[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1073/pnas.191360198; PubMed=11535825 [NCBI, ExPASy, EBI, Israel, Japan] Xu X.-Z.S., Moebius F., Gill D.L., Montell C.; "Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform."; Proc. Natl. Acad. Sci. U.S.A. 98:10692-10697(2001).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY. DOI=10.1016/S0092-8674(02)00719-5; PubMed=12015988 [NCBI, ExPASy, EBI, Israel, Japan] Launay P., Fleig A., Perraud A.-L., Scharenberg A.M., Penner R., Kinet J.-P.; "TRPM4 is a Ca2+-activated nonselective cation channel mediating cell membrane depolarization."; Cell 109:397-407(2002).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). DOI=10.1016/S0960-9822(03)00431-7; PubMed=12842017 [NCBI, ExPASy, EBI, Israel, Japan] Hofmann T., Chubanov V., Gudermann T., Montell C.; "TRPM5 is a voltage-modulated and Ca(2+)-activated monovalent selective cation channel."; Curr. Biol. 13:1153-1158(2003).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. TISSUE=Prostate; DOI=10.1074/jbc.M305127200; PubMed=12799367 [NCBI, ExPASy, EBI, Israel, Japan] Nilius B., Prenen J., Droogmans G., Voets T., Vennekens R., Freichel M., Wissenbach U., Flockerzi V.; "Voltage dependence of the Ca2+-activated cation channel TRPM4."; J. Biol. Chem. 278:30813-30820(2003).
[5]	ERRATUM. Nilius B., Prenen J., Droogmans G., Voets T., Vennekens R., Freichel M., Wissenbach U., Flockerzi V.; J. Biol. Chem. 278:42728-42728(2003).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-1214. DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[7]	FUNCTION, AND TISSUE SPECIFICITY. DOI=10.1161/01.RES.0000147311.54833.03; PubMed=15472118 [NCBI, ExPASy, EBI, Israel, Japan] Earley S., Waldron B.J., Brayden J.E.; "Critical role for transient receptor potential channel TRPM4 in myogenic constriction of cerebral arteries."; Circ. Res. 95:922-929(2004).
[8]	FUNCTION. DOI=10.1113/jphysiol.2004.063974; PubMed=15121803 [NCBI, ExPASy, EBI, Israel, Japan] Guinamard R., Chatelier A., Demion M., Potreau D., Patri S., Rahmati M., Bois P.; "Functional characterization of a Ca(2+)-activated non-selective cation channel in human atrial cardiomyocytes."; J. Physiol. (Lond.) 558:75-83(2004).
[9]	ENZYME REGULATION. DOI=10.1113/jphysiol.2004.070839; PubMed=15331675 [NCBI, ExPASy, EBI, Israel, Japan] Nilius B., Prenen J., Janssens A., Voets T., Droogmans G.; "Decavanadate modulates gating of TRPM4 cation channels."; J. Physiol. (Lond.) 560:753-765(2004).
[10]	ATP-BINDING, AND ENZYME REGULATION. DOI=10.1007/s00424-003-1221-x; PubMed=14758478 [NCBI, ExPASy, EBI, Israel, Japan] Nilius B., Prenen J., Voets T., Droogmans G.; "Intracellular nucleotides and polyamines inhibit the Ca2+-activated cation channel TRPM4b."; Pflugers Arch. 448:70-75(2004).
[11]	FUNCTION. DOI=10.1126/science.1098845; PubMed=15550671 [NCBI, ExPASy, EBI, Israel, Japan] Launay P., Cheng H., Srivatsan S., Penner R., Fleig A., Kinet J.-P.; "TRPM4 regulates calcium oscillations after T cell activation."; Science 306:1374-1377(2004).
[12]	PHOSPHORYLATION AT SER-1145 AND SER-1152, ATP-BINDING, CALMUDULIN-BINDING, AND MUTAGENESIS OF LEU-275; ILE-278; ASP-279; GLY-324; GLY-325; ARG-327; SER-1145 AND SER-1152. DOI=10.1074/jbc.M411089200; PubMed=15590641 [NCBI, ExPASy, EBI, Israel, Japan] Nilius B., Prenen J., Tang J., Wang C., Owsianik G., Janssens A., Voets T., Zhu M.X.; "Regulation of the Ca2+ sensitivity of the nonselective cation channel TRPM4."; J. Biol. Chem. 280:6423-6433(2005).
[13]	SELECTIVITY FILTER MOTIF, AND MUTAGENESIS OF GLN-977; GLU-981; 981-GLU--ALA-986; ASP-982 AND ASP-984. DOI=10.1074/jbc.M501686200; PubMed=15845551 [NCBI, ExPASy, EBI, Israel, Japan] Nilius B., Prenen J., Janssens A., Owsianik G., Wang C., Zhu M.X., Voets T.; "The selectivity filter of the cation channel TRPM4."; J. Biol. Chem. 280:22899-22906(2005).
[14]	ENZYME REGULATION, AND PIP2-BINDING. DOI=10.1074/jbc.M506965200; PubMed=16186107 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Okawa H., Wang Y., Liman E.R.; "Phosphatidylinositol 4,5-bisphosphate rescues TRPM4 channels from desensitization."; J. Biol. Chem. 280:39185-39192(2005).
[15]	FUNCTION. DOI=10.1016/j.ceca.2006.04.032; PubMed=16806463 [NCBI, ExPASy, EBI, Israel, Japan] Cheng H., Beck A., Launay P., Gross S.A., Stokes A.J., Kinet J.-P., Fleig A., Penner R.; "TRPM4 controls insulin secretion in pancreatic beta-cells."; Cell Calcium 41:51-61(2007).
[16]	ENZYME REGULATION, PIP2-BINDING, AND MUTAGENESIS OF LYS-1059; ARG-1072 AND 1136-ARG--ARG-1141. DOI=10.1038/sj.emboj.7600963; PubMed=16424899 [NCBI, ExPASy, EBI, Israel, Japan] Nilius B., Mahieu F., Prenen J., Janssens A., Owsianik G., Vennekens R., Voets T.; "The Ca2+-activated cation channel TRPM4 is regulated by phosphatidylinositol 4,5-biphosphate."; EMBO J. 25:467-478(2006).
[17]	TISSUE SPECIFICITY. DOI=10.1080/10799890600637506; PubMed=16777713 [NCBI, ExPASy, EBI, Israel, Japan] Fonfria E., Murdock P.R., Cusdin F.S., Benham C.D., Kelsell R.E., McNulty S.; "Tissue distribution profiles of the human TRPM cation channel family."; J. Recept. Signal Transduct. 26:159-178(2006).
[18]	ENZYME REGULATION. DOI=10.1124/mol.105.021154; PubMed=16407466 [NCBI, ExPASy, EBI, Israel, Japan] Takezawa R., Cheng H., Beck A., Ishikawa J., Launay P., Kubota H., Kinet J.-P., Fleig A., Yamada T., Penner R.; "A pyrazole derivative potently inhibits lymphocyte Ca2+ influx and cytokine production by facilitating transient receptor potential melastatin 4 channel activity."; Mol. Pharmacol. 69:1413-1420(2006).

Comments

FUNCTION: Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca(2+), it is impermeable to it. Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca(2+) oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca(2+) overload.
ENZYME REGULATION: Gating is voltage-dependent and repressed by decavanadate. Calmodulin-binding confers the Ca(2+) sensitivity. ATP is able to restore Ca(2+) sensitivity after desensitization. Phosphatidylinositol 4,5-biphosphate (PIP2)-binding strongly enhances activity, by increasing the channel's Ca(2+) sensitivity and shifting its voltage dependence of activation towards negative potentials. Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole derivative (BTP2).
SUBUNIT: Homomultimer.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	TRPM4b
Isoform ID	Q8TD43-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	TRPM4a
Isoform ID	Q8TD43-2
Features which should be applied to build the isoform sequence: VSP_021442.

Name	3
Synonyms	TRPM4c
Isoform ID	Q8TD43-3
Features which should be applied to build the isoform sequence: VSP_021443.

TISSUE SPECIFICITY: Widely expressed with a high expression in intestine and prostaste. In brain, it is both expressed in whole cerebral arteries and isolated vascular smooth muscle cells.
PTM: Phosphorylation by PKC leads to increase the sensitivity to Ca(2+).
SIMILARITY: Belongs to the transient receptor family. LTrpC subfamily.
SEQUENCE CAUTION:
- Sequence=BAA90907.1; Type=Erroneous termination; Positions=1191; Note=Translated as Glu

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY046396; AAL02142.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF497623; AAM18083.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY297044; AAP44473.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY297045; AAP44474.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY297046; AAP44475.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ575813; CAE05941.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000048; BAA90907.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00294933; -.
IPI00385243; -.
IPI00644607; -.

RefSeq

NP_060106.2; -.

UniGene

Hs.467101

3D structure databases

ModBase

Q8TD43.

Protein family/group databases

TCDB

1.A.4.5.4; transient receptor potential Ca2+ channel (TRP-CC) family.

PTM databases

PhosphoSite

Q8TD43; -.

Organism-specific databases

GC19P054352; -.

HIX0015320; -.

HGNC:17993; TRPM4.

606936; gene. [NCBI / EBI]

PharmGKB

PA38272; -.

Gene expression databases

Q8TD43; -.

Q8TD43; -.

HS_TRPM4; -.

ENSG00000130529; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005516;	Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006955;	Biological process: immune response (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005821; Ion_trans.
Graphical view of domain structure.

Pfam

PF00520; Ion_trans; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

Q8TD43; -.

Genome annotation databases

Ensembl

ENSG00000130529; Homo sapiens. [Contig view]

GeneID

54795; -.

KEGG

hsa:54795; -.

NMPDR

fig|9606.3.peg.16866; -.

Phylogenomic databases

HOVERGEN

Q8TD43; -.

Other

57471; -.

TRPM4; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; ATP-binding; Calcium; Calmodulin-binding; Cell membrane; Coiled coil; Immune response; Ion transport; Ionic channel; Membrane; Nucleotide-binding; Phosphoprotein; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1214`	`1214`	`Transient receptor potential cation channel subfamily M member 4.`	`PRO_0000259529`
`TOPO_DOM`	`1 683`	`683`	`Cytoplasmic (Potential).`
`TRANSMEM`	`684 704`	`21`	`Potential.`
`TOPO_DOM`	`705 776`	`72`	`Extracellular (Potential).`
`TRANSMEM`	`777 797`	`21`	`Potential.`
`TOPO_DOM`	`798 868`	`71`	`Cytoplasmic (Potential).`
`TRANSMEM`	`869 889`	`21`	`Potential.`
`TOPO_DOM`	`890 892`	`3`	`Extracellular (Potential).`
`TRANSMEM`	`893 913`	`21`	`Potential.`
`TOPO_DOM`	`914 929`	`16`	`Cytoplasmic (Potential).`
`TRANSMEM`	`930 950`	`21`	`Potential.`
`TOPO_DOM`	`951 965`	`15`	`Extracellular (Potential).`
`TOPO_DOM`	`966 993`	`28`	`Pore forming (Potential).`
`TOPO_DOM`	`994 1019`	`26`	`Extracellular (Potential).`
`TRANSMEM`	`1020 1040`	`21`	`Potential.`
`TOPO_DOM`	`1041 1214`	`174`	`Cytoplasmic (Potential).`
`REGION`	`1076 1176`	`101`	`Calmodulin-binding.`
`REGION`	`1136 1141`	`6`	`Mediates modulation by decavanadate and PIP2-binding.`
`COILED`	`1134 1187`	`54`	`Potential.`
`MOTIF`	`981 986`	`6`	`Selectivity filter.`
`MOD_RES`	`1145 1145`		`Phosphoserine; by PKC (Probable).`
`MOD_RES`	`1152 1152`		`Phosphoserine; by PKC (Probable).`
`VAR_SEQ`	`1 174`		`Missing (in isoform 2).`	`VSP_021442`
`VAR_SEQ`	`738 882`		`Missing (in isoform 3).`	`VSP_021443`
`MUTAGEN`	`275 275`		`L->A,C: Abolishes ability to restore sensitivity to Ca(2+) after desensitization.`
`MUTAGEN`	`278 278`		`I->N: No effect.`
`MUTAGEN`	`279 279`		`D->N: No effect.`
`MUTAGEN`	`324 324`		`G->A: No effect.`
`MUTAGEN`	`325 325`		`G->A: Abolishes ability to restore sensitivity to Ca(2+) after desensitization.`
`MUTAGEN`	`327 327`		`R->A: No effect.`
`MUTAGEN`	`977 977`		`Q->E: Alters the monovalent cation permeability sequence and results in a pore with moderate Ca(2+) permeability.`
`MUTAGEN`	`981 986`		`EDMDVA->TIIDGP: Induces a functional channel that combines the gating hallmarks of TRPM4 (activation by Ca(2+)) with TRPV6-like sensitivity to block by extracellular Ca(2+) and Mg(2+) as well as Ca(2+) permeation.`
`MUTAGEN`	`981 981`		`E->A: Results in a channel with normal permeability properties but with a reduced sensitivity to block by intracellular spermine.`
`MUTAGEN`	`982 982`		`D->A: Results in a functional channel that exhibits extremely fast desensitization, possibly indicating destabilization of the pore.`
`MUTAGEN`	`984 984`		`D->A: Results in a non-functional channel with a dominant negative phenotype.`
`MUTAGEN`	`1059 1059`		`K->Q: Does not affect PIP2-binding.`
`MUTAGEN`	`1072 1072`		`R->Q: Does not affect PIP2-binding.`
`MUTAGEN`	`1136 1141`		`Missing: Results in a channel with very rapid desensitization and highly reduced sensitivity to PIP2.`
`MUTAGEN`	`1145 1145`		`S->A: Decreases the sensitivity to Ca(2+).`
`MUTAGEN`	`1152 1152`		`S->A: Decreases the sensitivity to Ca(2+).`
`CONFLICT`	`1149 1149`		`K -> E (in Ref. 6; BAA90907).`
`CONFLICT`	`1207 1207`		`P -> L (in Ref. 6; BAA90907).`
`CONFLICT`	`1210 1210`		`P -> H (in Ref. 6; BAA90907).`
`CONFLICT`	`1214 1214`		`D -> E (in Ref. 6; BAA90907).`

Sequence information

Length: 1214 AA [This is the length of the unprocessed precursor]

Molecular weight: 134301 Da [This is the MW of the unprocessed precursor]

CRC64: 76ADA452690ED8F5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVVPEKEQSW IPKIFKKKTC TTFIVDSTDP GGTLCQCGRP RTAHPAVAME DAFGAAVVTV 

        70         80         90        100        110        120 
WDSDAHTTEK PTDAYGELDF TGAGRKHSNF LRLSDRTDPA AVYSLVTRTW GFRAPNLVVS 

       130        140        150        160        170        180 
VLGGSGGPVL QTWLQDLLRR GLVRAAQSTG AWIVTGGLHT GIGRHVGVAV RDHQMASTGG 

       190        200        210        220        230        240 
TKVVAMGVAP WGVVRNRDTL INPKGSFPAR YRWRGDPEDG VQFPLDYNYS AFFLVDDGTH 

       250        260        270        280        290        300 
GCLGGENRFR LRLESYISQQ KTGVGGTGID IPVLLLLIDG DEKMLTRIEN ATQAQLPCLL 

       310        320        330        340        350        360 
VAGSGGAADC LAETLEDTLA PGSGGARQGE ARDRIRRFFP KGDLEVLQAQ VERIMTRKEL 

       370        380        390        400        410        420 
LTVYSSEDGS EEFETIVLKA LVKACGSSEA SAYLDELRLA VAWNRVDIAQ SELFRGDIQW 

       430        440        450        460        470        480 
RSFHLEASLM DALLNDRPEF VRLLISHGLS LGHFLTPMRL AQLYSAAPSN SLIRNLLDQA 

       490        500        510        520        530        540 
SHSAGTKAPA LKGGAAELRP PDVGHVLRML LGKMCAPRYP SGGAWDPHPG QGFGESMYLL 

       550        560        570        580        590        600 
SDKATSPLSL DAGLGQAPWS DLLLWALLLN RAQMAMYFWE MGSNAVSSAL GACLLLRVMA 

       610        620        630        640        650        660 
RLEPDAEEAA RRKDLAFKFE GMGVDLFGEC YRSSEVRAAR LLLRRCPLWG DATCLQLAMQ 

       670        680        690        700        710        720 
ADARAFFAQD GVQSLLTQKW WGDMASTTPI WALVLAFFCP PLIYTRLITF RKSEEEPTRE 

       730        740        750        760        770        780 
ELEFDMDSVI NGEGPVGTAD PAEKTPLGVP RQSGRPGCCG GRCGGRRCLR RWFHFWGAPV 

       790        800        810        820        830        840 
TIFMGNVVSY LLFLLLFSRV LLVDFQPAPP GSLELLLYFW AFTLLCEELR QGLSGGGGSL 

       850        860        870        880        890        900 
ASGGPGPGHA SLSQRLRLYL ADSWNQCDLV ALTCFLLGVG CRLTPGLYHL GRTVLCIDFM 

       910        920        930        940        950        960 
VFTVRLLHIF TVNKQLGPKI VIVSKMMKDV FFFLFFLGVW LVAYGVATEG LLRPRDSDFP 

       970        980        990       1000       1010       1020 
SILRRVFYRP YLQIFGQIPQ EDMDVALMEH SNCSSEPGFW AHPPGAQAGT CVSQYANWLV 

      1030       1040       1050       1060       1070       1080 
VLLLVIFLLV ANILLVNLLI AMFSYTFGKV QGNSDLYWKA QRYRLIREFH SRPALAPPFI 

      1090       1100       1110       1120       1130       1140 
VISHLRLLLR QLCRRPRSPQ PSSPALEHFR VYLSKEAERK LLTWESVHKE NFLLARARDK 

      1150       1160       1170       1180       1190       1200 
RESDSERLKR TSQKVDLALK QLGHIREYEQ RLKVLEREVQ QCSRVLGWVA EALSRSALLP 

      1210 
PGGPPPPDLP GSKD

Q8TD43 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools