CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001192
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
 AAC23748.2; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAF75819.1; AAS47698.1; CAH70620.1; CAH70620.1; CAH70620.1; CAH71587.1; CAH71587.1; CAH71587.1; CAH71588.1; CAH71588.1; CAH71588.1; CAH71588.1; CAH71588.1; CAH71588.1; CAH71588.1; CAH71588.1; CAH71588.1; CAH73621.1; CAH73621.1; CAH73621.1; CAH73621.1; CAH73621.1; CAH73621.1; CAH73621.1; CAH73621.1; CAH73621.1; CAI23041.1; CAI23041.1; CAI23041.1; CAI23041.1; CAI23041.1; CAI23041.1; CAI23041.1; CAI23041.1; CAI23041.1; CAI19189.1; CAI19189.1; CAI19189.1; CAI19189.1; CAI19189.1; CAI19189.1; CAI19189.1; CAI19189.1; CAI19189.1; CAH70621.1; CAH70621.1; CAH70621.1; CAH70621.1; CAH70621.1; CAH70621.1; CAH70621.1; CAH70621.1; CAH70621.1 
Protein Name
 Usherin 
Protein Synonyms/Alias
 Usher syndrome type IIa protein; Usher syndrome type-2A protein 
Gene Name
 USH2A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1660RSYTILRKDPEIIQKubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 Involved in hearing and vision. 
Sequence Annotation
 DOMAIN 271 517 Laminin N-terminal.
 DOMAIN 518 574 Laminin EGF-like 1.
 DOMAIN 575 640 Laminin EGF-like 2.
 DOMAIN 641 693 Laminin EGF-like 3.
 DOMAIN 694 746 Laminin EGF-like 4.
 DOMAIN 747 794 Laminin EGF-like 5.
 DOMAIN 795 846 Laminin EGF-like 6.
 DOMAIN 847 899 Laminin EGF-like 7.
 DOMAIN 900 950 Laminin EGF-like 8.
 DOMAIN 951 1001 Laminin EGF-like 9.
 DOMAIN 1002 1052 Laminin EGF-like 10.
 DOMAIN 1058 1143 Fibronectin type-III 1.
 DOMAIN 1145 1238 Fibronectin type-III 2.
 DOMAIN 1242 1357 Fibronectin type-III 3.
 DOMAIN 1367 1462 Fibronectin type-III 4.
 DOMAIN 1517 1709 Laminin G-like 1.
 DOMAIN 1714 1891 Laminin G-like 2.
 DOMAIN 1871 1949 Fibronectin type-III 5.
 DOMAIN 1954 2051 Fibronectin type-III 6.
 DOMAIN 2052 2138 Fibronectin type-III 7.
 DOMAIN 2142 2236 Fibronectin type-III 8.
 DOMAIN 2241 2325 Fibronectin type-III 9.
 DOMAIN 2328 2432 Fibronectin type-III 10.
 DOMAIN 2435 2528 Fibronectin type-III 11.
 DOMAIN 2533 2619 Fibronectin type-III 12.
 DOMAIN 2621 2718 Fibronectin type-III 13.
 DOMAIN 2724 2812 Fibronectin type-III 14.
 DOMAIN 2821 2920 Fibronectin type-III 15.
 DOMAIN 2925 3015 Fibronectin type-III 16.
 DOMAIN 3020 3105 Fibronectin type-III 17.
 DOMAIN 3110 3200 Fibronectin type-III 18.
 DOMAIN 3404 3494 Fibronectin type-III 19.
 DOMAIN 3499 3585 Fibronectin type-III 20.
 DOMAIN 3590 3676 Fibronectin type-III 21.
 DOMAIN 3677 3767 Fibronectin type-III 22.
 DOMAIN 3768 3862 Fibronectin type-III 23.
 DOMAIN 3863 3960 Fibronectin type-III 24.
 DOMAIN 3961 4062 Fibronectin type-III 25.
 DOMAIN 4066 4150 Fibronectin type-III 26.
 DOMAIN 4154 4258 Fibronectin type-III 27.
 DOMAIN 4265 4351 Fibronectin type-III 28.
 DOMAIN 4356 4439 Fibronectin type-III 29.
 DOMAIN 4444 4528 Fibronectin type-III 30.
 DOMAIN 4529 4627 Fibronectin type-III 31.
 DOMAIN 4633 4730 Fibronectin type-III 32.
 DOMAIN 4732 4825 Fibronectin type-III 33.
 DOMAIN 4826 4927 Fibronectin type-III 34.
 DOMAIN 4928 5014 Fibronectin type-III 35.
 MOTIF 5200 5202 PDZ-binding.
 CARBOHYD 361 361 N-linked (GlcNAc...) (Potential).
 CARBOHYD 451 451 N-linked (GlcNAc...) (Potential).
 CARBOHYD 587 587 N-linked (GlcNAc...) (Potential).
 CARBOHYD 611 611 N-linked (GlcNAc...) (Potential).
 CARBOHYD 650 650 N-linked (GlcNAc...) (Potential).
 CARBOHYD 697 697 N-linked (GlcNAc...) (Potential).
 CARBOHYD 839 839 N-linked (GlcNAc...) (Potential).
 CARBOHYD 856 856 N-linked (GlcNAc...) (Potential).
 CARBOHYD 862 862 N-linked (GlcNAc...) (Potential).
 CARBOHYD 888 888 N-linked (GlcNAc...) (Potential).
 CARBOHYD 944 944 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1011 1011 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1071 1071 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1151 1151 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1174 1174 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1379 1379 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1388 1388 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1479 1479 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1635 1635 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1779 1779 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1903 1903 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2011 2011 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2014 2014 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2048 2048 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2130 2130 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2182 2182 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2195 2195 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2258 2258 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2285 2285 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2322 2322 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2377 2377 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2382 2382 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2407 2407 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2413 2413 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2581 2581 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2584 2584 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2656 2656 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2710 2710 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2770 2770 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2788 2788 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2930 2930 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2937 2937 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2970 2970 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3032 3032 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3099 3099 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3217 3217 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3330 3330 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3419 3419 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3433 3433 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3653 3653 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3694 3694 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3733 3733 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3780 3780 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3849 3849 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3984 3984 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4202 4202 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4226 4226 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4317 4317 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4418 4418 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4564 4564 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4583 4583 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4691 4691 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4754 4754 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4800 4800 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4943 4943 N-linked (GlcNAc...) (Potential).
 CARBOHYD 4950 4950 N-linked (GlcNAc...) (Potential).
 DISULFID 518 527 By similarity.
 DISULFID 520 536 By similarity.
 DISULFID 538 549 By similarity.
 DISULFID 552 572 By similarity.
 DISULFID 575 584 By similarity.
 DISULFID 577 605 By similarity.
 DISULFID 608 617 By similarity.
 DISULFID 620 638 By similarity.
 DISULFID 641 655 By similarity.
 DISULFID 643 662 By similarity.
 DISULFID 664 673 By similarity.
 DISULFID 676 691 By similarity.
 DISULFID 694 708 By similarity.
 DISULFID 696 715 By similarity.
 DISULFID 717 726 By similarity.
 DISULFID 729 744 By similarity.
 DISULFID 747 759 By similarity.
 DISULFID 749 766 By similarity.
 DISULFID 768 777 By similarity.
 DISULFID 780 792 By similarity.
 DISULFID 795 808 By similarity.
 DISULFID 797 815 By similarity.
 DISULFID 817 826 By similarity.
 DISULFID 829 844 By similarity.
 DISULFID 847 861 By similarity.
 DISULFID 849 868 By similarity.
 DISULFID 870 879 By similarity.
 DISULFID 882 897 By similarity.
 DISULFID 900 913 By similarity.
 DISULFID 902 920 By similarity.
 DISULFID 922 931 By similarity.
 DISULFID 934 948 By similarity.
 DISULFID 951 963 By similarity.
 DISULFID 953 970 By similarity.
 DISULFID 972 982 By similarity.
 DISULFID 985 999 By similarity.
 DISULFID 1002 1014 By similarity.
 DISULFID 1004 1021 By similarity.
 DISULFID 1023 1032 By similarity.
 DISULFID 1035 1050 By similarity.
 DISULFID 1672 1709 By similarity.
 DISULFID 1862 1891 By similarity.
 DISULFID 3371 3444 By similarity.
 DISULFID 3399 3425 By similarity.  
Keyword
 Alternative splicing; Cell membrane; Cell projection; Complete proteome; Deafness; Disease mutation; Disulfide bond; Glycoprotein; Hearing; Laminin EGF-like domain; Membrane; Polymorphism; Reference proteome; Repeat; Retinitis pigmentosa; Secreted; Sensory transduction; Signal; Transmembrane; Transmembrane helix; Usher syndrome; Vision. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 5202 AA 
Protein Sequence
MNCPVLSLGS GFLFQVIEML IFAYFASISL TESRGLFPRL ENVGAFKKVS IVPTQAVCGL 60
PDRSTFCHSS AAAESIQFCT QRFCIQDCPY RSSHPTYTAL FSAGLSSCIT PDKNDLHPNA 120
HSNSASFIFG NHKSCFSSPP SPKLMASFTL AVWLKPEQQG VMCVIEKTVD GQIVFKLTIS 180
EKETMFYYRT VNGLQPPIKV MTLGRILVKK WIHLSVQVHQ TKISFFINGV EKDHTPFNAR 240
TLSGSITDFA SGTVQIGQSL NGLEQFVGRM QDFRLYQVAL TNREILEVFS GDLLRLHAQS 300
HCRCPGSHPR VHPLAQRYCI PNDAGDTADN RVSRLNPEAH PLSFVNDNDV GTSWVSNVFT 360
NITQLNQGVT ISVDLENGQY QVFYIIIQFF SPQPTEIRIQ RKKENSLDWE DWQYFARNCG 420
AFGMKNNGDL EKPDSVNCLQ LSNFTPYSRG NVTFSILTPG PNYRPGYNNF YNTPSLQEFV 480
KATQIRFHFH GQYYTTETAV NLRHRYYAVD EITISGRCQC HGHADNCDTT SQPYRCLCSQ 540
ESFTEGLHCD RCLPLYNDKP FRQGDQVYAF NCKPCQCNSH SKSCHYNISV DPFPFEHFRG 600
GGGVCDDCEH NTTGRNCELC KDYFFRQVGA DPSAIDVCKP CDCDTVGTRN GSILCDQIGG 660
QCNCKRHVSG RQCNQCQNGF YNLQELDPDG CSPCNCNTSG TVDGDITCHQ NSGQCKCKAN 720
VIGLRCDHCN FGFKFLRSFN DVGCEPCQCN LHGSVNKFCN PHSGQCECKK EAKGLQCDTC 780
RENFYGLDVT NCKACDCDTA GSLPGTVCNA KTGQCICKPN VEGRQCNKCL EGNFYLRQNN 840
SFLCLPCNCD KTGTINGSLL CNKSTGQCPC KLGVTGLRCN QCEPHRYNLT IDNFQHCQMC 900
ECDSLGTLPG TICDPISGQC LCVPNRQGRR CNQCQPGFYI SPGNATGCLP CSCHTTGAVN 960
HICNSLTGQC VCQDASIAGQ RCDQCKDHYF GFDPQTGRCQ PCNCHLSGAL NETCHLVTGQ 1020
CFCKQFVTGS KCDACVPSAS HLDVNNLLGC SKTPFQQPPP RGQVQSSSAI NLSWSPPDSP 1080
NAHWLTYSLL RDGFEIYTTE DQYPYSIQYF LDTDLLPYTK YSYYIETTNV HGSTRSVAVT 1140
YKTKPGVPEG NLTLSYIIPI GSDSVTLTWT TLSNQSGPIE KYILSCAPLA GGQPCVSYEG 1200
HETSATIWNL VPFAKYDFSV QACTSGGCLH SLPITVTTAQ APPQRLSPPK MQKISSTELH 1260
VEWSPPAELN GIIIRYELYM RRLRSTKETT SEESRVFQSS GWLSPHSFVE SANENALKPP 1320
QTMTTITGLE PYTKYEFRVL AVNMAGSVSS AWVSERTGES APVFMIPPSV FPLSSYSLNI 1380
SWEKPADNVT RGKVVGYDIN MLSEQSPQQS IPMAFSQLLH TAKSQELSYT VEGLKPYRIY 1440
EFTITLCNSV GCVTSASGAG QTLAAAPAQL RPPLVKGINS TTIHLRWFPP EELNGPSPIY 1500
QLERRESSLP ALMTTMMKGI RFIGNGYCKF PSSTHPVNTD FTGIKASFRT KVPEGLIVFA 1560
ASPGNQEEYF ALQLKKGRLY FLFDPQGSPV EVTTTNDHGK QYSDGKWHEI IAIRHQAFGQ 1620
ITLDGIYTGS SAILNGSTVI GDNTGVFLGG LPRSYTILRK DPEIIQKGFV GCLKDVHFMK 1680
NYNPSAIWEP LDWQSSEEQI NVYNSWEGCP ASLNEGAQFL GAGFLELHPY MFHGGMNFEI 1740
SFKFRTDQLN GLLLFVYNKD GPDFLAMELK SGILTFRLNT SLAFTQVDLL LGLSYCNGKW 1800
NKVIIKKEGS FISASVNGLM KHASESGDQP LVVNSPVYVG GIPQELLNSY QHLCLEQGFG 1860
GCMKDVKFTR GAVVNLASVS SGAVRVNLDG CLSTDSAVNC RGNDSILVYQ GKEQSVYEGG 1920
LQPFTEYLYR VIASHEGGSV YSDWSRGRTT GAAPQSVPTP SRVRSLNGYS IEVTWDEPVV 1980
RGVIEKYILK AYSEDSTRPP RMPSASAEFV NTSNLTGILT GLLPFKNYAV TLTACTLAGC 2040
TESSHALNIS TPQEAPQEVQ PPVAKSLPSS LLLSWNPPKK ANGIITQYCL YMDGRLIYSG 2100
SEENYIVTDL AVFTPHQFLL SACTHVGCTN SSWVLLYTAQ LPPEHVDSPV LTVLDSRTIH 2160
IQWKQPRKIS GILERYVLYM SNHTHDFTIW SVIYNSTELF QDHMLQYVLP GNKYLIKLGA 2220
CTGGGCTVSE ASEALTDEDI PEGVPAPKAH SYSPDSFNVS WTEPEYPNGV ITSYGLYLDG 2280
ILIHNSSELS YRAYGFAPWS LHSFRVQACT AKGCALGPLV ENRTLEAPPE GTVNVFVKTQ 2340
GSRKAHVRWE APFRPNGLLT HSVLFTGIFY VDPVGNNYTL LNVTKVMYSG EETNLWVLID 2400
GLVPFTNYTV QVNISNSQGS LITDPITIAM PPGAPDGVLP PRLSSATPTS LQVVWSTPAR 2460
NNAPGSPRYQ LQMRSGDSTH GFLELFSNPS ASLSYEVSDL QPYTEYMFRL VASNGFGSAH 2520
SSWIPFMTAE DKPGPVVPPI LLDVKSRMML VTWQHPRKSN GVITHYNIYL HGRLYLRTPG 2580
NVTNCTVMHL HPYTAYKFQV EACTSKGCSL SPESQTVWTL PGAPEGIPSP ELFSDTPTSV 2640
IISWQPPTHP NGLVENFTIE RRVKGKEEVT TLVTLPRSHS MRFIDKTSAL SPWTKYEYRV 2700
LMSTLHGGTN SSAWVEVTTR PSRPAGVQPP VVTVLEPDAV QVTWKPPLIQ NGDILSYEIH 2760
MPDPHITLTN VTSAVLSQKV THLIPFTNYS VTIVACSGGN GYLGGCTESL PTYVTTHPTV 2820
PQNVGPLSVI PLSESYVVIS WQPPSKPNGP NLRYELLRRK IQQPLASNPP EDLNRWHNIY 2880
SGTQWLYEDK GLSRFTTYEY MLFVHNSVGF TPSREVTVTT LAGLPERGAN LTASVLNHTA 2940
IDVRWAKPTV QDLQGEVEYY TLFWSSATSN DSLKILPDVN SHVIGHLKPN TEYWIFISVF 3000
NGVHSINSAG LHATTCDGEP QGMLPPEVVI INSTAVRVIW TSPSNPNGVV TEYSIYVNNK 3060
LYKTGMNVPG SFILRDLSPF TIYDIQVEVC TIYACVKSNG TQITTVEDTP SDIPTPTIRG 3120
ITSRSLQIDW VSPRKPNGII LGYDLLWKTW YPCAKTQKLV QDQSDELCKA VRCQKPESIC 3180
GHICYSSEAK VCCNGVLYNP KPGHRCCEEK YIPFVLNSTG VCCGGRIQEA QPNHQCCSGY 3240
YARILPGEVC CPDEQHNRVS VGIGDSCCGR MPYSTSGNQI CCAGRLHDGH GQKCCGRQIV 3300
SNDLECCGGE EGVVYNRLPG MFCCGQDYVN MSDTICCSAS SGESKAHIKK NDPVPVKCCE 3360
TELIPKSQKC CNGVGYNPLK YVCSDKISTG MMMKETKECR ILCPASMEAT EHCGRCDFNF 3420
TSHICTVIRG SHNSTGKASI EEMCSSAEET IHTGSVNTYS YTDVNLKPYM TYEYRISAWN 3480
SYGRGLSKAV RARTKEDVPQ GVSPPTWTKI DNLEDTIVLN WRKPIQSNGP IIYYILLRNG 3540
IERFRGTSLS FSDKEGIQPF QEYSYQLKAC TVAGCATSSK VVAATTQGVP ESILPPSITA 3600
LSAVALHLSW SVPEKSNGVI KEYQIRQVGK GLIHTDTTDR RQHTVTGLQP YTNYSFTLTA 3660
CTSAGCTSSE PFLGQTLQAA PEGVWVTPRH IIINSTTVEL YWSLPEKPNG LVSQYQLSRN 3720
GNLLFLGGSE EQNFTDKNLE PNSRYTYKLE VKTGGGSSAS DDYIVQTPMS TPEEIYPPYN 3780
ITVIGPYSIF VAWIPPGILI PEIPVEYNVL LNDGSVTPLA FSVGHHQSTL LENLTPFTQY 3840
EIRIQACQNG SCGVSSRMFV KTPEAAPMDL NSPVLKALGS ACIEIKWMPP EKPNGIIINY 3900
FIYRRPAGIE EESVLFVWSE GALEFMDEGD TLRPFTLYEY RVRACNSKGS VESLWSLTQT 3960
LEAPPQDFPA PWAQATSAHS VLLNWTKPES PNGIISHYRV VYQERPDDPT FNSPTVHAFT 4020
VKGTSHQAHL YGLEPFTTYR IGVVAANHAG EILSPWTLIQ TLESSPSGLR NFIVEQKENG 4080
RALLLQWSEP MRTNGVIKTY NIFSDGFLEY SGLNRQFLFR RLDPFTLYTL TLEACTRAGC 4140
AHSAPQPLWT DEAPPDSQLA PTVHSVKSTS VELSWSEPVN PNGKIIRYEV IRRCFEGKAW 4200
GNQTIQADEK IVFTEYNTER NTFMYNDTGL QPWTQCEYKI YTWNSAGHTC SSWNVVRTLQ 4260
APPEGLSPPV ISYVSMNPQK LLISWIPPEQ SNGIIQSYRL QRNEMLYPFS FDPVTFNYTD 4320
EELLPFSTYS YALQACTSGG CSTSKPTSIT TLEAAPSEVS PPDLWAVSAT QMNVCWSPPT 4380
VQNGKITKYL VRYDNKESLA GQGLCLLVSH LQPYSQYNFS LVACTNGGCT ASVSKSAWTM 4440
EALPENMDSP TLQVTGSESI EITWKPPRNP NGQIRSYELR RDGTIVYTGL ETRYRDFTLT 4500
PGVEYSYTVT ASNSQGGILS PLVKDRTSPS APSGMEPPKL QARGPQEILV NWDPPVRTNG 4560
DIINYTLFIR ELFERETKII HINTTHNSFG MQSYIVNQLK PFHRYEIRIQ ACTTLGCASS 4620
DWTFIQTPEI APLMQPPPHL EVQMAPGGFQ PTVSLLWTGP LQPNGKVLYY ELYRRQIATQ 4680
PRKSNPVLIY NGSSTSFIDS ELLPFTEYEY QVWAVNSAGK APSSWTWCRT GPAPPEGLRA 4740
PTFHVISSTQ AVVNISAPGK PNGIVSLYRL FSSSAHGAET VLSEGMATQQ TLHGLQAFTN 4800
YSIGVEACTC FNCCSKGPTA ELRTHPAPPS GLSSPQIGTL ASRTASFRWS PPMFPNGVIH 4860
SYELQFHVAC PPDSALPCTP SQIETKYTGL GQKASLGGLQ PYTTYKLRVV AHNEVGSTAS 4920
EWISFTTQKE LPQYRAPFSV DSNLSVVCVN WSDTFLLNGQ LKEYVLTDGG RRVYSGLDTT 4980
LYIPRTADKT FFFQVICTTD EGSVKTPLIQ YDTSTGLGLV LTTPGKKKGS RSKSTEFYSE 5040
LWFIVLMAML GLILLAIFLS LILQRKIHKE PYIRERPPLV PLQKRMSPLN VYPPGENHMF 5100
DSVADISDVS SNVTLKSYTM HFEGLADTKI PRSGTPVSIR SNRSACVLRI PSQNQTSLTY 5160
SQGSLHRSVS QLMDIQDKKV LMDNSLWEAI MGHNSGLYVD EEDLMNAIKD FSSVTKERTT 5220
FTDTHL 5226 
Gene Ontology
 GO:0016324; C:apical plasma membrane; ISS:BHF-UCL.
 GO:0005604; C:basement membrane; IDA:HGNC.
 GO:0005737; C:cytoplasm; IDA:HGNC.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0002142; C:stereocilia ankle link complex; ISS:BHF-UCL.
 GO:0060171; C:stereocilium membrane; ISS:BHF-UCL.
 GO:0005518; F:collagen binding; IDA:HGNC.
 GO:0017022; F:myosin binding; ISS:BHF-UCL.
 GO:0035315; P:hair cell differentiation; ISS:BHF-UCL.
 GO:0060113; P:inner ear receptor cell differentiation; ISS:BHF-UCL.
 GO:0048496; P:maintenance of organ identity; IMP:HGNC.
 GO:0045494; P:photoreceptor cell maintenance; IMP:HGNC.
 GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
 GO:0007605; P:sensory perception of sound; IMP:HGNC. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR002049; EGF_laminin.
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR006558; LamG-like.
 IPR001791; Laminin_G.
 IPR008211; Laminin_N.
 IPR026915; USH2A. 
Pfam
 PF00041; fn3
 PF00053; Laminin_EGF
 PF02210; Laminin_G_2
 PF00055; Laminin_N 
SMART
 SM00180; EGF_Lam
 SM00060; FN3
 SM00282; LamG
 SM00560; LamGL
 SM00136; LamNT 
PROSITE
 PS00022; EGF_1
 PS01248; EGF_LAM_1
 PS50027; EGF_LAM_2
 PS50853; FN3
 PS50025; LAM_G_DOMAIN
 PS51117; LAMININ_NTER 
PRINTS