Q14517 (FAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Protocadherin Fat 1, nuclear form

Gene names

Name:	FAT1
Synonyms:	CDHF7, FAT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4588 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact By similarity.
Subunit structure	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. Ref.5
Subcellular location	Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm › perinuclear region Ref.3.
Tissue specificity	Expressed in many epithelial and some endothelial and smooth muscle cells.
Domain	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.
Post-translational modification	Undergoes proteolytic cleavage. The extracellular domain is cleaved off and the cytoplasmic domain (about 400 AA) shuttles to the nucleus. Ref.3
Sequence similarities	Contains 33 cadherin domains. Contains 5 EGF-like domains. Contains 1 laminin G-like domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from sequence or structural similarity. Source: UniProtKB anatomical structure morphogenesis Traceable author statement Ref.1. Source: ProtInc cell migration Inferred from sequence or structural similarity. Source: UniProtKB cell-cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB cell-cell signaling Traceable author statement Ref.1. Source: ProtInc establishment or maintenance of cell polarity Inferred from sequence or structural similarity. Source: UniProtKB homophilic cell adhesion Inferred from electronic annotation. Source: InterPro
Cellular_component	cell-cell junction Inferred from direct assay PubMed 15148305. Source: UniProtKB filopodium Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc lamellipodium Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.3. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 4588	4567	Protocadherin Fat 1		PRO_0000004017
	Chain	? – 4588		Protocadherin Fat 1, nuclear form		PRO_0000408559
Regions
	Topological domain	22 – 4181	4160	Extracellular Potential
	Transmembrane	4182 – 4202	21	Helical; Potential
	Topological domain	4203 – 4588	386	Cytoplasmic Potential
	Domain	35 – 149	115	Cadherin 1
	Domain	150 – 257	108	Cadherin 2
	Domain	368 – 463	96	Cadherin 3
	Domain	464 – 569	106	Cadherin 4
	Domain	570 – 673	104	Cadherin 5
	Domain	718 – 822	105	Cadherin 6
	Domain	823 – 927	105	Cadherin 7
	Domain	928 – 1034	107	Cadherin 8
	Domain	1035 – 1139	105	Cadherin 9
	Domain	1140 – 1245	106	Cadherin 10
	Domain	1246 – 1357	112	Cadherin 11
	Domain	1359 – 1456	98	Cadherin 12
	Domain	1457 – 1562	106	Cadherin 13
	Domain	1563 – 1667	105	Cadherin 14
	Domain	1668 – 1765	98	Cadherin 15
	Domain	1766 – 1879	114	Cadherin 16
	Domain	1880 – 1979	100	Cadherin 17
	Domain	1980 – 2081	102	Cadherin 18
	Domain	2082 – 2182	101	Cadherin 19
	Domain	2183 – 2283	101	Cadherin 20
	Domain	2284 – 2390	107	Cadherin 21
	Domain	2391 – 2492	102	Cadherin 22
	Domain	2493 – 2596	104	Cadherin 23
	Domain	2597 – 2703	107	Cadherin 24
	Domain	2704 – 2809	106	Cadherin 25
	Domain	2810 – 2918	109	Cadherin 26
	Domain	2919 – 3023	105	Cadherin 27
	Domain	3024 – 3125	102	Cadherin 28
	Domain	3126 – 3230	105	Cadherin 29
	Domain	3231 – 3335	105	Cadherin 30
	Domain	3336 – 3440	105	Cadherin 31
	Domain	3441 – 3545	105	Cadherin 32
	Domain	3546 – 3647	102	Cadherin 33
	Domain	3790 – 3827	38	EGF-like 1
	Domain	3829 – 4009	181	Laminin G-like
	Domain	4013 – 4050	38	EGF-like 2
	Domain	4052 – 4088	37	EGF-like 3
	Domain	4089 – 4125	37	EGF-like 4
	Domain	4127 – 4163	37	EGF-like 5; calcium-binding Potential
	Motif	4204 – 4214	11	Nuclear localization signal Potential
	Motif	4378 – 4382	5	PTB-like motif By similarity
Amino acid modifications
	Glycosylation	40	1	N-linked (GlcNAc...) Potential
	Glycosylation	333	1	N-linked (GlcNAc...) Potential
	Glycosylation	660	1	N-linked (GlcNAc...) Potential
	Glycosylation	740	1	N-linked (GlcNAc...) Potential
	Glycosylation	791	1	N-linked (GlcNAc...) Potential
	Glycosylation	998	1	N-linked (GlcNAc...) Potential
	Glycosylation	1426	1	N-linked (GlcNAc...) Potential
	Glycosylation	1551	1	N-linked (GlcNAc...) Potential
	Glycosylation	1748	1	N-linked (GlcNAc...) Potential
	Glycosylation	1864	1	N-linked (GlcNAc...) Potential
	Glycosylation	1902	1	N-linked (GlcNAc...) Potential
	Glycosylation	1940	1	N-linked (GlcNAc...) Potential
	Glycosylation	1991	1	N-linked (GlcNAc...) Potential
	Glycosylation	2325	1	N-linked (GlcNAc...) Potential
	Glycosylation	2464	1	N-linked (GlcNAc...) Potential
	Glycosylation	3324	1	N-linked (GlcNAc...) Potential
	Glycosylation	3415	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	3422	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	3444	1	N-linked (GlcNAc...) Potential
	Glycosylation	3613	1	N-linked (GlcNAc...) Potential
	Glycosylation	3640	1	N-linked (GlcNAc...) Potential
	Glycosylation	3716	1	N-linked (GlcNAc...) Ref.6 Ref.7
	Glycosylation	4152	1	N-linked (GlcNAc...) Potential
	Disulfide bond	3794 ↔ 3805		By similarity
	Disulfide bond	3799 ↔ 3816		By similarity
	Disulfide bond	3818 ↔ 3826		By similarity
	Disulfide bond	3976 ↔ 4009		By similarity
	Disulfide bond	4017 ↔ 4028		By similarity
	Disulfide bond	4022 ↔ 4038		By similarity
	Disulfide bond	4040 ↔ 4049		By similarity
	Disulfide bond	4056 ↔ 4067		By similarity
	Disulfide bond	4061 ↔ 4076		By similarity
	Disulfide bond	4078 ↔ 4087		By similarity
	Disulfide bond	4093 ↔ 4104		By similarity
	Disulfide bond	4098 ↔ 4113		By similarity
	Disulfide bond	4115 ↔ 4124		By similarity
	Disulfide bond	4131 ↔ 4142		By similarity
	Disulfide bond	4136 ↔ 4151		By similarity
	Disulfide bond	4153 ↔ 4162		By similarity
Natural variations
	Natural variant	131	1	A → V. Corresponds to variant rs3733415 [ dbSNP | Ensembl ].		VAR_055590
	Natural variant	1330	1	N → S. Corresponds to variant rs874111 [ dbSNP | Ensembl ].		VAR_055591
	Natural variant	1564	1	A → T. Corresponds to variant rs2304867 [ dbSNP | Ensembl ].		VAR_055592
	Natural variant	1605	1	N → D. Corresponds to variant rs6836935 [ dbSNP | Ensembl ].		VAR_055593
	Natural variant	3800	1	P → H. Corresponds to variant rs11731738 [ dbSNP | Ensembl ].		VAR_055594
Experimental info
	Sequence conflict	322	1	G → D in CAA60685. Ref.1
	Sequence conflict	404	1	S → R in CAA60685. Ref.1
	Sequence conflict	482	1	V → I in CAA60685. Ref.1
	Sequence conflict	614	1	F → L in CAA60685. Ref.1
	Sequence conflict	862	1	V → L in CAA60685. Ref.1
	Sequence conflict	1064	1	R → G in CAA60685. Ref.1
	Sequence conflict	1273	1	H → R in CAA60685. Ref.1
	Sequence conflict	1351	1	P → Q in CAA60685. Ref.1
	Sequence conflict	1526 – 1529	4	HQHT → SPAH in CAA60685. Ref.1
	Sequence conflict	1604	1	G → GNIG in CAA60685. Ref.1
	Sequence conflict	2006	1	N → S in CAA60685. Ref.1
	Sequence conflict	2054	1	T → I in CAA60685. Ref.1
	Sequence conflict	2385	1	D → G in CAA60685. Ref.1
	Sequence conflict	2618 – 2619	2	VL → S in CAA60685. Ref.1
	Sequence conflict	2718	1	I → V in CAA60685. Ref.1
	Sequence conflict	3113	1	L → V in CAA60685. Ref.1
	Sequence conflict	4059	1	K → N in CAA60685. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q14517 [UniParc]. Last modified May 31, 2011. Version 2. Checksum: 1896223E46E3B892	FASTA	4,588	506,273
	10 20 30 40 50 60 MGRHLALLLL LLLLFQHFGD SDGSQRLEQT PLQFTHLEYN VTVQENSAAK TYVGHPVKMG 70 80 90 100 110 120 VYITHPAWEV RYKIVSGDSE NLFKAEEYIL GDFCFLRIRT KGGNTAILNR EVKDHYTLIV 130 140 150 160 170 180 KALEKNTNVE ARTKVRVQVL DTNDLRPLFS PTSYSVSLPE NTAIRTSIAR VSATDADIGT 190 200 210 220 230 240 NGEFYYSFKD RTDMFAIHPT SGVIVLTGRL DYLETKLYEM EILAADRGMK LYGSSGISSM 250 260 270 280 290 300 AKLTVHIEQA NECAPVITAV TLSPSELDRD PAYAIVTVDD CDQGANGDIA SLSIVAGDLL 310 320 330 340 350 360 QQFRTVRSFP GSKEYKVKAI GGIDWDSHPF GYNLTLQAKD KGTPPQFSSV KVIHVTSPQF 370 380 390 400 410 420 KAGPVKFEKD VYRAEISEFA PPNTPVVMVK AIPAYSHLRY VFKSTPGKAK FSLNYNTGLI 430 440 450 460 470 480 SILEPVKRQQ AAHFELEVTT SDRKASTKVL VKVLGANSNP PEFTQTAYKA AFDENVPIGT 490 500 510 520 530 540 TVMSLSAVDP DEGENGYVTY SIANLNHVPF AIDHFTGAVS TSENLDYELM PRVYTLRIRA 550 560 570 580 590 600 SDWGLPYRRE VEVLATITLN NLNDNTPLFE KINCEGTIPR DLGVGEQITT VSAIDADELQ 610 620 630 640 650 660 LVQYQIEAGN ELDFFSLNPN SGVLSLKRSL MDGLGAKVSF HSLRITATDG ENFATPLYIN 670 680 690 700 710 720 ITVAASHKLV NLQCEETGVA KMLAEKLLQA NKLHNQGEVE DIFFDSHSVN AHIPQFRSTL 730 740 750 760 770 780 PTGIQVKENQ PVGSSVIFMN STDLDTGFNG KLVYAVSGGN EDSCFMIDME TGMLKILSPL 790 800 810 820 830 840 DRETTDKYTL NITVYDLGIP QKAAWRLLHV VVVDANDNPP EFLQESYFVE VSEDKEVHSE 850 860 870 880 890 900 IIQVEATDKD LGPNGHVTYS IVTDTDTFSI DSVTGVVNIA RPLDRELQHE HSLKIEARDQ 910 920 930 940 950 960 AREEPQLFST VVVKVSLEDV NDNPPTFIPP NYRVKVREDL PEGTVIMWLE AHDPDLGQSG 970 980 990 1000 1010 1020 QVRYSLLDHG EGNFDVDKLS GAVRIVQQLD FEKKQVYNLT VRAKDKGKPV SLSSTCYVEV 1030 1040 1050 1060 1070 1080 EVVDVNENLH PPVFSSFVEK GTVKEDAPVG SLVMTVSAHD EDARRDGEIR YSIRDGSGVG 1090 1100 1110 1120 1130 1140 VFKIGEETGV IETSDRLDRE STSHYWLTVF ATDQGVVPLS SFIEIYIEVE DVNDNAPQTS 1150 1160 1170 1180 1190 1200 EPVYYPEIME NSPKDVSVVQ IEAFDPDSSS NDKLMYKITS GNPQGFFSIH PKTGLITTTS 1210 1220 1230 1240 1250 1260 RKLDREQQDE HILEVTVTDN GSPPKSTIAR VIVKILDEND NKPQFLQKFY KIRLPEREKP 1270 1280 1290 1300 1310 1320 DRERNARREP LYHVIATDKD EGPNAEISYS IEDGNEHGKF FIEPKTGVVS SKRFSAAGEY 1330 1340 1350 1360 1370 1380 DILSIKAVDN GRPQKSSTTR LHIEWISKPK PSLEPISFEE SFFTFTVMES DPVAHMIGVI 1390 1400 1410 1420 1430 1440 SVEPPGIPLW FDITGGNYDS HFDVDKGTGT IIVAKPLDAE QKSNYNLTVE ATDGTTTILT 1450 1460 1470 1480 1490 1500 QVFIKVIDTN DHRPQFSTSK YEVVIPEDTA PETEILQISA VDQDEKNKLI YTLQSSRDPL 1510 1520 1530 1540 1550 1560 SLKKFRLDPA TGSLYTSEKL DHEAVHQHTL TVMVRDQDVP VKRNFARIVV NVSDTNDHAP 1570 1580 1590 1600 1610 1620 WFTASSYKGR VYESAAVGSV VLQVTALDKD KGKNAEVLYS IESGNIGNSF MIDPVLGSIK 1630 1640 1650 1660 1670 1680 TAKELDRSNQ AEYDLMVKAT DKGSPPMSEI TSVRIFVTIA DNASPKFTSK EYSVELSETV 1690 1700 1710 1720 1730 1740 SIGSFVGMVT AHSQSSVVYE IKDGNTGDAF DINPHSGTII TQKALDFETL PIYTLIIQGT 1750 1760 1770 1780 1790 1800 NMAGLSTNTT VLVHLQDEND NAPVFMQAEY TGLISESASI NSVVLTDRNV PLVIRAADAD 1810 1820 1830 1840 1850 1860 KDSNALLVYH IVEPSVHTYF AIDSSTGAIH TVLSLDYEET SIFHFTVQVH DMGTPRLFAE 1870 1880 1890 1900 1910 1920 YAANVTVHVI DINDCPPVFA KPLYEASLLL PTYKGVKVIT VNATDADSSA FSQLIYSITE 1930 1940 1950 1960 1970 1980 GNIGEKFSMD YKTGALTVQN TTQLRSRYEL TVRASDGRFA GLTSVKINVK ESKESHLKFT 1990 2000 2010 2020 2030 2040 QDVYSAVVKE NSTEAETLAV ITAIGNPINE PLFYHILNPD RRFKISRTSG VLSTTGTPFD 2050 2060 2070 2080 2090 2100 REQQEAFDVV VEVTEEHKPS AVAHVVVKVI VEDQNDNAPV FVNLPYYAVV KVDTEVGHVI 2110 2120 2130 2140 2150 2160 RYVTAVDRDS GRNGEVHYYL KEHHEHFQIG PLGEISLKKQ FELDTLNKEY LVTVVAKDGG 2170 2180 2190 2200 2210 2220 NPAFSAEVIV PITVMNKAMP VFEKPFYSAE IAESIQVHSP VVHVQANSPE GLKVFYSITD 2230 2240 2250 2260 2270 2280 GDPFSQFTIN FNTGVINVIA PLDFEAHPAY KLSIRATDSL TGAHAEVFVD IIVDDINDNP 2290 2300 2310 2320 2330 2340 PVFAQQSYAV TLSEASVIGT SVVQVRATDS DSEPNRGISY QMFGNHSKSH DHFHVDSSTG 2350 2360 2370 2380 2390 2400 LISLLRTLDY EQSRQHTIFV RAVDGGMPTL SSDVIVTVDV TDLNDNPPLF EQQIYEARIS 2410 2420 2430 2440 2450 2460 EHAPHGHFVT CVKAYDADSS DIDKLQYSIL SGNDHKHFVI DSATGIITLS NLHRHALKPF 2470 2480 2490 2500 2510 2520 YSLNLSVSDG VFRSSTQVHV TVIGGNLHSP AFLQNEYEVE LAENAPLHTL VMEVKTTDGD 2530 2540 2550 2560 2570 2580 SGIYGHVTYH IVNDFAKDRF YINERGQIFT LEKLDRETPA EKVISVRLMA KDAGGKVAFC 2590 2600 2610 2620 2630 2640 TVNVILTDDN DNAPQFRATK YEVNIGSSAA KGTSVVKVLA SDADEGSNAD ITYAIEADSE 2650 2660 2670 2680 2690 2700 SVKENLEINK LSGVITTKES LIGLENEFFT FFVRAVDNGS PSKESVVLVY VKILPPEMQL 2710 2720 2730 2740 2750 2760 PKFSEPFYTF TVSEDVPIGT EIDLIRAEHS GTVLYSLVKG NTPESNRDES FVIDRQSGRL 2770 2780 2790 2800 2810 2820 KLEKSLDHET TKWYQFSILA RCTQDDHEMV ASVDVSIQVK DANDNSPVFE SSPYEAFIVE 2830 2840 2850 2860 2870 2880 NLPGGSRVIQ IRASDADSGT NGQVMYSLDQ SQSVEVIESF AINMETGWIT TLKELDHEKR 2890 2900 2910 2920 2930 2940 DNYQIKVVAS DHGEKIQLSS TAIVDVTVTD VNDSPPRFTA EIYKGTVSED DPQGGVIAIL 2950 2960 2970 2980 2990 3000 STTDADSEEI NRQVTYFITG GDPLGQFAVE TIQNEWKVYV KKPLDREKRD NYLLTITATD 3010 3020 3030 3040 3050 3060 GTFSSKAIVE VKVLDANDNS PVCEKTLYSD TIPEDVLPGK LIMQISATDA DIRSNAEITY 3070 3080 3090 3100 3110 3120 TLLGSGAEKF KLNPDTGELK TSTPLDREEQ AVYHLLVRAT DGGGRFCQAS IVLTLEDVND 3130 3140 3150 3160 3170 3180 NAPEFSADPY AITVFENTEP GTLLTRVQAT DADAGLNRKI LYSLIDSADG QFSINELSGI 3190 3200 3210 3220 3230 3240 IQLEKPLDRE LQAVYTLSLK AVDQGLPRRL TATGTVIVSV LDINDNPPVF EYREYGATVS 3250 3260 3270 3280 3290 3300 EDILVGTEVL QVYAASRDIE ANAEITYSII SGNEHGKFSI DSKTGAVFII ENLDYESSHE 3310 3320 3330 3340 3350 3360 YYLTVEATDG GTPSLSDVAT VNVNVTDIND NTPVFSQDTY TTVISEDAVL EQSVITVMAD 3370 3380 3390 3400 3410 3420 DADGPSNSHI HYSIIDGNQG SSFTIDPVRG EVKVTKLLDR ETISGYTLTV QASDNGSPPR 3430 3440 3450 3460 3470 3480 VNTTTVNIDV SDVNDNAPVF SRGNYSVIIQ ENKPVGFSVL QLVVTDEDSS HNGPPFFFTI 3490 3500 3510 3520 3530 3540 VTGNDEKAFE VNPQGVLLTS SAIKRKEKDH YLLQVKVADN GKPQLSSLTY IDIRVIEESI 3550 3560 3570 3580 3590 3600 YPPAILPLEI FITSSGEEYS GGVIGKIHAT DQDVYDTLTY SLDPQMDNLF SVSSTGGKLI 3610 3620 3630 3640 3650 3660 AHKKLDIGQY LLNVSVTDGK FTTVADITVH IRQVTQEMLN HTIAIRFANL TPEEFVGDYW 3670 3680 3690 3700 3710 3720 RNFQRALRNI LGVRRNDIQI VSLQSSEPHP HLDVLLFVEK PGSAQISTKQ LLHKINSSVT 3730 3740 3750 3760 3770 3780 DIEEIIGVRI LNVFQKLCAG LDCPWKFCDE KVSVDESVMS THSTARLSFV TPRHHRAAVC 3790 3800 3810 3820 3830 3840 LCKEGRCPPV HHGCEDDPCP EGSECVSDPW EEKHTCVCPS GRFGQCPGSS SMTLTGNSYV 3850 3860 3870 3880 3890 3900 KYRLTENENK LEMKLTMRLR TYSTHAVVMY ARGTDYSILE IHHGRLQYKF DCGSGPGIVS 3910 3920 3930 3940 3950 3960 VQSIQVNDGQ WHAVALEVNG NYARLVLDQV HTASGTAPGT LKTLNLDNYV FFGGHIRQQG 3970 3980 3990 4000 4010 4020 TRHGRSPQVG NGFRGCMDSI YLNGQELPLN SKPRSYAHIE ESVDVSPGCF LTATEDCASN 4030 4040 4050 4060 4070 4080 PCQNGGVCNP SPAGGYYCKC SALYIGTHCE ISVNPCSSKP CLYGGTCVVD NGGFVCQCRG 4090 4100 4110 4120 4130 4140 LYTGQRCQLS PYCKDEPCKN GGTCFDSLDG AVCQCDSGFR GERCQSDIDE CSGNPCLHGA 4150 4160 4170 4180 4190 4200 LCENTHGSYH CNCSHEYRGR HCEDAAPNQY VSTPWNIGLA EGIGIVVFVA GIFLLVVVFV 4210 4220 4230 4240 4250 4260 LCRKMISRKK KHQAEPKDKH LGPATAFLQR PYFDSKLNKN IYSDIPPQVP VRPISYTPSI 4270 4280 4290 4300 4310 4320 PSDSRNNLDR NSFEGSAIPE HPEFSTFNPE SVHGHRKAVA VCSVAPNLPP PPPSNSPSDS 4330 4340 4350 4360 4370 4380 DSIQKPSWDF DYDTKVVDLD PCLSKKPLEE KPSQPYSARE SLSEVQSLSS FQSESCDDNG 4390 4400 4410 4420 4430 4440 YHWDTSDWMP SVPLPDIQEF PNYEVIDEQT PLYSADPNAI DTDYYPGGYD IESDFPPPPE 4450 4460 4470 4480 4490 4500 DFPAADELPP LPPEFSNQFE SIHPPRDMPA AGSLGSSSRN RQRFNLNQYL PNFYPLDMSE 4510 4520 4530 4540 4550 4560 PQTKGTGENS TCREPHAPYP PGYQRHFEAP AVESMPMSVY ASTASCSDVS ACCEVESEVM 4570 4580 MSDYESGDDG HFEEVTIPPL DSQQHTEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X87241 mRNA. Translation: CAA60685.1. AC107050 Genomic DNA. No translation available. AC110761 Genomic DNA. No translation available.
IPI	IPI00940698.
RefSeq	NP_005236.2. NM_005245.3.
UniGene	Hs.481371.
3D structure databases
ProteinModelPortal	Q14517.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14517. 2 interactions.
MINT	MINT-2806731.
STRING	9606.ENSP00000406229.
PTM databases
PhosphoSite	Q14517.
Polymorphism databases
DMDM	8928104.
Proteomic databases
PaxDb	Q14517.
PRIDE	Q14517.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000441802; ENSP00000406229; ENSG00000083857.
GeneID	2195.
KEGG	hsa:2195.
UCSC	uc003izf.3. human.
Organism-specific databases
CTD	2195.
GeneCards	GC04M187508.
HGNC	HGNC:3595. FAT1.
HPA	HPA001869. HPA023882.
MIM	600976. gene.
neXtProt	NX_Q14517.
PharmGKB	PA164719952.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000046499.
HOVERGEN	HBG005641.
InParanoid	Q14517.
KO	K16506.
Gene expression databases
ArrayExpress	Q14517.
Bgee	Q14517.
CleanEx	HS_FAT1.
Genevestigator	Q14517.
GermOnline	ENSG00000083857. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 2 hits. 2.60.40.60. 33 hits.
InterPro	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. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR001791. Laminin_G. [Graphical view]
Pfam	PF00028. Cadherin. 29 hits. PF00008. EGF. 2 hits. PF07645. EGF_CA. 1 hit. PF02210. Laminin_G_2. 1 hit. [Graphical view]
PRINTS	PR00205. CADHERIN.
SMART	SM00112. CA. 34 hits. SM00181. EGF. 3 hits. SM00179. EGF_CA. 1 hit. SM00282. LamG. 1 hit. [Graphical view]
SUPFAM	SSF49313. Cadherin. 33 hits. SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChiTaRS	FAT1. human.
GenomeRNAi	2195.
NextBio	8873.
SOURCE	Search...

Entry information

Entry name

FAT1_HUMAN

Accession

Primary (citable) accession number: Q14517

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 31, 2011
Last modified:	April 3, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.