.1.
CCDSiCCDS14561.1.
RefSeqiNP_036603.1. NM_012471.2.
UniGeneiHs.657709.

Genome annotation databases

EnsembliENST00000262839; ENSP00000262839; ENSG00000072315.
GeneIDi7224.
KEGGihsa:7224.
UCSCiuc004epl.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054568 mRNA. Translation: AAF00002.1.
AC005191 Genomic DNA. Translation: AAC24563.1.
AL049563, AC005191 Genomic DNA. Translation: CAI43017.1.
CH471120 Genomic DNA. Translation: EAX02630.1.
BC137271 mRNA. Translation: AAI37272.1.
BC137274 mRNA. Translation: AAI37275.1.
CCDSiCCDS14561.1.
RefSeqiNP_036603.1. NM_012471.2.
UniGeneiHs.657709.

3D structure databases

ProteinModelPortaliQ9UL62.
SMRiQ9UL62. Positions 60-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113075. 17 interactions.
IntActiQ9UL62. 1 interaction.
STRINGi9606.ENSP00000262839.

Chemistry

ChEMBLiCHEMBL1250411.
GuidetoPHARMACOLOGYi490.

Protein family/group databases

TCDBi1.A.4.1.7. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteiQ9UL62.

Polymorphism and mutation databases

BioMutaiTRPC5.
DMDMi10720321.

Proteomic databases

MaxQBiQ9UL62.
PaxDbiQ9UL62.
PRIDEiQ9UL62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262839; ENSP00000262839; ENSG00000072315.
GeneIDi7224.
KEGGihsa:7224.
UCSCiuc004epl.1. human.

Organism-specific databases

CTDi7224.
GeneCardsiGC0XM111017.
HGNCiHGNC:12337. TRPC5.
HPAiHPA000510.
MIMi300334. gene.
neXtProtiNX_Q9UL62.
PharmGKBiPA37010.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG254238.
GeneTreeiENSGT00760000119180.
HOGENOMiHOG000020589.
HOVERGENiHBG068337.
InParanoidiQ9UL62.
KOiK04968.
OMAiHPRRSFS.
OrthoDBiEOG72G17P.
PhylomeDBiQ9UL62.
TreeFamiTF313147.

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.
REACT_22228. Role of second messengers in netrin-1 signaling.

Miscellaneous databases

ChiTaRSiTRPC5. human.
GeneWikiiTRPC5.
GenomeRNAii7224.
NextBioi28291.
PROiQ9UL62.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UL62.
CleanExiHS_TRPC5.
GenevestigatoriQ9UL62.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR005461. TRPC5_channel.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERiPTHR10117. PTHR10117. 1 hit.
PTHR10117:SF24. PTHR10117:SF24. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSiPR01097. TRNSRECEPTRP.
PR01646. TRPCHANNEL5.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca(2+) entry channel."
    Sossey-Alaoui K., Lyon J.A., Jones L., Abidi F.E., Hartung A.J., Hane B., Schwartz C.E., Stevenson R.E., Srivastava A.K.
    Genomics 60:330-340(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Brain.
  5. "A novel capacitative calcium entry channel expressed in excitable cells."
    Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M., Murakami M., Cavalie A., Flockerzi V.
    EMBO J. 17:4274-4282(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Subunit composition of mammalian transient receptor potential channels in living cells."
    Hofmann T., Schaefer M., Schultz G., Gudermann T.
    Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC."
    Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N., St-Hilaire M., Pinard M., Boulay G.
    J. Biol. Chem. 280:19393-19400(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MX1.
  8. "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes."
    Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.
    Pflugers Arch. 450:345-354(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CABP1.
  9. "Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells."
    Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M., Seto M., Sakurada K., Kiuchi Y., Mori Y.
    J. Physiol. (Lond.) 570:219-235(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS CALCIUM CHANNEL, ENZYME REGULATION, SUBCELLULAR LOCATION.
  10. "RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC."
    Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.
    Cell Calcium 43:432-443(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF24.
  11. "The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5."
    Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.
    J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SESTD1.
  12. Cited for: VARIANT THR-667.

Entry informationi

Entry nameiTRPC5_HUMAN
AccessioniPrimary (citable) accession number: Q9UL62
Secondary accession number(s): B2RP53
, O75233, Q5JXY8, Q9Y514
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: May 27, 2015
This is version 134 of the entry and version 1 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. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.