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Protocadherin Fat 3 (hFat3) (Cadherin family member 15) (FAT tumor suppressor homolog 3)

 FAT3_HUMAN              Reviewed;        4557 AA.
Q8TDW7; B5MDB0; Q96AU6;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
12-SEP-2018, sequence version 3.
13-FEB-2019, entry version 133.
RecName: Full=Protocadherin Fat 3;
Short=hFat3;
AltName: Full=Cadherin family member 15;
AltName: Full=FAT tumor suppressor homolog 3;
Flags: Precursor;
Name=FAT3; Synonyms=CDHF15, KIAA1989;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1026-4557 (ISOFORM 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 3493-4557 (ISOFORM 3), AND VARIANT
GLY-3812.
TISSUE=Brain;
PubMed=11811999; DOI=10.1006/bbrc.2002.6338;
Mitsui K., Nakajima D., Ohara O., Nakayama M.;
"Mammalian fat3: a large protein that contains multiple cadherin and
EGF-like motifs.";
Biochem. Biophys. Res. Commun. 290:1260-1266(2002).
[4]
IDENTIFICATION, AND TISSUE SPECIFICITY.
PubMed=16865240;
Katoh Y., Katoh M.;
"Comparative integromics on FAT1, FAT2, FAT3 and FAT4.";
Int. J. Mol. Med. 18:523-528(2006).
-!- FUNCTION: May play a role in the interactions between neurites
derived from specific subsets of neurons during development.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8TDW7-3; Sequence=Displayed;
Name=3;
IsoId=Q8TDW7-1; Sequence=VSP_059739;
Name=2;
IsoId=Q8TDW7-2; Sequence=VSP_059761;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in ES cells, primitive
neuroectoderm, fetal brain, infant brain, adult neural tissues and
prostate. {ECO:0000269|PubMed:16865240}.
-!- SEQUENCE CAUTION:
Sequence=AAH16722.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AP000722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016722; AAH16722.1; ALT_INIT; mRNA.
EMBL; AB076400; BAB86868.1; -; mRNA.
RefSeq; NP_001008781.2; NM_001008781.2. [Q8TDW7-3]
RefSeq; XP_016872670.1; XM_017017181.1. [Q8TDW7-1]
RefSeq; XP_016872672.1; XM_017017183.1. [Q8TDW7-3]
UniGene; Hs.98523; -.
ProteinModelPortal; Q8TDW7; -.
SMR; Q8TDW7; -.
BioGrid; 125669; 36.
STRING; 9606.ENSP00000298047; -.
iPTMnet; Q8TDW7; -.
PhosphoSitePlus; Q8TDW7; -.
BioMuta; FAT3; -.
DMDM; 172045818; -.
EPD; Q8TDW7; -.
jPOST; Q8TDW7; -.
PaxDb; Q8TDW7; -.
PeptideAtlas; Q8TDW7; -.
PRIDE; Q8TDW7; -.
ProteomicsDB; 74356; -.
ProteomicsDB; 74357; -. [Q8TDW7-2]
ProteomicsDB; 74358; -. [Q8TDW7-3]
Ensembl; ENST00000409404; ENSP00000387040; ENSG00000165323. [Q8TDW7-3]
Ensembl; ENST00000634703; ENSP00000489369; ENSG00000282908. [Q8TDW7-3]
GeneID; 120114; -.
KEGG; hsa:120114; -.
UCSC; uc001pdj.5; human. [Q8TDW7-3]
CTD; 120114; -.
DisGeNET; 120114; -.
EuPathDB; HostDB:ENSG00000165323.15; -.
GeneCards; FAT3; -.
HGNC; HGNC:23112; FAT3.
HPA; HPA026878; -.
MIM; 612483; gene.
neXtProt; NX_Q8TDW7; -.
OpenTargets; ENSG00000165323; -.
PharmGKB; PA134962612; -.
eggNOG; KOG1219; Eukaryota.
eggNOG; ENOG410XPEI; LUCA.
GeneTree; ENSGT00940000154981; -.
HOGENOM; HOG000046499; -.
HOVERGEN; HBG005641; -.
InParanoid; Q8TDW7; -.
KO; K16506; -.
OMA; GHLVTQV; -.
OrthoDB; 12779at2759; -.
PhylomeDB; Q8TDW7; -.
TreeFam; TF316403; -.
ChiTaRS; FAT3; human.
GenomeRNAi; 120114; -.
PRO; PR:Q8TDW7; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000165323; Expressed in 150 organ(s), highest expression level in primary visual cortex.
ExpressionAtlas; Q8TDW7; baseline and differential.
Genevisible; Q8TDW7; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
InterPro; IPR002126; Cadherin-like_dom.
InterPro; IPR015919; Cadherin-like_sf.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR001791; Laminin_G.
Pfam; PF00028; Cadherin; 26.
Pfam; PF02210; Laminin_G_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 32.
SMART; SM00181; EGF; 4.
SMART; SM00179; EGF_CA; 3.
SMART; SM00282; LamG; 1.
SUPFAM; SSF49313; SSF49313; 34.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00232; CADHERIN_1; 19.
PROSITE; PS50268; CADHERIN_2; 32.
PROSITE; PS00022; EGF_1; 3.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 1.
2: Evidence at transcript level;
Alternative splicing; Calcium; Cell adhesion; Complete proteome;
Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
Membrane; Methylation; Polymorphism; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 4557 Protocadherin Fat 3.
/FTId=PRO_0000324634.
TOPO_DOM 33 4154 Extracellular. {ECO:0000255}.
TRANSMEM 4155 4175 Helical. {ECO:0000255}.
TOPO_DOM 4176 4557 Cytoplasmic. {ECO:0000255}.
DOMAIN 44 158 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 159 266 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 264 375 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 377 472 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 473 578 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 579 681 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 727 831 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 832 936 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 937 1043 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1044 1148 Cadherin 10. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1149 1254 Cadherin 11. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1255 1359 Cadherin 12. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1363 1460 Cadherin 13. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1461 1566 Cadherin 14. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1567 1769 Cadherin 15. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1770 1883 Cadherin 16. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1884 1986 Cadherin 17. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1983 2084 Cadherin 18. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2085 2186 Cadherin 19. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2187 2287 Cadherin 20. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2288 2394 Cadherin 21. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2395 2496 Cadherin 22. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2497 2600 Cadherin 23. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2601 2708 Cadherin 24. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2709 2814 Cadherin 25. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2815 2924 Cadherin 26. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2925 3029 Cadherin 27. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3030 3131 Cadherin 28. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3132 3236 Cadherin 29. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3237 3341 Cadherin 30. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3342 3446 Cadherin 31. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3447 3551 Cadherin 32. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3552 3653 Cadherin 33. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3795 3833 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3835 4018 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 4021 4058 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4060 4096 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4098 4134 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
COMPBIAS 4406 4477 Pro-rich.
MOD_RES 4510 4510 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8BNA6}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 800 800 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 880 880 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 899 899 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1007 1007 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1368 1368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1430 1430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1752 1752 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1945 1945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1994 1994 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1997 1997 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2209 2209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2293 2293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2332 2332 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2468 2468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3001 3001 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3202 3202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3330 3330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3450 3450 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3619 3619 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3742 3742 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3927 3927 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 3799 3810 {ECO:0000250}.
DISULFID 3804 3822 {ECO:0000250}.
DISULFID 3824 3832 {ECO:0000250}.
DISULFID 3985 4018 {ECO:0000250}.
DISULFID 4025 4036 {ECO:0000250}.
DISULFID 4030 4046 {ECO:0000250}.
DISULFID 4048 4057 {ECO:0000250}.
DISULFID 4064 4075 {ECO:0000250}.
DISULFID 4069 4084 {ECO:0000250}.
DISULFID 4086 4095 {ECO:0000250}.
DISULFID 4102 4113 {ECO:0000250}.
DISULFID 4107 4122 {ECO:0000250}.
DISULFID 4124 4133 {ECO:0000250}.
VAR_SEQ 1204 4557 LITTTSRKLDREQQAEHFLEVTVTDGGPSPKQSTIWVVVQV
LDENDNKPQFPEKVYQIKLPERDRKKRGEPIYRAFAFDRDE
GPNAEISYSIVDGNDDGKFFIDPKTGMVSSRKQFTAGSYDI
LTIKAVDNGRPQKSSTARLHIEWIKKPPPSPIPLTFDEPFY
NFTVMESDRVTEIVGVVSVQPANTPLWFDIVGGNFDSAFDA
EKGVGTIVIAKPLDAEQRSIYNMSVEVTDGTNVAVTQVFIK
VLDNNDNGPEFSQPNYDVTISEDVLPDTEILQIEATDRDEK
HKLSYTVHSSIDSISMRKFRIDPSTGVLYTAERLDHEAQDK
HILNIMVRDQEFPYRRNLARVIVNVEDANDHSPYFTNPLYE
ASVFESAALGSAVLQVTALDKDKGENAELIYTIEAGNTGNM
FKIEPVLGIITICKEPDMTTMGQFVLSIKVTDQGSPPMSAT
AIVRISVTMSDNSHPKFIHKDYQAEVNENVDIGTSVILISA
ISQSTLIYEVKDGDINGIFTINPYSGVITTQKALDYERTSS
YQLIIQATNMAGMASNATVNIQIVDENDNAPVFLFSQYSGS
LSEAAPINSIVRSLDNSPLVIRATDADSNRNALLVYQIVES
TAKKFFTVDSSTGAIRTIANLDHETIAHFHFHVHVRDSGSP
QLTAESPVEVNIEVTDVNDNPPVFTQAVFETILLLPTYVGV
EVLKVSATDPDSEVPPELTYSLMEGSLDHFLIDSNSGVLTI
KNNNLSKDHYMLIVKVSDGKFYSTSMVTIMVKEAMDSGLHF
TQSFYSTSISENNTNITKVAIVNAVGNRLNEPLKYSILNPG
NKFKIKSTSGVIQTTGVPFDREEQELYELVVEASRELDHLR
VARVVVRVNIEDINDNSPVFVGLPYYAAVQVDAEPGTLIYQ
VTAIDKDKGPNGEVTYVLQDDYGHFEINPNSGNVILKEAFN
SDLSNIEYGVTILAKDGGKPSLSTSVELPITIVNKAMPVFD
KPFYTASVNEDIRMNTPILSINATSPEGQGIIYIIIDGDPF
KQFNIDFDTGVLKVVSPLDYEVTSAYKLTIRASDALTGARA
EVTVDLLVNDVNDNPPIFDQPTYNTTLSEASLIGTPVLQVV
SIDADSENNKMVHYQIVQDTYNSTDYFHIDSSSGLILTARM
LDHELVQHCTLKVRSIDSGFPSLSSEVLVHIYISDVNDNPP
VFNQLIYESYVSELAPRGHFVTCVQASDADSSDFDRLEYSI
LSGNDRTSFLMDSKSGVITLSNHRKQRMEPLYSLNVSVSDG
LFTSTAQVHIRVLGANLYSPAFSQSTYVAEVRENVAAGTKV
IHVRATDGDPGTYGQISYAIINDFAKDRFLIDSNGQVITTE
RLDRENPLEGDVSIFVRALDGGGRTTFCTVRVIVVDENDNA
PQFMTVEYRASVRADVGRGHLVTQVQAIDPDDGANSRITYS
LYSEASVSVADLLEIDPDNGWMVTKGNFNQLKNTVLSFFVK
AVDGGIPVKHSLIPVYIHVLPPETFLPSFTQSQYSFTIAED
TAIGSTVDTLRILPSQNVWFSTVNGERPENNKGGIFVIEQE
TGTIKLDKRLDRETSPAFHFKVAATIPLDKVDIVFTVDVDI
KVLDLNDNKPVFETSSYDTIIMEGMPVGTKLTQVRAIDMDW
GANGQVTYSLHSDSQPEKVMEAFNIDSNTGWISTLKDLDHE
TDPTFTFSVVASDLGEAFSLSSTALVSVRVTDINDNAPVFA
QEVYRGNVKESDPPGEVVAVLSTWDRDTSDVNRQVSYHITG
GNPRGRFALGLVQSEWKVYVKRPLDREEQDIYFLNITATDG
LFVTQAMVEVSVSDVNDNSPVCDQVAYTALLPEDIPSNKII
LKVSAKDADIGSNGYIRYSLYGSGNSEFFLDPESGELKTLA
LLDRERIPVYSLMAKATDGGGRFCQSNIHLILEDVNDNPPV
FSSDHYNTCVYENTATKALLTRVQAVDPDIGINRKVVYSLA
DSAGGVFSIDSSSGIIILEQPLDREQQSSYNISVRATDQSP
GQSLSSLTTVTITVLDINDNPPVFERRDYLVTVPEDTSPGT
QVLAVFATSKDIGTNAEITYLIRSGNEQGKFKINPKTGGIS
VSEVLDYELCKRFYLVVEAKDGGTPALSAVATVNINLTDVN
DNPPKFSQDVYSAVISEDALVGDSVILLIAEDVDSQPNGQI
HFSIVNGDRDNEFTVDPVLGLVKVKKKLDRERVSGYSLLVQ
AVDSGIPAMSSTATVNIDISDVNDNSPVFTPANYTAVIQEN
KPVGTSILQLVVTDRDSFHNGPPFSFSILSGNEEEEFVLDP
HGILRSAVVFQHTESLEYVLCVQAKDSGKPQQVSHTYIRVR
VIEESTHKPTAIPLEIFIVTMEDDFPGGVIGKIHATDQDMY
DVLTFALKSEQKSLFKVNSHDGKIIALGGLDSGKYVLNVSV
SDGRFQVPIDVVVHVEQLVHEMLQNTVTIRFENVSPEDFVG
LHMHGFRRTLRNAVLTQKQDSLRIISIQPVAGTNQLDMLFA
VEMHSSEFYKPAYLIQKLSNARRHLENIMRISAILEKNCSG
LDCQEQHCEQGLSLDSHALMTYSTARISFVCPRFYRNVRCT
CNGGLCPGSNDPCVEKPCPGDMQCVSYEASRRPFLCQCPPG
KLGECSGHTSLSFAGNSYIKYRLSENSKEEDFKLALRLRTL
QSNGIIMYTRANPCIILKIVDGKLWFQLDCGSGPGILGISG
RAVNDGSWHSVFLELNRNFTSLSLDDSYVERRRAPLYFQTL
STESSIYFGALVQADNIRSLTDTRVTQVLSGFQGCLDSVIL
NNNELPLQNKRSSFAEVVGLTELKLGCVLYPDACKRSPCQH
GGSCTGLPSGGYQCTCLSQFTGRNCESEITACFPNPCRNGG
SCDPIGNTFICNCKAGLTGVTCEEDINECEREECENGGSCV
NVFGSFLCNCTPGYVGQYCGLRPVVVPNIQAGHSYVGKEEL
IGIAVVLFVIFILVVLFIVFRKKVFRKNYSRNNITLVQDPA
TAALLNKSNGIPFRNLRGSGDGRNVYQEVGPPQVPVRPMAY
TPCFQSDSRSNLDKIVDGLGGEHQEMTTFHPESPRILTARR
GVVVCSVAPNLPAVSPCRSDCDSIRKNGWDAGTENKGVDDP
GEVTCFAGSNKGSNSEVQSLSSFQSDSGDDNAYHWDTSDWM
PGARLSDIEEVPNYENQDGGSAHQGSTRELESDYYLGGYDI
DSEYPPPHEEEFLSQDQLPPPLPEDFPDQYEALPPSQPVSL
ASTLSPDCRRRPQFHPSQYLPPHPFPNETDLVGPPASCEFS
TFAVSMNQGTEPTGPADSVSLSLHNSRGTSSSDVSANCGFD
DSEVAMSDYESVGELSLASLHIPFVETQHQTQV -> SCSV
AQAGMQWHDRSSLQSRTPGFKGYPCLSLLSSWDYRHAPPCP
ATFLNS (in isoform 2).
/FTId=VSP_059761.
VAR_SEQ 4350 4350 N -> NASIVTVIQLVNNVVDTIENEVSVMDQGQNYNR
(in isoform 3).
/FTId=VSP_059739.
VARIANT 412 412 S -> F (in dbSNP:rs10830902).
/FTId=VAR_039851.
VARIANT 462 462 I -> V (in dbSNP:rs16917409).
/FTId=VAR_039852.
VARIANT 1167 1167 V -> G (in dbSNP:rs11821058).
/FTId=VAR_039853.
VARIANT 1726 1726 Q -> R (in dbSNP:rs7949157).
/FTId=VAR_039854.
VARIANT 2293 2293 N -> S (in dbSNP:rs16918105).
/FTId=VAR_039855.
VARIANT 2622 2622 V -> F (in dbSNP:rs17615477).
/FTId=VAR_039856.
VARIANT 2755 2755 I -> V (in dbSNP:rs3847531).
/FTId=VAR_039857.
VARIANT 3518 3518 V -> L (in dbSNP:rs10765565).
/FTId=VAR_039858.
VARIANT 3812 3812 S -> G (in dbSNP:rs4753069).
{ECO:0000269|PubMed:11811999}.
/FTId=VAR_039859.
SEQUENCE 4557 AA; 501978 MW; 66964BED3E55BC0A CRC64;
MDIIMGHCVG TRPPACCLIL LLFKLLATVS QGLPGTGPLG FHFTHSIYNA TVYENSAART
YVNSQSRMGI TLIDLSWDIK YRIVSGDEEG FFKAEEVIIA DFCFLRIRTK GGNSAILNRE
IQDNYLLIVK GSVRGEDLEA WTKVNIQVLD MNDLRPLFSP TTYSVTIAES TPLRTSVAQV
TATDADIGSN GEFYYYFKNK VDLFSVHPTS GVISLSGRLN YDEKNRYDLE ILAVDRGMKL
YGNNGVSSTA KLYVHIERIN EHAPTIHVVT HVPFSLEKEP TYAVVTVDDL DDGANGEIES
VSIVAGDPLD QFFLAKEGKW LNEYKIKERK QIDWESFPYG YNLTLQAKDK GSPQKCSALK
AVYIGNPTRD TVPIRFEKEV YDVSISEFSP PGVVVAIVKL SPEPIDVEYK LSPGEDAVYF
KINPRSGLIV TARPLNTVKK EVYKLEVTNK EGDLKAQVTI SIEDANDHTP EFQQPLYDAY
VNESVPVGTS VLTVSASDKD KGENGYITYS IASLNLLPFV INQFTGVIST TEELDFESSP
EIYRFIVRAS DWGSPYRHES EVNVTIRIGN VNDNSPLFEK VACQGVISYD FPVGGHITAV
SAIDIDELEL VKYKIISGNE LGFFYLNPDS GVLQLKKSLT NSGIKNGNFA LRITATDGEN
LADPMSINIS VLHGKVSSKS FSCRETRVAQ KLAEKLLIKA KANGKLNLED GFLDFYSINR
QGPYFDKSFP SDVAVKEDLP VGANILKIKA YDADSGFNGK VLFTISDGNT DSCFNIDMET
GQLKVLMPMD REHTDLYLLN ITIYDLGNPQ KSSWRLLTIN VEDANDNSPV FIQDSYSVNI
LESSGIGTEI IQVEARDKDL GSNGEVTYSV LTDTQQFAIN SSTGIVYVAD QLDRESKANY
SLKIEARDKA ESGQQLFSVV TLKVFLDDVN DCSPAFIPSS YSVKVLEDLP VGTVIAWLET
HDPDLGLGGQ VRYSLVNDYN GRFEIDKASG AIRLSKELDY EKQQFYNLTV RAKDKGRPVS
LSSVSFVEVE VVDVNENLHT PYFPDFAVVG SVKENSRIGT SVLQVTARDE DSGRDGEIQY
SIRDGSGLGR FSIDDESGVI TAADILDRET MGSYWLTVYA TDRGVVPLYS TIEVYIEVED
VNDNAPLTSE PIYYPVVMEN SPKDVSVIQI QAEDPDSSSN EKLTYRITSG NPQNFFAINI
KTGLITTTSR KLDREQQAEH FLEVTVTDGG PSPKQSTIWV VVQVLDENDN KPQFPEKVYQ
IKLPERDRKK RGEPIYRAFA FDRDEGPNAE ISYSIVDGND DGKFFIDPKT GMVSSRKQFT
AGSYDILTIK AVDNGRPQKS STARLHIEWI KKPPPSPIPL TFDEPFYNFT VMESDRVTEI
VGVVSVQPAN TPLWFDIVGG NFDSAFDAEK GVGTIVIAKP LDAEQRSIYN MSVEVTDGTN
VAVTQVFIKV LDNNDNGPEF SQPNYDVTIS EDVLPDTEIL QIEATDRDEK HKLSYTVHSS
IDSISMRKFR IDPSTGVLYT AERLDHEAQD KHILNIMVRD QEFPYRRNLA RVIVNVEDAN
DHSPYFTNPL YEASVFESAA LGSAVLQVTA LDKDKGENAE LIYTIEAGNT GNMFKIEPVL
GIITICKEPD MTTMGQFVLS IKVTDQGSPP MSATAIVRIS VTMSDNSHPK FIHKDYQAEV
NENVDIGTSV ILISAISQST LIYEVKDGDI NGIFTINPYS GVITTQKALD YERTSSYQLI
IQATNMAGMA SNATVNIQIV DENDNAPVFL FSQYSGSLSE AAPINSIVRS LDNSPLVIRA
TDADSNRNAL LVYQIVESTA KKFFTVDSST GAIRTIANLD HETIAHFHFH VHVRDSGSPQ
LTAESPVEVN IEVTDVNDNP PVFTQAVFET ILLLPTYVGV EVLKVSATDP DSEVPPELTY
SLMEGSLDHF LIDSNSGVLT IKNNNLSKDH YMLIVKVSDG KFYSTSMVTI MVKEAMDSGL
HFTQSFYSTS ISENNTNITK VAIVNAVGNR LNEPLKYSIL NPGNKFKIKS TSGVIQTTGV
PFDREEQELY ELVVEASREL DHLRVARVVV RVNIEDINDN SPVFVGLPYY AAVQVDAEPG
TLIYQVTAID KDKGPNGEVT YVLQDDYGHF EINPNSGNVI LKEAFNSDLS NIEYGVTILA
KDGGKPSLST SVELPITIVN KAMPVFDKPF YTASVNEDIR MNTPILSINA TSPEGQGIIY
IIIDGDPFKQ FNIDFDTGVL KVVSPLDYEV TSAYKLTIRA SDALTGARAE VTVDLLVNDV
NDNPPIFDQP TYNTTLSEAS LIGTPVLQVV SIDADSENNK MVHYQIVQDT YNSTDYFHID
SSSGLILTAR MLDHELVQHC TLKVRSIDSG FPSLSSEVLV HIYISDVNDN PPVFNQLIYE
SYVSELAPRG HFVTCVQASD ADSSDFDRLE YSILSGNDRT SFLMDSKSGV ITLSNHRKQR
MEPLYSLNVS VSDGLFTSTA QVHIRVLGAN LYSPAFSQST YVAEVRENVA AGTKVIHVRA
TDGDPGTYGQ ISYAIINDFA KDRFLIDSNG QVITTERLDR ENPLEGDVSI FVRALDGGGR
TTFCTVRVIV VDENDNAPQF MTVEYRASVR ADVGRGHLVT QVQAIDPDDG ANSRITYSLY
SEASVSVADL LEIDPDNGWM VTKGNFNQLK NTVLSFFVKA VDGGIPVKHS LIPVYIHVLP
PETFLPSFTQ SQYSFTIAED TAIGSTVDTL RILPSQNVWF STVNGERPEN NKGGIFVIEQ
ETGTIKLDKR LDRETSPAFH FKVAATIPLD KVDIVFTVDV DIKVLDLNDN KPVFETSSYD
TIIMEGMPVG TKLTQVRAID MDWGANGQVT YSLHSDSQPE KVMEAFNIDS NTGWISTLKD
LDHETDPTFT FSVVASDLGE AFSLSSTALV SVRVTDINDN APVFAQEVYR GNVKESDPPG
EVVAVLSTWD RDTSDVNRQV SYHITGGNPR GRFALGLVQS EWKVYVKRPL DREEQDIYFL
NITATDGLFV TQAMVEVSVS DVNDNSPVCD QVAYTALLPE DIPSNKIILK VSAKDADIGS
NGYIRYSLYG SGNSEFFLDP ESGELKTLAL LDRERIPVYS LMAKATDGGG RFCQSNIHLI
LEDVNDNPPV FSSDHYNTCV YENTATKALL TRVQAVDPDI GINRKVVYSL ADSAGGVFSI
DSSSGIIILE QPLDREQQSS YNISVRATDQ SPGQSLSSLT TVTITVLDIN DNPPVFERRD
YLVTVPEDTS PGTQVLAVFA TSKDIGTNAE ITYLIRSGNE QGKFKINPKT GGISVSEVLD
YELCKRFYLV VEAKDGGTPA LSAVATVNIN LTDVNDNPPK FSQDVYSAVI SEDALVGDSV
ILLIAEDVDS QPNGQIHFSI VNGDRDNEFT VDPVLGLVKV KKKLDRERVS GYSLLVQAVD
SGIPAMSSTA TVNIDISDVN DNSPVFTPAN YTAVIQENKP VGTSILQLVV TDRDSFHNGP
PFSFSILSGN EEEEFVLDPH GILRSAVVFQ HTESLEYVLC VQAKDSGKPQ QVSHTYIRVR
VIEESTHKPT AIPLEIFIVT MEDDFPGGVI GKIHATDQDM YDVLTFALKS EQKSLFKVNS
HDGKIIALGG LDSGKYVLNV SVSDGRFQVP IDVVVHVEQL VHEMLQNTVT IRFENVSPED
FVGLHMHGFR RTLRNAVLTQ KQDSLRIISI QPVAGTNQLD MLFAVEMHSS EFYKPAYLIQ
KLSNARRHLE NIMRISAILE KNCSGLDCQE QHCEQGLSLD SHALMTYSTA RISFVCPRFY
RNVRCTCNGG LCPGSNDPCV EKPCPGDMQC VSYEASRRPF LCQCPPGKLG ECSGHTSLSF
AGNSYIKYRL SENSKEEDFK LALRLRTLQS NGIIMYTRAN PCIILKIVDG KLWFQLDCGS
GPGILGISGR AVNDGSWHSV FLELNRNFTS LSLDDSYVER RRAPLYFQTL STESSIYFGA
LVQADNIRSL TDTRVTQVLS GFQGCLDSVI LNNNELPLQN KRSSFAEVVG LTELKLGCVL
YPDACKRSPC QHGGSCTGLP SGGYQCTCLS QFTGRNCESE ITACFPNPCR NGGSCDPIGN
TFICNCKAGL TGVTCEEDIN ECEREECENG GSCVNVFGSF LCNCTPGYVG QYCGLRPVVV
PNIQAGHSYV GKEELIGIAV VLFVIFILVV LFIVFRKKVF RKNYSRNNIT LVQDPATAAL
LNKSNGIPFR NLRGSGDGRN VYQEVGPPQV PVRPMAYTPC FQSDSRSNLD KIVDGLGGEH
QEMTTFHPES PRILTARRGV VVCSVAPNLP AVSPCRSDCD SIRKNGWDAG TENKGVDDPG
EVTCFAGSNK GSNSEVQSLS SFQSDSGDDN AYHWDTSDWM PGARLSDIEE VPNYENQDGG
SAHQGSTREL ESDYYLGGYD IDSEYPPPHE EEFLSQDQLP PPLPEDFPDQ YEALPPSQPV
SLASTLSPDC RRRPQFHPSQ YLPPHPFPNE TDLVGPPASC EFSTFAVSMN QGTEPTGPAD
SVSLSLHNSR GTSSSDVSAN CGFDDSEVAM SDYESVGELS LASLHIPFVE TQHQTQV


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EIAAB14459 Cadherin family member 14,CDHF14,FAT tumor suppressor homolog 4,FAT4,FATJ,Fat-like cadherin protein FAT-J,hFat4,Homo sapiens,Human,Nbla00548,Protocadherin Fat 4
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EIAAB06485 Cadherin-related family member 2,CDHR2,Homo sapiens,Human,PCDH24,PCLKC,PC-LKC,Protocadherin LKC,Protocadherin-24
EIAAB06490 Cadherin-related family member 5,Cdhr5,Mouse,Mucdhl,Mucin and cadherin-like protein,Mupcdh,Mu-protocadherin,Mus musculus
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EIAAB14455 FAT tumor suppressor homolog 3,Fat3,Gm1132,Gm510,Mouse,Mus musculus,Protocadherin Fat 3
EIAAB14454 FAT tumor suppressor homolog 2,Fat2,Fath2,Kiaa0811,Mouse,Mus musculus,Protocadherin Fat 2
EIAAB06482 Bos taurus,Bovine,Cadherin-related family member 1,CDHR1,PCDH21,Photoreceptor cadherin,prCAD,PRCAD,Protocadherin-21
EIAAB06483 Cadherin-related family member 1,Cdhr1,Kiaa1775,Mouse,Mus musculus,Pcdh21,Photoreceptor cadherin,prCAD,Prcad,Protocadherin-21
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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1485: Interactions between CFTR and other ion channels
WP152: FGF signaling pathway
WP1780: ABC-family proteins mediated transport
WP1799: Costimulation by the CD28 family
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
WP1909: Signal regulatory protein (SIRP) family interactions
WP1983: Splicing factor NOVA regulated synpatic proteins
WP2249: Metastatic brain tumor
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP32: Translation Factors
WP566: canonical wnt - zebrafish

Related Genes :
[FAT1 CDHF7 FAT] Protocadherin Fat 1 (Cadherin family member 7) (Cadherin-related tumor suppressor homolog) (Protein fat homolog) [Cleaved into: Protocadherin Fat 1, nuclear form]
[kug fat2 CG7749] Fat-like cadherin-related tumor suppressor homolog (Protein kugelei)
[ft CG3352] Cadherin-related tumor suppressor (Protein fat) [Cleaved into: Ft-mito]
[FAT2 CDHF8 KIAA0811 MEGF1] Protocadherin Fat 2 (hFat2) (Cadherin family member 8) (Multiple epidermal growth factor-like domains protein 1) (Multiple EGF-like domains protein 1)
[Fat1 Fath mfat1] Fat 1 cadherin (Fragment)
[UBD FAT10] Ubiquitin D (Diubiquitin) (Ubiquitin-like protein FAT10)
[DCHS1 CDH19 CDH25 FIB1 KIAA1773 PCDH16] Protocadherin-16 (Cadherin-19) (Cadherin-25) (Fibroblast cadherin-1) (Protein dachsous homolog 1)
[PLA2G16 HRASLS3 HREV107] HRAS-like suppressor 3 (HRSL3) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[TP53 P53] Cellular tumor antigen p53 (Antigen NY-CO-13) (Phosphoprotein p53) (Tumor suppressor p53)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[fat-3 W08D2.4] Delta(6)-fatty-acid desaturase fat-3 (EC 1.14.19.-) (Fatty acid desaturase 3)
[MUC1 PUM] Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[Ubd Fat10] Ubiquitin D (Diubiquitin) (Ubiquitin-like protein FAT10)
[CIDEC FSP27] Cell death activator CIDE-3 (Cell death-inducing DFFA-like effector protein C) (Fat-specific protein FSP27 homolog)
[Pla2g16 H-rev107 Hrasls3 Hrev107] HRAS-like suppressor 3 (HRSL3) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A2) (H-rev 107 protein homolog)
[CD36 GP3B GP4] Platelet glycoprotein 4 (Fatty acid translocase) (FAT) (Glycoprotein IIIb) (GPIIIB) (Leukocyte differentiation antigen CD36) (PAS IV) (PAS-4) (Platelet collagen receptor) (Platelet glycoprotein IV) (GPIV) (Thrombospondin receptor) (CD antigen CD36)
[TRIM13 LEU5 RFP2 RNF77] E3 ubiquitin-protein ligase TRIM13 (EC 2.3.2.27) (B-cell chronic lymphocytic leukemia tumor suppressor Leu5) (Leukemia-associated protein 5) (Putative tumor suppressor RFP2) (RING finger protein 77) (RING-type E3 ubiquitin transferase TRIM13) (Ret finger protein 2) (Tripartite motif-containing protein 13)
[Ucp1 Slc25a7 Ucp] Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[USP9X DFFRX FAM USP9] Probable ubiquitin carboxyl-terminal hydrolase FAF-X (EC 3.4.19.12) (Deubiquitinating enzyme FAF-X) (Fat facets in mammals) (hFAM) (Fat facets protein-related, X-linked) (Ubiquitin thioesterase FAF-X) (Ubiquitin-specific protease 9, X chromosome) (Ubiquitin-specific-processing protease FAF-X)
[Cdkn2a] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)
[Sirt1 Sir2l1] NAD-dependent protein deacetylase sirtuin-1 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (SIR2alpha) (Sir2) (mSIR2a) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]
[PCDH12 UNQ395/PRO731] Protocadherin-12 (Vascular cadherin-2) (Vascular endothelial cadherin-2) (VE-cad-2) (VE-cadherin-2) [Cleaved into: Protocadherin-12, secreted form]
[Atm] Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated homolog) (A-T mutated homolog)
[Sirt2 Sir2l2] NAD-dependent protein deacetylase sirtuin-2 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2) (mSIR2L2)
[LATS2 KPM] Serine/threonine-protein kinase LATS2 (EC 2.7.11.1) (Kinase phosphorylated during mitosis protein) (Large tumor suppressor homolog 2) (Serine/threonine-protein kinase kpm) (Warts-like kinase)
[TRAF2 TRAP3] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3)
[Lats2] Serine/threonine-protein kinase LATS2 (EC 2.7.11.1) (Kinase phosphorylated during mitosis protein) (Large tumor suppressor homolog 2) (Serine/threonine-protein kinase kpm)
[FTO KIAA1752] Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-)
[UCP1 SLC25A7 UCP] Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin)

Bibliography :
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