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Q14517

- FAT1_HUMAN

UniProt

Q14517 - FAT1_HUMAN

Protein

Protocadherin Fat 1

Gene

FAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      Previous versions | rss
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    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
    2. protein binding Source: UniProtKB

    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

    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. integral component of plasma membrane Source: ProtInc
    5. lamellipodium Source: Ensembl
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    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

    ArrayExpressiQ14517.
    BgeeiQ14517.
    CleanExiHS_FAT1.
    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. 5 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.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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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    MGRHLALLLL LLLLFQHFGD SDGSQRLEQT PLQFTHLEYN VTVQENSAAK     50
    TYVGHPVKMG VYITHPAWEV RYKIVSGDSE NLFKAEEYIL GDFCFLRIRT 100
    KGGNTAILNR EVKDHYTLIV KALEKNTNVE ARTKVRVQVL DTNDLRPLFS 150
    PTSYSVSLPE NTAIRTSIAR VSATDADIGT NGEFYYSFKD RTDMFAIHPT 200
    SGVIVLTGRL DYLETKLYEM EILAADRGMK LYGSSGISSM AKLTVHIEQA 250
    NECAPVITAV TLSPSELDRD PAYAIVTVDD CDQGANGDIA SLSIVAGDLL 300
    QQFRTVRSFP GSKEYKVKAI GGIDWDSHPF GYNLTLQAKD KGTPPQFSSV 350
    KVIHVTSPQF KAGPVKFEKD VYRAEISEFA PPNTPVVMVK AIPAYSHLRY 400
    VFKSTPGKAK FSLNYNTGLI SILEPVKRQQ AAHFELEVTT SDRKASTKVL 450
    VKVLGANSNP PEFTQTAYKA AFDENVPIGT TVMSLSAVDP DEGENGYVTY 500
    SIANLNHVPF AIDHFTGAVS TSENLDYELM PRVYTLRIRA SDWGLPYRRE 550
    VEVLATITLN NLNDNTPLFE KINCEGTIPR DLGVGEQITT VSAIDADELQ 600
    LVQYQIEAGN ELDFFSLNPN SGVLSLKRSL MDGLGAKVSF HSLRITATDG 650
    ENFATPLYIN ITVAASHKLV NLQCEETGVA KMLAEKLLQA NKLHNQGEVE 700
    DIFFDSHSVN AHIPQFRSTL PTGIQVKENQ PVGSSVIFMN STDLDTGFNG 750
    KLVYAVSGGN EDSCFMIDME TGMLKILSPL DRETTDKYTL NITVYDLGIP 800
    QKAAWRLLHV VVVDANDNPP EFLQESYFVE VSEDKEVHSE IIQVEATDKD 850
    LGPNGHVTYS IVTDTDTFSI DSVTGVVNIA RPLDRELQHE HSLKIEARDQ 900
    AREEPQLFST VVVKVSLEDV NDNPPTFIPP NYRVKVREDL PEGTVIMWLE 950
    AHDPDLGQSG QVRYSLLDHG EGNFDVDKLS GAVRIVQQLD FEKKQVYNLT 1000
    VRAKDKGKPV SLSSTCYVEV EVVDVNENLH PPVFSSFVEK GTVKEDAPVG 1050
    SLVMTVSAHD EDARRDGEIR YSIRDGSGVG VFKIGEETGV IETSDRLDRE 1100
    STSHYWLTVF ATDQGVVPLS SFIEIYIEVE DVNDNAPQTS EPVYYPEIME 1150
    NSPKDVSVVQ IEAFDPDSSS NDKLMYKITS GNPQGFFSIH PKTGLITTTS 1200
    RKLDREQQDE HILEVTVTDN GSPPKSTIAR VIVKILDEND NKPQFLQKFY 1250
    KIRLPEREKP DRERNARREP LYHVIATDKD EGPNAEISYS IEDGNEHGKF 1300
    FIEPKTGVVS SKRFSAAGEY DILSIKAVDN GRPQKSSTTR LHIEWISKPK 1350
    PSLEPISFEE SFFTFTVMES DPVAHMIGVI SVEPPGIPLW FDITGGNYDS 1400
    HFDVDKGTGT IIVAKPLDAE QKSNYNLTVE ATDGTTTILT QVFIKVIDTN 1450
    DHRPQFSTSK YEVVIPEDTA PETEILQISA VDQDEKNKLI YTLQSSRDPL 1500
    SLKKFRLDPA TGSLYTSEKL DHEAVHQHTL TVMVRDQDVP VKRNFARIVV 1550
    NVSDTNDHAP WFTASSYKGR VYESAAVGSV VLQVTALDKD KGKNAEVLYS 1600
    IESGNIGNSF MIDPVLGSIK TAKELDRSNQ AEYDLMVKAT DKGSPPMSEI 1650
    TSVRIFVTIA DNASPKFTSK EYSVELSETV SIGSFVGMVT AHSQSSVVYE 1700
    IKDGNTGDAF DINPHSGTII TQKALDFETL PIYTLIIQGT NMAGLSTNTT 1750
    VLVHLQDEND NAPVFMQAEY TGLISESASI NSVVLTDRNV PLVIRAADAD 1800
    KDSNALLVYH IVEPSVHTYF AIDSSTGAIH TVLSLDYEET SIFHFTVQVH 1850
    DMGTPRLFAE YAANVTVHVI DINDCPPVFA KPLYEASLLL PTYKGVKVIT 1900
    VNATDADSSA FSQLIYSITE GNIGEKFSMD YKTGALTVQN TTQLRSRYEL 1950
    TVRASDGRFA GLTSVKINVK ESKESHLKFT QDVYSAVVKE NSTEAETLAV 2000
    ITAIGNPINE PLFYHILNPD RRFKISRTSG VLSTTGTPFD REQQEAFDVV 2050
    VEVTEEHKPS AVAHVVVKVI VEDQNDNAPV FVNLPYYAVV KVDTEVGHVI 2100
    RYVTAVDRDS GRNGEVHYYL KEHHEHFQIG PLGEISLKKQ FELDTLNKEY 2150
    LVTVVAKDGG NPAFSAEVIV PITVMNKAMP VFEKPFYSAE IAESIQVHSP 2200
    VVHVQANSPE GLKVFYSITD GDPFSQFTIN FNTGVINVIA PLDFEAHPAY 2250
    KLSIRATDSL TGAHAEVFVD IIVDDINDNP PVFAQQSYAV TLSEASVIGT 2300
    SVVQVRATDS DSEPNRGISY QMFGNHSKSH DHFHVDSSTG LISLLRTLDY 2350
    EQSRQHTIFV RAVDGGMPTL SSDVIVTVDV TDLNDNPPLF EQQIYEARIS 2400
    EHAPHGHFVT CVKAYDADSS DIDKLQYSIL SGNDHKHFVI DSATGIITLS 2450
    NLHRHALKPF YSLNLSVSDG VFRSSTQVHV TVIGGNLHSP AFLQNEYEVE 2500
    LAENAPLHTL VMEVKTTDGD SGIYGHVTYH IVNDFAKDRF YINERGQIFT 2550
    LEKLDRETPA EKVISVRLMA KDAGGKVAFC TVNVILTDDN DNAPQFRATK 2600
    YEVNIGSSAA KGTSVVKVLA SDADEGSNAD ITYAIEADSE SVKENLEINK 2650
    LSGVITTKES LIGLENEFFT FFVRAVDNGS PSKESVVLVY VKILPPEMQL 2700
    PKFSEPFYTF TVSEDVPIGT EIDLIRAEHS GTVLYSLVKG NTPESNRDES 2750
    FVIDRQSGRL KLEKSLDHET TKWYQFSILA RCTQDDHEMV ASVDVSIQVK 2800
    DANDNSPVFE SSPYEAFIVE NLPGGSRVIQ IRASDADSGT NGQVMYSLDQ 2850
    SQSVEVIESF AINMETGWIT TLKELDHEKR DNYQIKVVAS DHGEKIQLSS 2900
    TAIVDVTVTD VNDSPPRFTA EIYKGTVSED DPQGGVIAIL STTDADSEEI 2950
    NRQVTYFITG GDPLGQFAVE TIQNEWKVYV KKPLDREKRD NYLLTITATD 3000
    GTFSSKAIVE VKVLDANDNS PVCEKTLYSD TIPEDVLPGK LIMQISATDA 3050
    DIRSNAEITY TLLGSGAEKF KLNPDTGELK TSTPLDREEQ AVYHLLVRAT 3100
    DGGGRFCQAS IVLTLEDVND NAPEFSADPY AITVFENTEP GTLLTRVQAT 3150
    DADAGLNRKI LYSLIDSADG QFSINELSGI IQLEKPLDRE LQAVYTLSLK 3200
    AVDQGLPRRL TATGTVIVSV LDINDNPPVF EYREYGATVS EDILVGTEVL 3250
    QVYAASRDIE ANAEITYSII SGNEHGKFSI DSKTGAVFII ENLDYESSHE 3300
    YYLTVEATDG GTPSLSDVAT VNVNVTDIND NTPVFSQDTY TTVISEDAVL 3350
    EQSVITVMAD DADGPSNSHI HYSIIDGNQG SSFTIDPVRG EVKVTKLLDR 3400
    ETISGYTLTV QASDNGSPPR VNTTTVNIDV SDVNDNAPVF SRGNYSVIIQ 3450
    ENKPVGFSVL QLVVTDEDSS HNGPPFFFTI VTGNDEKAFE VNPQGVLLTS 3500
    SAIKRKEKDH YLLQVKVADN GKPQLSSLTY IDIRVIEESI YPPAILPLEI 3550
    FITSSGEEYS GGVIGKIHAT DQDVYDTLTY SLDPQMDNLF SVSSTGGKLI 3600
    AHKKLDIGQY LLNVSVTDGK FTTVADITVH IRQVTQEMLN HTIAIRFANL 3650
    TPEEFVGDYW RNFQRALRNI LGVRRNDIQI VSLQSSEPHP HLDVLLFVEK 3700
    PGSAQISTKQ LLHKINSSVT DIEEIIGVRI LNVFQKLCAG LDCPWKFCDE 3750
    KVSVDESVMS THSTARLSFV TPRHHRAAVC LCKEGRCPPV HHGCEDDPCP 3800
    EGSECVSDPW EEKHTCVCPS GRFGQCPGSS SMTLTGNSYV KYRLTENENK 3850
    LEMKLTMRLR TYSTHAVVMY ARGTDYSILE IHHGRLQYKF DCGSGPGIVS 3900
    VQSIQVNDGQ WHAVALEVNG NYARLVLDQV HTASGTAPGT LKTLNLDNYV 3950
    FFGGHIRQQG TRHGRSPQVG NGFRGCMDSI YLNGQELPLN SKPRSYAHIE 4000
    ESVDVSPGCF LTATEDCASN PCQNGGVCNP SPAGGYYCKC SALYIGTHCE 4050
    ISVNPCSSKP CLYGGTCVVD NGGFVCQCRG LYTGQRCQLS PYCKDEPCKN 4100
    GGTCFDSLDG AVCQCDSGFR GERCQSDIDE CSGNPCLHGA LCENTHGSYH 4150
    CNCSHEYRGR HCEDAAPNQY VSTPWNIGLA EGIGIVVFVA GIFLLVVVFV 4200
    LCRKMISRKK KHQAEPKDKH LGPATAFLQR PYFDSKLNKN IYSDIPPQVP 4250
    VRPISYTPSI PSDSRNNLDR NSFEGSAIPE HPEFSTFNPE SVHGHRKAVA 4300
    VCSVAPNLPP PPPSNSPSDS DSIQKPSWDF DYDTKVVDLD PCLSKKPLEE 4350
    KPSQPYSARE SLSEVQSLSS FQSESCDDNG YHWDTSDWMP SVPLPDIQEF 4400
    PNYEVIDEQT PLYSADPNAI DTDYYPGGYD IESDFPPPPE DFPAADELPP 4450
    LPPEFSNQFE SIHPPRDMPA AGSLGSSSRN RQRFNLNQYL PNFYPLDMSE 4500
    PQTKGTGENS TCREPHAPYP PGYQRHFEAP AVESMPMSVY ASTASCSDVS 4550
    ACCEVESEVM MSDYESGDDG HFEEVTIPPL DSQQHTEV 4588
    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. 5 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.
    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

    ArrayExpressi Q14517.
    Bgeei Q14517.
    CleanExi HS_FAT1.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    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 1, 2014
    This is version 146 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