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Q14517

- FAT1_HUMAN

UniProt

Q14517 - FAT1_HUMAN

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Protein

Protocadherin Fat 1

Gene

FAT1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. actin filament organization Source: UniProtKB
  2. anatomical structure morphogenesis Source: ProtInc
  3. cell adhesion Source: ProtInc
  4. cell-cell signaling Source: ProtInc
  5. cell migration Source: UniProtKB
  6. establishment or maintenance of cell polarity Source: UniProtKB
  7. homophilic cell adhesion Source: InterPro
  8. single organismal cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:3595. FAT1.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Nucleus 1 Publication. Cytoplasmperinuclear region 1 Publication

GO - Cellular componenti

  1. cell-cell junction Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. filopodium Source: Ensembl
  4. focal adhesion Source: UniProtKB
  5. integral component of plasma membrane Source: ProtInc
  6. lamellipodium Source: Ensembl
  7. nucleus Source: UniProtKB
  8. perinuclear region of cytoplasm Source: UniProtKB
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164719952.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 4588Protocadherin Fat 1, nuclear formPRO_0000408559
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 45884567Protocadherin Fat 1PRO_0000004017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi660 – 6601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi998 – 9981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1426 – 14261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1551 – 15511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1748 – 17481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1864 – 18641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1902 – 19021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1940 – 19401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1991 – 19911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2325 – 23251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2464 – 24641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3324 – 33241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3415 – 34151N-linked (GlcNAc...)1 Publication
Glycosylationi3422 – 34221N-linked (GlcNAc...)1 Publication
Glycosylationi3444 – 34441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3613 – 36131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3640 – 36401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3716 – 37161N-linked (GlcNAc...)2 Publications
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
Glycosylationi4152 – 41521N-linked (GlcNAc...)Sequence Analysis
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

MaxQBiQ14517.
PaxDbiQ14517.
PRIDEiQ14517.

PTM databases

PhosphoSiteiQ14517.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ14517.
CleanExiHS_FAT1.
ExpressionAtlasiQ14517. baseline and differential.
GenevestigatoriQ14517.

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. 18 interactions.
IntActiQ14517. 10 interactions.
MINTiMINT-2806731.
STRINGi9606.ENSP00000406229.

Structurei

3D structure databases

ProteinModelPortaliQ14517.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 41814160ExtracellularSequence AnalysisAdd
BLAST
Topological domaini4203 – 4588386CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4182 – 420221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 149115Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini150 – 257108Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini368 – 46396Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini464 – 569106Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini570 – 673104Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini718 – 822105Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini823 – 927105Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini928 – 1034107Cadherin 8PROSITE-ProRule annotationAdd
BLAST
Domaini1035 – 1139105Cadherin 9PROSITE-ProRule annotationAdd
BLAST
Domaini1140 – 1245106Cadherin 10PROSITE-ProRule annotationAdd
BLAST
Domaini1246 – 1357112Cadherin 11PROSITE-ProRule annotationAdd
BLAST
Domaini1359 – 145698Cadherin 12PROSITE-ProRule annotationAdd
BLAST
Domaini1457 – 1562106Cadherin 13PROSITE-ProRule annotationAdd
BLAST
Domaini1563 – 1667105Cadherin 14PROSITE-ProRule annotationAdd
BLAST
Domaini1668 – 176598Cadherin 15PROSITE-ProRule annotationAdd
BLAST
Domaini1766 – 1879114Cadherin 16PROSITE-ProRule annotationAdd
BLAST
Domaini1880 – 1979100Cadherin 17PROSITE-ProRule annotationAdd
BLAST
Domaini1980 – 2081102Cadherin 18PROSITE-ProRule annotationAdd
BLAST
Domaini2082 – 2182101Cadherin 19PROSITE-ProRule annotationAdd
BLAST
Domaini2183 – 2283101Cadherin 20PROSITE-ProRule annotationAdd
BLAST
Domaini2284 – 2390107Cadherin 21PROSITE-ProRule annotationAdd
BLAST
Domaini2391 – 2492102Cadherin 22PROSITE-ProRule annotationAdd
BLAST
Domaini2493 – 2596104Cadherin 23PROSITE-ProRule annotationAdd
BLAST
Domaini2597 – 2703107Cadherin 24PROSITE-ProRule annotationAdd
BLAST
Domaini2704 – 2809106Cadherin 25PROSITE-ProRule annotationAdd
BLAST
Domaini2810 – 2918109Cadherin 26PROSITE-ProRule annotationAdd
BLAST
Domaini2919 – 3023105Cadherin 27PROSITE-ProRule annotationAdd
BLAST
Domaini3024 – 3125102Cadherin 28PROSITE-ProRule annotationAdd
BLAST
Domaini3126 – 3230105Cadherin 29PROSITE-ProRule annotationAdd
BLAST
Domaini3231 – 3335105Cadherin 30PROSITE-ProRule annotationAdd
BLAST
Domaini3336 – 3440105Cadherin 31PROSITE-ProRule annotationAdd
BLAST
Domaini3441 – 3545105Cadherin 32PROSITE-ProRule annotationAdd
BLAST
Domaini3546 – 3647102Cadherin 33PROSITE-ProRule annotationAdd
BLAST
Domaini3790 – 382738EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini3829 – 4009181Laminin G-likePROSITE-ProRule annotationAdd
BLAST
Domaini4013 – 405038EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini4052 – 408837EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini4089 – 412537EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini4127 – 416337EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4204 – 421411Nuclear localization signalSequence AnalysisAdd
BLAST
Motifi4378 – 43825PTB-like motifBy similarity

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

eggNOGiNOG12793.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000046499.
HOVERGENiHBG005641.
InParanoidiQ14517.
KOiK16506.
OMAiPYEAFIV.
OrthoDBiEOG7WMCHJ.
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.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
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.
PF07645. EGF_CA. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 34 hits.
SM00181. EGF. 3 hits.
SM00179. EGF_CA. 1 hit.
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

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        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti322 – 3221G → D in CAA60685. (PubMed:8586420)Curated
Sequence conflicti404 – 4041S → R in CAA60685. (PubMed:8586420)Curated
Sequence conflicti482 – 4821V → I in CAA60685. (PubMed:8586420)Curated
Sequence conflicti614 – 6141F → L in CAA60685. (PubMed:8586420)Curated
Sequence conflicti862 – 8621V → L in CAA60685. (PubMed:8586420)Curated
Sequence conflicti1064 – 10641R → G in CAA60685. (PubMed:8586420)Curated
Sequence conflicti1273 – 12731H → R in CAA60685. (PubMed:8586420)Curated
Sequence conflicti1351 – 13511P → Q in CAA60685. (PubMed:8586420)Curated
Sequence conflicti1526 – 15294HQHT → SPAH in CAA60685. (PubMed:8586420)Curated
Sequence conflicti1604 – 16041G → GNIG in CAA60685. (PubMed:8586420)Curated
Sequence conflicti2006 – 20061N → S in CAA60685. (PubMed:8586420)Curated
Sequence conflicti2054 – 20541T → I in CAA60685. (PubMed:8586420)Curated
Sequence conflicti2385 – 23851D → G in CAA60685. (PubMed:8586420)Curated
Sequence conflicti2618 – 26192VL → S in CAA60685. (PubMed:8586420)Curated
Sequence conflicti2718 – 27181I → V in CAA60685. (PubMed:8586420)Curated
Sequence conflicti3113 – 31131L → V in CAA60685. (PubMed:8586420)Curated
Sequence conflicti4059 – 40591K → N in CAA60685. (PubMed:8586420)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311A → V.
Corresponds to variant rs3733415 [ dbSNP | Ensembl ].
VAR_055590
Natural varianti1330 – 13301N → S.
Corresponds to variant rs874111 [ dbSNP | Ensembl ].
VAR_055591
Natural varianti1564 – 15641A → T.
Corresponds to variant rs2304867 [ dbSNP | Ensembl ].
VAR_055592
Natural varianti1605 – 16051N → D.
Corresponds to variant rs6836935 [ dbSNP | Ensembl ].
VAR_055593
Natural varianti3800 – 38001P → H.
Corresponds to variant rs11731738 [ dbSNP | Ensembl ].
VAR_055594

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006714139.1.
UniGeneiHs.481371.

Genome annotation databases

EnsembliENST00000441802; ENSP00000406229; ENSG00000083857.
GeneIDi2195.
KEGGihsa:2195.
UCSCiuc003izf.3. human.

Polymorphism databases

DMDMi334302792.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X87241 mRNA. Translation: CAA60685.1 .
AC107050 Genomic DNA. No translation available.
AC110761 Genomic DNA. No translation available.
CCDSi CCDS47177.1.
RefSeqi NP_005236.2. NM_005245.3.
XP_006714202.1. XM_006714139.1.
UniGenei Hs.481371.

3D structure databases

ProteinModelPortali Q14517.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108489. 18 interactions.
IntActi Q14517. 10 interactions.
MINTi MINT-2806731.
STRINGi 9606.ENSP00000406229.

PTM databases

PhosphoSitei Q14517.

Polymorphism databases

DMDMi 334302792.

Proteomic databases

MaxQBi Q14517.
PaxDbi Q14517.
PRIDEi Q14517.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000441802 ; ENSP00000406229 ; ENSG00000083857 .
GeneIDi 2195.
KEGGi hsa:2195.
UCSCi uc003izf.3. human.

Organism-specific databases

CTDi 2195.
GeneCardsi GC04M187508.
HGNCi HGNC:3595. FAT1.
HPAi HPA001869.
HPA023882.
MIMi 600976. gene.
neXtProti NX_Q14517.
PharmGKBi PA164719952.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118805.
HOGENOMi HOG000046499.
HOVERGENi HBG005641.
InParanoidi Q14517.
KOi K16506.
OMAi PYEAFIV.
OrthoDBi EOG7WMCHJ.
TreeFami TF316403.

Miscellaneous databases

ChiTaRSi FAT1. human.
GeneWikii FAT_(gene).
GenomeRNAii 2195.
NextBioi 8873.
PROi Q14517.
SOURCEi Search...

Gene expression databases

Bgeei Q14517.
CleanExi HS_FAT1.
ExpressionAtlasi Q14517. baseline and differential.
Genevestigatori Q14517.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
2.60.40.60. 33 hits.
InterProi IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF00028. Cadherin. 29 hits.
PF00008. EGF. 2 hits.
PF07645. EGF_CA. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view ]
PRINTSi PR00205. CADHERIN.
SMARTi SM00112. CA. 34 hits.
SM00181. EGF. 3 hits.
SM00179. EGF_CA. 1 hit.
SM00282. LamG. 1 hit.
[Graphical view ]
SUPFAMi SSF49313. SSF49313. 33 hits.
SSF49899. SSF49899. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and tissue expression of FAT, the human homologue of the Drosophila fat gene that is located on chromosome 4q34-q35 and encodes a putative adhesion molecule."
    Dunne J., Hanby A.M., Poulsom R., Jones T.A., Sheer D., Chin W.G., Da S.M., Zhao Q., Beverley P.C.L., Owen M.J.
    Genomics 30:207-223(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphocyte.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Processing of the human protocadherin Fat1 and translocation of its cytoplasmic domain to the nucleus."
    Magg T., Schreiner D., Solis G.P., Bade E.G., Hofer H.W.
    Exp. Cell Res. 307:100-108(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  4. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Atrophin proteins interact with the Fat1 cadherin and regulate migration and orientation in vascular smooth muscle cells."
    Hou R., Sibinga N.E.
    J. Biol. Chem. 284:6955-6965(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATN1 AND RERE.
  6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3415; ASN-3422 AND ASN-3716.
    Tissue: Liver.
  7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3716.
    Tissue: Leukemic T-cell.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: October 29, 2014
This is version 147 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

External Data

Dasty 3