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Protein

Protocadherin Fat 1

Gene

FAT1

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

Functioni

Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact.By similarity

GO - Molecular functioni

GO - Biological processi

  • actin filament organization Source: UniProtKB
  • anatomical structure morphogenesis Source: ProtInc
  • cell adhesion Source: ProtInc
  • cell-cell signaling Source: ProtInc
  • cell migration Source: UniProtKB
  • establishment or maintenance of cell polarity Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • single organismal cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000083857-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protocadherin Fat 1
Alternative name(s):
Cadherin family member 7
Cadherin-related tumor suppressor homolog
Protein fat homolog
Cleaved into the following chain:
Gene namesi
Name:FAT1
Synonyms:CDHF7, FAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3595. FAT1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 4181ExtracellularSequence analysisAdd BLAST4160
Transmembranei4182 – 4202HelicalSequence analysisAdd BLAST21
Topological domaini4203 – 4588CytoplasmicSequence analysisAdd BLAST386

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • filopodium Source: Ensembl
  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • lamellipodium Source: Ensembl
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi2195.
OpenTargetsiENSG00000083857.
PharmGKBiPA164719952.

Polymorphism and mutation databases

BioMutaiFAT1.
DMDMi334302792.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000408559? – 4588Protocadherin Fat 1, nuclear form
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000000401722 – 4588Protocadherin Fat 1Add BLAST4567

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...)Sequence analysis1
Glycosylationi333N-linked (GlcNAc...)Sequence analysis1
Glycosylationi660N-linked (GlcNAc...)Sequence analysis1
Glycosylationi740N-linked (GlcNAc...)Sequence analysis1
Glycosylationi791N-linked (GlcNAc...)Sequence analysis1
Glycosylationi998N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1426N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1551N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1748N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1864N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1902N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1940N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1991N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2325N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2464N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3415N-linked (GlcNAc...)1 Publication1
Glycosylationi3422N-linked (GlcNAc...)1 Publication1
Glycosylationi3444N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3613N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3640N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3716N-linked (GlcNAc...)2 Publications1
Disulfide bondi3794 ↔ 3805By similarity
Disulfide bondi3799 ↔ 3816By similarity
Disulfide bondi3818 ↔ 3826By similarity
Disulfide bondi3976 ↔ 4009By similarity
Disulfide bondi4017 ↔ 4028By similarity
Disulfide bondi4022 ↔ 4038By similarity
Disulfide bondi4040 ↔ 4049By similarity
Disulfide bondi4056 ↔ 4067By similarity
Disulfide bondi4061 ↔ 4076By similarity
Disulfide bondi4078 ↔ 4087By similarity
Disulfide bondi4093 ↔ 4104By similarity
Disulfide bondi4098 ↔ 4113By similarity
Disulfide bondi4115 ↔ 4124By similarity
Disulfide bondi4131 ↔ 4142By similarity
Disulfide bondi4136 ↔ 4151By similarity
Glycosylationi4152N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4153 ↔ 4162By similarity

Post-translational modificationi

Undergoes proteolytic cleavage. The extracellular domain is cleaved off and the cytoplasmic domain (about 400 AA) shuttles to the nucleus.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ14517.
MaxQBiQ14517.
PaxDbiQ14517.
PeptideAtlasiQ14517.
PRIDEiQ14517.

PTM databases

iPTMnetiQ14517.
PhosphoSitePlusiQ14517.

Expressioni

Tissue specificityi

Expressed in many epithelial and some endothelial and smooth muscle cells.

Gene expression databases

BgeeiENSG00000083857.
CleanExiHS_FAT1.
ExpressionAtlasiQ14517. baseline and differential.
GenevisibleiQ14517. HS.

Organism-specific databases

HPAiHPA001869.
HPA023882.

Interactioni

Subunit structurei

Interacts (via the C-terminus 4300-4400 AA) with ATN1. Interacts with RERE. Interacts (via EVH1 domains) with ENAH (By similarity). Interacts (via cytoplasmic domain) with CTNNB1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ENAHQ8N8S72EBI-1171918,EBI-2834410
HOMER3Q9NSC54EBI-1171918,EBI-748420
Homer3Q99JP62EBI-1171918,EBI-6272061From a different organism.

Protein-protein interaction databases

BioGridi108489. 36 interactors.
IntActiQ14517. 23 interactors.
MINTiMINT-2806731.
STRINGi9606.ENSP00000406229.

Structurei

3D structure databases

ProteinModelPortaliQ14517.
SMRiQ14517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 149Cadherin 1PROSITE-ProRule annotationAdd BLAST115
Domaini150 – 257Cadherin 2PROSITE-ProRule annotationAdd BLAST108
Domaini368 – 463Cadherin 3PROSITE-ProRule annotationAdd BLAST96
Domaini464 – 569Cadherin 4PROSITE-ProRule annotationAdd BLAST106
Domaini570 – 673Cadherin 5PROSITE-ProRule annotationAdd BLAST104
Domaini718 – 822Cadherin 6PROSITE-ProRule annotationAdd BLAST105
Domaini823 – 927Cadherin 7PROSITE-ProRule annotationAdd BLAST105
Domaini928 – 1034Cadherin 8PROSITE-ProRule annotationAdd BLAST107
Domaini1035 – 1139Cadherin 9PROSITE-ProRule annotationAdd BLAST105
Domaini1140 – 1245Cadherin 10PROSITE-ProRule annotationAdd BLAST106
Domaini1246 – 1357Cadherin 11PROSITE-ProRule annotationAdd BLAST112
Domaini1359 – 1456Cadherin 12PROSITE-ProRule annotationAdd BLAST98
Domaini1457 – 1562Cadherin 13PROSITE-ProRule annotationAdd BLAST106
Domaini1563 – 1667Cadherin 14PROSITE-ProRule annotationAdd BLAST105
Domaini1668 – 1765Cadherin 15PROSITE-ProRule annotationAdd BLAST98
Domaini1766 – 1879Cadherin 16PROSITE-ProRule annotationAdd BLAST114
Domaini1880 – 1979Cadherin 17PROSITE-ProRule annotationAdd BLAST100
Domaini1980 – 2081Cadherin 18PROSITE-ProRule annotationAdd BLAST102
Domaini2082 – 2182Cadherin 19PROSITE-ProRule annotationAdd BLAST101
Domaini2183 – 2283Cadherin 20PROSITE-ProRule annotationAdd BLAST101
Domaini2284 – 2390Cadherin 21PROSITE-ProRule annotationAdd BLAST107
Domaini2391 – 2492Cadherin 22PROSITE-ProRule annotationAdd BLAST102
Domaini2493 – 2596Cadherin 23PROSITE-ProRule annotationAdd BLAST104
Domaini2597 – 2703Cadherin 24PROSITE-ProRule annotationAdd BLAST107
Domaini2704 – 2809Cadherin 25PROSITE-ProRule annotationAdd BLAST106
Domaini2810 – 2918Cadherin 26PROSITE-ProRule annotationAdd BLAST109
Domaini2919 – 3023Cadherin 27PROSITE-ProRule annotationAdd BLAST105
Domaini3024 – 3125Cadherin 28PROSITE-ProRule annotationAdd BLAST102
Domaini3126 – 3230Cadherin 29PROSITE-ProRule annotationAdd BLAST105
Domaini3231 – 3335Cadherin 30PROSITE-ProRule annotationAdd BLAST105
Domaini3336 – 3440Cadherin 31PROSITE-ProRule annotationAdd BLAST105
Domaini3441 – 3545Cadherin 32PROSITE-ProRule annotationAdd BLAST105
Domaini3546 – 3647Cadherin 33PROSITE-ProRule annotationAdd BLAST102
Domaini3790 – 3827EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini3829 – 4009Laminin G-likePROSITE-ProRule annotationAdd BLAST181
Domaini4013 – 4050EGF-like 2PROSITE-ProRule annotationAdd BLAST38
Domaini4052 – 4088EGF-like 3PROSITE-ProRule annotationAdd BLAST37
Domaini4089 – 4125EGF-like 4PROSITE-ProRule annotationAdd BLAST37
Domaini4127 – 4163EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4204 – 4214Nuclear localization signalSequence analysisAdd BLAST11
Motifi4378 – 4382PTB-like motifBy similarity5

Domaini

A PTB-like motif (DNXYH sequence) is required for the targeting to the leading edge. This motif represents a minimal protein-protein interaction core motif that is not regulated by tyrosine phosphorylation (By similarity).By similarity

Sequence similaritiesi

Contains 33 cadherin domains.PROSITE-ProRule annotation
Contains 5 EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000046499.
HOVERGENiHBG005641.
InParanoidiQ14517.
KOiK16506.
TreeFamiTF316403.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
2.60.40.60. 33 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00028. Cadherin. 29 hits.
PF00008. EGF. 2 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 34 hits.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 4 hits.
SM00282. LamG. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 33 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00232. CADHERIN_1. 17 hits.
PS50268. CADHERIN_2. 33 hits.
PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 1 hit.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q14517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRHLALLLL LLLLFQHFGD SDGSQRLEQT PLQFTHLEYN VTVQENSAAK
60 70 80 90 100
TYVGHPVKMG VYITHPAWEV RYKIVSGDSE NLFKAEEYIL GDFCFLRIRT
110 120 130 140 150
KGGNTAILNR EVKDHYTLIV KALEKNTNVE ARTKVRVQVL DTNDLRPLFS
160 170 180 190 200
PTSYSVSLPE NTAIRTSIAR VSATDADIGT NGEFYYSFKD RTDMFAIHPT
210 220 230 240 250
SGVIVLTGRL DYLETKLYEM EILAADRGMK LYGSSGISSM AKLTVHIEQA
260 270 280 290 300
NECAPVITAV TLSPSELDRD PAYAIVTVDD CDQGANGDIA SLSIVAGDLL
310 320 330 340 350
QQFRTVRSFP GSKEYKVKAI GGIDWDSHPF GYNLTLQAKD KGTPPQFSSV
360 370 380 390 400
KVIHVTSPQF KAGPVKFEKD VYRAEISEFA PPNTPVVMVK AIPAYSHLRY
410 420 430 440 450
VFKSTPGKAK FSLNYNTGLI SILEPVKRQQ AAHFELEVTT SDRKASTKVL
460 470 480 490 500
VKVLGANSNP PEFTQTAYKA AFDENVPIGT TVMSLSAVDP DEGENGYVTY
510 520 530 540 550
SIANLNHVPF AIDHFTGAVS TSENLDYELM PRVYTLRIRA SDWGLPYRRE
560 570 580 590 600
VEVLATITLN NLNDNTPLFE KINCEGTIPR DLGVGEQITT VSAIDADELQ
610 620 630 640 650
LVQYQIEAGN ELDFFSLNPN SGVLSLKRSL MDGLGAKVSF HSLRITATDG
660 670 680 690 700
ENFATPLYIN ITVAASHKLV NLQCEETGVA KMLAEKLLQA NKLHNQGEVE
710 720 730 740 750
DIFFDSHSVN AHIPQFRSTL PTGIQVKENQ PVGSSVIFMN STDLDTGFNG
760 770 780 790 800
KLVYAVSGGN EDSCFMIDME TGMLKILSPL DRETTDKYTL NITVYDLGIP
810 820 830 840 850
QKAAWRLLHV VVVDANDNPP EFLQESYFVE VSEDKEVHSE IIQVEATDKD
860 870 880 890 900
LGPNGHVTYS IVTDTDTFSI DSVTGVVNIA RPLDRELQHE HSLKIEARDQ
910 920 930 940 950
AREEPQLFST VVVKVSLEDV NDNPPTFIPP NYRVKVREDL PEGTVIMWLE
960 970 980 990 1000
AHDPDLGQSG QVRYSLLDHG EGNFDVDKLS GAVRIVQQLD FEKKQVYNLT
1010 1020 1030 1040 1050
VRAKDKGKPV SLSSTCYVEV EVVDVNENLH PPVFSSFVEK GTVKEDAPVG
1060 1070 1080 1090 1100
SLVMTVSAHD EDARRDGEIR YSIRDGSGVG VFKIGEETGV IETSDRLDRE
1110 1120 1130 1140 1150
STSHYWLTVF ATDQGVVPLS SFIEIYIEVE DVNDNAPQTS EPVYYPEIME
1160 1170 1180 1190 1200
NSPKDVSVVQ IEAFDPDSSS NDKLMYKITS GNPQGFFSIH PKTGLITTTS
1210 1220 1230 1240 1250
RKLDREQQDE HILEVTVTDN GSPPKSTIAR VIVKILDEND NKPQFLQKFY
1260 1270 1280 1290 1300
KIRLPEREKP DRERNARREP LYHVIATDKD EGPNAEISYS IEDGNEHGKF
1310 1320 1330 1340 1350
FIEPKTGVVS SKRFSAAGEY DILSIKAVDN GRPQKSSTTR LHIEWISKPK
1360 1370 1380 1390 1400
PSLEPISFEE SFFTFTVMES DPVAHMIGVI SVEPPGIPLW FDITGGNYDS
1410 1420 1430 1440 1450
HFDVDKGTGT IIVAKPLDAE QKSNYNLTVE ATDGTTTILT QVFIKVIDTN
1460 1470 1480 1490 1500
DHRPQFSTSK YEVVIPEDTA PETEILQISA VDQDEKNKLI YTLQSSRDPL
1510 1520 1530 1540 1550
SLKKFRLDPA TGSLYTSEKL DHEAVHQHTL TVMVRDQDVP VKRNFARIVV
1560 1570 1580 1590 1600
NVSDTNDHAP WFTASSYKGR VYESAAVGSV VLQVTALDKD KGKNAEVLYS
1610 1620 1630 1640 1650
IESGNIGNSF MIDPVLGSIK TAKELDRSNQ AEYDLMVKAT DKGSPPMSEI
1660 1670 1680 1690 1700
TSVRIFVTIA DNASPKFTSK EYSVELSETV SIGSFVGMVT AHSQSSVVYE
1710 1720 1730 1740 1750
IKDGNTGDAF DINPHSGTII TQKALDFETL PIYTLIIQGT NMAGLSTNTT
1760 1770 1780 1790 1800
VLVHLQDEND NAPVFMQAEY TGLISESASI NSVVLTDRNV PLVIRAADAD
1810 1820 1830 1840 1850
KDSNALLVYH IVEPSVHTYF AIDSSTGAIH TVLSLDYEET SIFHFTVQVH
1860 1870 1880 1890 1900
DMGTPRLFAE YAANVTVHVI DINDCPPVFA KPLYEASLLL PTYKGVKVIT
1910 1920 1930 1940 1950
VNATDADSSA FSQLIYSITE GNIGEKFSMD YKTGALTVQN TTQLRSRYEL
1960 1970 1980 1990 2000
TVRASDGRFA GLTSVKINVK ESKESHLKFT QDVYSAVVKE NSTEAETLAV
2010 2020 2030 2040 2050
ITAIGNPINE PLFYHILNPD RRFKISRTSG VLSTTGTPFD REQQEAFDVV
2060 2070 2080 2090 2100
VEVTEEHKPS AVAHVVVKVI VEDQNDNAPV FVNLPYYAVV KVDTEVGHVI
2110 2120 2130 2140 2150
RYVTAVDRDS GRNGEVHYYL KEHHEHFQIG PLGEISLKKQ FELDTLNKEY
2160 2170 2180 2190 2200
LVTVVAKDGG NPAFSAEVIV PITVMNKAMP VFEKPFYSAE IAESIQVHSP
2210 2220 2230 2240 2250
VVHVQANSPE GLKVFYSITD GDPFSQFTIN FNTGVINVIA PLDFEAHPAY
2260 2270 2280 2290 2300
KLSIRATDSL TGAHAEVFVD IIVDDINDNP PVFAQQSYAV TLSEASVIGT
2310 2320 2330 2340 2350
SVVQVRATDS DSEPNRGISY QMFGNHSKSH DHFHVDSSTG LISLLRTLDY
2360 2370 2380 2390 2400
EQSRQHTIFV RAVDGGMPTL SSDVIVTVDV TDLNDNPPLF EQQIYEARIS
2410 2420 2430 2440 2450
EHAPHGHFVT CVKAYDADSS DIDKLQYSIL SGNDHKHFVI DSATGIITLS
2460 2470 2480 2490 2500
NLHRHALKPF YSLNLSVSDG VFRSSTQVHV TVIGGNLHSP AFLQNEYEVE
2510 2520 2530 2540 2550
LAENAPLHTL VMEVKTTDGD SGIYGHVTYH IVNDFAKDRF YINERGQIFT
2560 2570 2580 2590 2600
LEKLDRETPA EKVISVRLMA KDAGGKVAFC TVNVILTDDN DNAPQFRATK
2610 2620 2630 2640 2650
YEVNIGSSAA KGTSVVKVLA SDADEGSNAD ITYAIEADSE SVKENLEINK
2660 2670 2680 2690 2700
LSGVITTKES LIGLENEFFT FFVRAVDNGS PSKESVVLVY VKILPPEMQL
2710 2720 2730 2740 2750
PKFSEPFYTF TVSEDVPIGT EIDLIRAEHS GTVLYSLVKG NTPESNRDES
2760 2770 2780 2790 2800
FVIDRQSGRL KLEKSLDHET TKWYQFSILA RCTQDDHEMV ASVDVSIQVK
2810 2820 2830 2840 2850
DANDNSPVFE SSPYEAFIVE NLPGGSRVIQ IRASDADSGT NGQVMYSLDQ
2860 2870 2880 2890 2900
SQSVEVIESF AINMETGWIT TLKELDHEKR DNYQIKVVAS DHGEKIQLSS
2910 2920 2930 2940 2950
TAIVDVTVTD VNDSPPRFTA EIYKGTVSED DPQGGVIAIL STTDADSEEI
2960 2970 2980 2990 3000
NRQVTYFITG GDPLGQFAVE TIQNEWKVYV KKPLDREKRD NYLLTITATD
3010 3020 3030 3040 3050
GTFSSKAIVE VKVLDANDNS PVCEKTLYSD TIPEDVLPGK LIMQISATDA
3060 3070 3080 3090 3100
DIRSNAEITY TLLGSGAEKF KLNPDTGELK TSTPLDREEQ AVYHLLVRAT
3110 3120 3130 3140 3150
DGGGRFCQAS IVLTLEDVND NAPEFSADPY AITVFENTEP GTLLTRVQAT
3160 3170 3180 3190 3200
DADAGLNRKI LYSLIDSADG QFSINELSGI IQLEKPLDRE LQAVYTLSLK
3210 3220 3230 3240 3250
AVDQGLPRRL TATGTVIVSV LDINDNPPVF EYREYGATVS EDILVGTEVL
3260 3270 3280 3290 3300
QVYAASRDIE ANAEITYSII SGNEHGKFSI DSKTGAVFII ENLDYESSHE
3310 3320 3330 3340 3350
YYLTVEATDG GTPSLSDVAT VNVNVTDIND NTPVFSQDTY TTVISEDAVL
3360 3370 3380 3390 3400
EQSVITVMAD DADGPSNSHI HYSIIDGNQG SSFTIDPVRG EVKVTKLLDR
3410 3420 3430 3440 3450
ETISGYTLTV QASDNGSPPR VNTTTVNIDV SDVNDNAPVF SRGNYSVIIQ
3460 3470 3480 3490 3500
ENKPVGFSVL QLVVTDEDSS HNGPPFFFTI VTGNDEKAFE VNPQGVLLTS
3510 3520 3530 3540 3550
SAIKRKEKDH YLLQVKVADN GKPQLSSLTY IDIRVIEESI YPPAILPLEI
3560 3570 3580 3590 3600
FITSSGEEYS GGVIGKIHAT DQDVYDTLTY SLDPQMDNLF SVSSTGGKLI
3610 3620 3630 3640 3650
AHKKLDIGQY LLNVSVTDGK FTTVADITVH IRQVTQEMLN HTIAIRFANL
3660 3670 3680 3690 3700
TPEEFVGDYW RNFQRALRNI LGVRRNDIQI VSLQSSEPHP HLDVLLFVEK
3710 3720 3730 3740 3750
PGSAQISTKQ LLHKINSSVT DIEEIIGVRI LNVFQKLCAG LDCPWKFCDE
3760 3770 3780 3790 3800
KVSVDESVMS THSTARLSFV TPRHHRAAVC LCKEGRCPPV HHGCEDDPCP
3810 3820 3830 3840 3850
EGSECVSDPW EEKHTCVCPS GRFGQCPGSS SMTLTGNSYV KYRLTENENK
3860 3870 3880 3890 3900
LEMKLTMRLR TYSTHAVVMY ARGTDYSILE IHHGRLQYKF DCGSGPGIVS
3910 3920 3930 3940 3950
VQSIQVNDGQ WHAVALEVNG NYARLVLDQV HTASGTAPGT LKTLNLDNYV
3960 3970 3980 3990 4000
FFGGHIRQQG TRHGRSPQVG NGFRGCMDSI YLNGQELPLN SKPRSYAHIE
4010 4020 4030 4040 4050
ESVDVSPGCF LTATEDCASN PCQNGGVCNP SPAGGYYCKC SALYIGTHCE
4060 4070 4080 4090 4100
ISVNPCSSKP CLYGGTCVVD NGGFVCQCRG LYTGQRCQLS PYCKDEPCKN
4110 4120 4130 4140 4150
GGTCFDSLDG AVCQCDSGFR GERCQSDIDE CSGNPCLHGA LCENTHGSYH
4160 4170 4180 4190 4200
CNCSHEYRGR HCEDAAPNQY VSTPWNIGLA EGIGIVVFVA GIFLLVVVFV
4210 4220 4230 4240 4250
LCRKMISRKK KHQAEPKDKH LGPATAFLQR PYFDSKLNKN IYSDIPPQVP
4260 4270 4280 4290 4300
VRPISYTPSI PSDSRNNLDR NSFEGSAIPE HPEFSTFNPE SVHGHRKAVA
4310 4320 4330 4340 4350
VCSVAPNLPP PPPSNSPSDS DSIQKPSWDF DYDTKVVDLD PCLSKKPLEE
4360 4370 4380 4390 4400
KPSQPYSARE SLSEVQSLSS FQSESCDDNG YHWDTSDWMP SVPLPDIQEF
4410 4420 4430 4440 4450
PNYEVIDEQT PLYSADPNAI DTDYYPGGYD IESDFPPPPE DFPAADELPP
4460 4470 4480 4490 4500
LPPEFSNQFE SIHPPRDMPA AGSLGSSSRN RQRFNLNQYL PNFYPLDMSE
4510 4520 4530 4540 4550
PQTKGTGENS TCREPHAPYP PGYQRHFEAP AVESMPMSVY ASTASCSDVS
4560 4570 4580
ACCEVESEVM MSDYESGDDG HFEEVTIPPL DSQQHTEV
Length:4,588
Mass (Da):506,273
Last modified:May 31, 2011 - v2
Checksum:i1896223E46E3B892
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti322G → D in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti404S → R in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti482V → I in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti614F → L in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti862V → L in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti1064R → G in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti1273H → R in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti1351P → Q in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti1526 – 1529HQHT → SPAH in CAA60685 (PubMed:8586420).Curated4
Sequence conflicti1604G → GNIG in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti2006N → S in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti2054T → I in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti2385D → G in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti2618 – 2619VL → S in CAA60685 (PubMed:8586420).Curated2
Sequence conflicti2718I → V in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti3113L → V in CAA60685 (PubMed:8586420).Curated1
Sequence conflicti4059K → N in CAA60685 (PubMed:8586420).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055590131A → V.Corresponds to variant rs3733415dbSNPEnsembl.1
Natural variantiVAR_076441902R → S.1 PublicationCorresponds to variant rs555992573dbSNPEnsembl.1
Natural variantiVAR_0555911330N → S.Corresponds to variant rs874111dbSNPEnsembl.1
Natural variantiVAR_0764421393I → V.1 PublicationCorresponds to variant rs753226094dbSNPEnsembl.1
Natural variantiVAR_0555921564A → T.Corresponds to variant rs2304867dbSNPEnsembl.1
Natural variantiVAR_0555931605N → D.Corresponds to variant rs6836935dbSNPEnsembl.1
Natural variantiVAR_0764433732N → S.1 PublicationCorresponds to variant rs373241719dbSNPEnsembl.1
Natural variantiVAR_0555943800P → H.Corresponds to variant rs11731738dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87241 mRNA. Translation: CAA60685.1.
AC107050 Genomic DNA. No translation available.
AC110761 Genomic DNA. No translation available.
CCDSiCCDS47177.1.
RefSeqiNP_005236.2. NM_005245.3.
XP_006714202.1. XM_006714139.2.
UniGeneiHs.481371.

Genome annotation databases

EnsembliENST00000441802; ENSP00000406229; ENSG00000083857.
GeneIDi2195.
KEGGihsa:2195.
UCSCiuc003izf.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87241 mRNA. Translation: CAA60685.1.
AC107050 Genomic DNA. No translation available.
AC110761 Genomic DNA. No translation available.
CCDSiCCDS47177.1.
RefSeqiNP_005236.2. NM_005245.3.
XP_006714202.1. XM_006714139.2.
UniGeneiHs.481371.

3D structure databases

ProteinModelPortaliQ14517.
SMRiQ14517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108489. 36 interactors.
IntActiQ14517. 23 interactors.
MINTiMINT-2806731.
STRINGi9606.ENSP00000406229.

PTM databases

iPTMnetiQ14517.
PhosphoSitePlusiQ14517.

Polymorphism and mutation databases

BioMutaiFAT1.
DMDMi334302792.

Proteomic databases

EPDiQ14517.
MaxQBiQ14517.
PaxDbiQ14517.
PeptideAtlasiQ14517.
PRIDEiQ14517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000441802; ENSP00000406229; ENSG00000083857.
GeneIDi2195.
KEGGihsa:2195.
UCSCiuc003izf.4. human.

Organism-specific databases

CTDi2195.
DisGeNETi2195.
GeneCardsiFAT1.
HGNCiHGNC:3595. FAT1.
HPAiHPA001869.
HPA023882.
MIMi600976. gene.
neXtProtiNX_Q14517.
OpenTargetsiENSG00000083857.
PharmGKBiPA164719952.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000046499.
HOVERGENiHBG005641.
InParanoidiQ14517.
KOiK16506.
TreeFamiTF316403.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000083857-MONOMER.

Miscellaneous databases

ChiTaRSiFAT1. human.
GeneWikiiFAT_(gene).
GenomeRNAii2195.
PROiQ14517.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000083857.
CleanExiHS_FAT1.
ExpressionAtlasiQ14517. baseline and differential.
GenevisibleiQ14517. HS.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
2.60.40.60. 33 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00028. Cadherin. 29 hits.
PF00008. EGF. 2 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 34 hits.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 4 hits.
SM00282. LamG. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 33 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00232. CADHERIN_1. 17 hits.
PS50268. CADHERIN_2. 33 hits.
PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 1 hit.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFAT1_HUMAN
AccessioniPrimary (citable) accession number: Q14517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 31, 2011
Last modified: November 2, 2016
This is version 165 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. Human chromosome 4
    Human chromosome 4: 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

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 one 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.