Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8NI35

- INADL_HUMAN

UniProt

Q8NI35 - INADL_HUMAN

Protein

InaD-like protein

Gene

INADL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions. May regulate the surface expression and/or function of ASIC3 in sensory neurons.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell-cell junction organization Source: Reactome
    2. cell junction assembly Source: Reactome
    3. intracellular signal transduction Source: UniProtKB
    4. tight junction assembly Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_19373. Tight junction interactions.
    SignaLinkiQ8NI35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    InaD-like protein
    Short name:
    Inadl protein
    Short name:
    hINADL
    Alternative name(s):
    Pals1-associated tight junction protein
    Protein associated to tight junctions
    Gene namesi
    Name:INADL
    Synonyms:PATJ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28881. INADL.

    Subcellular locationi

    Membrane. Cell junctiontight junction. Apical cell membrane. Cytoplasmperinuclear region
    Note: Localized in the paranodal region of myelinating Schwann cells By similarity. Membrane-associated. Localizes to tight junctions in epithelial cells. Also found at the apical plasma membrane.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. perinuclear region of cytoplasm Source: UniProtKB
    4. plasma membrane Source: Reactome
    5. protein complex Source: Ensembl
    6. tight junction Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191L → W: Reduces L27 domain binding affinity to MPP5 L27 domain. 1 Publication
    Mutagenesisi38 – 381F → W: Reduces L27 domain binding affinity to MPP5 L27 domain. 1 Publication

    Organism-specific databases

    PharmGKBiPA134919267.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18011801InaD-like proteinPRO_0000094592Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei522 – 5221Phosphoserine1 Publication
    Modified residuei645 – 6451Phosphoserine1 Publication
    Modified residuei1209 – 12091Phosphothreonine1 Publication
    Modified residuei1212 – 12121Phosphoserine3 Publications
    Modified residuei1508 – 15081Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8NI35.
    PaxDbiQ8NI35.
    PRIDEiQ8NI35.

    PTM databases

    PhosphoSiteiQ8NI35.

    Expressioni

    Tissue specificityi

    Expressed in bladder, testis, ovary, small intestine, colon, heart, skeletal muscle, pancreas and cerebellum in the brain.2 Publications

    Gene expression databases

    ArrayExpressiQ8NI35.
    BgeeiQ8NI35.
    GenevestigatoriQ8NI35.

    Interactioni

    Subunit structurei

    Interacts with ASIC3, KCNJ10, KCNJ15, GRIN2A, GRIN2B, GRIN2C, GRIN2D, NLGN2, MPP7, HTR2A and SLC6A4 By similarity. Forms a ternary complex with MPP5, CRB1 and CRB3. Interacts with TJP3/ZO-3 and CLDN1/claudin-1. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Directly interacts with HTR4 By similarity. Interacts (via PDZ domain 8) with WWC1 (via the ADDV motif).By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRB1P822792EBI-724390,EBI-1048648
    MPP5Q8N3R94EBI-724390,EBI-2513978
    NF2P352402EBI-724390,EBI-1014472

    Protein-protein interaction databases

    BioGridi115502. 20 interactions.
    IntActiQ8NI35. 19 interactions.
    MINTiMINT-237883.

    Structurei

    Secondary structure

    1
    1801
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2614
    Helixi32 – 4312
    Helixi45 – 6723
    Helixi119 – 1279
    Beta strandi131 – 1388
    Beta strandi141 – 1433
    Beta strandi148 – 1536
    Beta strandi155 – 1584
    Beta strandi160 – 1656
    Helixi172 – 1754
    Beta strandi184 – 1907
    Helixi199 – 20810
    Beta strandi211 – 2199
    Beta strandi244 – 2529
    Beta strandi260 – 2634
    Beta strandi266 – 27510
    Helixi281 – 2844
    Beta strandi292 – 2987
    Helixi306 – 31611
    Beta strandi318 – 32710
    Beta strandi361 – 3688
    Beta strandi378 – 3836
    Beta strandi387 – 3893
    Beta strandi394 – 4007
    Helixi405 – 4095
    Beta strandi417 – 4215
    Helixi431 – 44010
    Beta strandi443 – 45715
    Beta strandi685 – 6917
    Beta strandi697 – 7048
    Beta strandi712 – 7198
    Helixi724 – 7285
    Beta strandi736 – 7427
    Helixi750 – 75910
    Beta strandi762 – 7709
    Beta strandi1058 – 10614
    Beta strandi1067 – 10715
    Beta strandi1075 – 10773
    Beta strandi1081 – 10833
    Beta strandi1101 – 11077
    Beta strandi1109 – 11113
    Turni1112 – 11143
    Beta strandi1124 – 11307
    Helixi1138 – 11469
    Beta strandi1150 – 11567
    Helixi1219 – 12213
    Helixi1223 – 12297
    Beta strandi1233 – 124311
    Beta strandi1251 – 12544
    Beta strandi1256 – 12583
    Beta strandi1264 – 12696
    Helixi1274 – 12785
    Beta strandi1289 – 12924
    Helixi1300 – 130910
    Beta strandi1312 – 13209
    Helixi1324 – 13274
    Beta strandi1425 – 14273
    Beta strandi1436 – 14416
    Beta strandi1460 – 14634
    Beta strandi1469 – 14713
    Helixi1472 – 14765
    Beta strandi1484 – 14885
    Beta strandi1494 – 14963
    Helixi1498 – 15069
    Beta strandi1510 – 15178

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VF6X-ray2.10A/B9-67[»]
    2D92NMR-A676-770[»]
    2DAZNMR-A1219-1329[»]
    2DB5NMR-A114-228[»]
    2DLUNMR-A238-335[»]
    2DM8NMR-A1425-1527[»]
    2DMZNMR-A355-470[»]
    2EHRNMR-A1058-1167[»]
    ProteinModelPortaliQ8NI35.
    SMRiQ8NI35. Positions 10-67, 116-473, 569-638, 675-770, 1054-1198, 1219-1332, 1389-1765.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8NI35.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6565L27PROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 22188PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini248 – 32881PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini365 – 45389PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini553 – 63987PDZ 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini686 – 77287PDZ 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1068 – 116093PDZ 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1239 – 132284PDZ 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1437 – 152084PDZ 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1533 – 161583PDZ 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1676 – 176287PDZ 10PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The L27 domain (also called Maguk recruitment domain) is required for interaction with MPP5 and CRB3, and MPP5 localization to tight junctions.
    The PDZ domain 6 mediates interaction with the C-terminus of TJP3 and is crucial for localization to the tight junctions. The PDZ domain 8 interacts with CLDN1 but is not required for proper localization.

    Sequence similaritiesi

    Contains 1 L27 domain.PROSITE-ProRule annotation
    Contains 10 PDZ (DHR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG252837.
    HOVERGENiHBG080134.
    KOiK06092.
    OMAiEAWEMHE.
    OrthoDBiEOG72ZCD0.
    PhylomeDBiQ8NI35.
    TreeFamiTF330709.

    Family and domain databases

    Gene3Di2.30.42.10. 10 hits.
    InterProiIPR004172. L27.
    IPR015132. L27_2.
    IPR001478. PDZ.
    [Graphical view]
    PfamiPF09045. L27_2. 1 hit.
    PF00595. PDZ. 10 hits.
    [Graphical view]
    SMARTiSM00569. L27. 1 hit.
    SM00228. PDZ. 10 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 10 hits.
    PROSITEiPS51022. L27. 1 hit.
    PS50106. PDZ. 10 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NI35-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPENPATDKL QVLQVLDRLK MKLQEKGDTS QNEKLSMFYE TLKSPLFNQI     50
    LTLQQSIKQL KGQLNHIPSD CSANFDFSRK GLLVFTDGSI TNGNVHRPSN 100
    NSTVSGLFPW TPKLGNEDFN SVIQQMAQGR QIEYIDIERP STGGLGFSVV 150
    ALRSQNLGKV DIFVKDVQPG SVADRDQRLK ENDQILAINH TPLDQNISHQ 200
    QAIALLQQTT GSLRLIVARE PVHTKSSTSS SLNDTTLPET VCWGHVEEVE 250
    LINDGSGLGF GIVGGKTSGV VVRTIVPGGL ADRDGRLQTG DHILKIGGTN 300
    VQGMTSEQVA QVLRNCGNSV RMLVARDPAG DISVTPPAPA ALPVALPTVA 350
    SKGPGSDSSL FETYNVELVR KDGQSLGIRI VGYVGTSHTG EASGIYVKSI 400
    IPGSAAYHNG HIQVNDKIVA VDGVNIQGFA NHDVVEVLRN AGQVVHLTLV 450
    RRKTSSSTSP LEPPSDRGTV VEPLKPPALF LTGAVETETN VDGEDEEIKE 500
    RIDTLKNDNI QALEKLEKVP DSPENELKSR WENLLGPDYE VMVATLDTQI 550
    ADDAELQKYS KLLPIHTLRL GVEVDSFDGH HYISSIVSGG PVDTLGLLQP 600
    EDELLEVNGM QLYGKSRREA VSFLKEVPPP FTLVCCRRLF DDEASVDEPR 650
    RTETSLPETE VDHNMDVNTE EDDDGELALW SPEVKIVELV KDCKGLGFSI 700
    LDYQDPLDPT RSVIVIRSLV ADGVAERSGG LLPGDRLVSV NEYCLDNTSL 750
    AEAVEILKAV PPGLVHLGIC KPLVEDNEEE SCYILHSSSN EDKTEFSGTI 800
    HDINSSLILE APKGFRDEPY FKEELVDEPF LDLGKSFHSQ QKEIEQSKEA 850
    WEMHEFLTPR LQEMDEEREI LVDEEYELYQ DPSPSMELYP LSHIQEATPV 900
    PSVNELHFGT QWLHDNEPSE SQEARTGRTV YSQEAQPYGY CPENVMKENF 950
    VMESLPSVPS TEGNSQQGRF DDLENLNSLA KTSLDLGMIP NDVQGPSLLI 1000
    DLPVVAQRRE QEDLPLYQHQ ATRVISKASA YTGMLSSRYA TDTCELPERE 1050
    EGEGEETPNF SHWGPPRIVE IFREPNVSLG ISIVGGQTVI KRLKNGEELK 1100
    GIFIKQVLED SPAGKTNALK TGDKILEVSG VDLQNASHSE AVEAIKNAGN 1150
    PVVFIVQSLS STPRVIPNVH NKANKITGNQ NQDTQEKKEK RQGTAPPPMK 1200
    LPPPYKALTD DSDENEEEDA FTDQKIRQRY ADLPGELHII ELEKDKNGLG 1250
    LSLAGNKDRS RMSIFVVGIN PEGPAAADGR MRIGDELLEI NNQILYGRSH 1300
    QNASAIIKTA PSKVKLVFIR NEDAVNQMAV TPFPVPSSSP SSIEDQSGTE 1350
    PISSEEDGSV EVGIKQLPES ESFKLAVSQM KQQKYPTKVS FSSQEIPLAP 1400
    ASSYHSTDAD FTGYGGFQAP LSVDPATCPI VPGQEMIIEI SKGRSGLGLS 1450
    IVGGKDTPLN AIVIHEVYEE GAAARDGRLW AGDQILEVNG VDLRNSSHEE 1500
    AITALRQTPQ KVRLVVYRDE AHYRDEENLE IFPVDLQKKA GRGLGLSIVG 1550
    KRNGSGVFIS DIVKGGAADL DGRLIQGDQI LSVNGEDMRN ASQETVATIL 1600
    KCAQGLVQLE IGRLRAGSWT SARTTSQNSQ GSQQSAHSSC HPSFAPVITG 1650
    LQNLVGTKRV SDPSQKNSGT DMEPRTVEIN RELSDALGIS IAGGRGSPLG 1700
    DIPVFIAMIQ ASGVAARTQK LKVGDRIVSI NGQPLDGLSH ADVVNLLKNA 1750
    YGRIILQVVA DTNISAIAAQ LENMSTGYHL GSPTAEHHPE DTEEQLQMTA 1800
    D 1801
    Length:1,801
    Mass (Da):196,368
    Last modified:October 17, 2006 - v3
    Checksum:i313DD1F12B6AD80A
    GO
    Isoform 2 (identifier: Q8NI35-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1459-1459: L → LFWRLGSPRAWSQHLVRAFMLHHPVTEVEGQ
         1553-1801: Missing.

    Show »
    Length:1,582
    Mass (Da):173,793
    Checksum:i9444B48DB84DE81E
    GO
    Isoform 3 (identifier: Q8NI35-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1553-1801: Missing.

    Show »
    Length:1,552
    Mass (Da):170,238
    Checksum:i646145A57C61152A
    GO
    Isoform 4 (identifier: Q8NI35-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1460-1487: Missing.
         1553-1801: Missing.

    Show »
    Length:1,524
    Mass (Da):167,159
    Checksum:i5203884719B4B152
    GO
    Isoform 5 (identifier: Q8NI35-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-541: Missing.
         1631-1675: GSQQSAHSSC...KNSGTDMEPR → SAECTQQLSS...FRHRYGTKDC
         1676-1801: Missing.

    Show »
    Length:1,134
    Mass (Da):125,231
    Checksum:i2717B2D492419866
    GO

    Sequence cautioni

    The sequence CAH70416.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI21733.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI22258.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1443 – 14431G → R in CAA04666. (PubMed:9280290)Curated
    Sequence conflicti1699 – 16991L → I in AAM28433. (PubMed:11927608)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti303 – 3031G → R.
    Corresponds to variant rs3762321 [ dbSNP | Ensembl ].
    VAR_027988
    Natural varianti362 – 3621E → A.
    Corresponds to variant rs1286823 [ dbSNP | Ensembl ].
    VAR_027989
    Natural varianti400 – 4001I → V.
    Corresponds to variant rs7516332 [ dbSNP | Ensembl ].
    VAR_027990
    Natural varianti599 – 5991Q → H.
    Corresponds to variant rs1286812 [ dbSNP | Ensembl ].
    VAR_027991
    Natural varianti744 – 7441C → R.1 Publication
    Corresponds to variant rs1134764 [ dbSNP | Ensembl ].
    VAR_022695
    Natural varianti779 – 7791E → K.
    Corresponds to variant rs12141598 [ dbSNP | Ensembl ].
    VAR_027992
    Natural varianti780 – 7801E → K.
    Corresponds to variant rs12141599 [ dbSNP | Ensembl ].
    VAR_027993
    Natural varianti870 – 8701I → M.3 Publications
    Corresponds to variant rs2799627 [ dbSNP | Ensembl ].
    VAR_027994
    Natural varianti1178 – 11781G → S.1 Publication
    Corresponds to variant rs1056513 [ dbSNP | Ensembl ].
    VAR_027995
    Natural varianti1282 – 12821R → H.2 Publications
    Corresponds to variant rs1134767 [ dbSNP | Ensembl ].
    VAR_027996
    Natural varianti1360 – 13601V → L.2 Publications
    Corresponds to variant rs2498982 [ dbSNP | Ensembl ].
    VAR_027997
    Natural varianti1504 – 15041A → P.
    Corresponds to variant rs13376115 [ dbSNP | Ensembl ].
    VAR_027998

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 541541Missing in isoform 5. 1 PublicationVSP_014204Add
    BLAST
    Alternative sequencei1459 – 14591L → LFWRLGSPRAWSQHLVRAFM LHHPVTEVEGQ in isoform 2. 1 PublicationVSP_014205
    Alternative sequencei1460 – 148728Missing in isoform 4. 1 PublicationVSP_014206Add
    BLAST
    Alternative sequencei1553 – 1801249Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_014207Add
    BLAST
    Alternative sequencei1631 – 167545GSQQS…DMEPR → SAECTQQLSSLLRSCHHWPA KPGWHKKSFRSFPEKFRHRY GTKDC in isoform 5. 1 PublicationVSP_014208Add
    BLAST
    Alternative sequencei1676 – 1801126Missing in isoform 5. 1 PublicationVSP_014209Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001306 mRNA. Translation: CAA04666.1.
    AJ224747 mRNA. Translation: CAA12112.1.
    AJ224748 mRNA. Translation: CAA12113.1.
    AB044807 mRNA. Translation: BAB19683.1.
    AF397170 mRNA. Translation: AAM28433.1.
    AL590374, AL136458, AL353802 Genomic DNA. Translation: CAH70416.1. Sequence problems.
    AL590374
    , AC097064, AL136458, AL353802, AL449143 Genomic DNA. Translation: CAH70418.1.
    AL590374
    , AC097064, AL136458, AL353802, AL449143 Genomic DNA. Translation: CAH70420.1.
    AL353802, AL136458, AL590374 Genomic DNA. Translation: CAI22258.1. Sequence problems.
    AL353802
    , AC097064, AL136458, AL449143, AL590374 Genomic DNA. Translation: CAI22260.1.
    AL353802
    , AC097064, AL136458, AL449143, AL590374 Genomic DNA. Translation: CAI22262.1.
    AL449143
    , AC097064, AL136458, AL353802, AL590374 Genomic DNA. Translation: CAI15923.1.
    AL449143
    , AC097064, AL136458, AL353802, AL590374 Genomic DNA. Translation: CAI15925.1.
    AL136458, AL353802, AL590374 Genomic DNA. Translation: CAI21733.1. Sequence problems.
    AL136458
    , AC097064, AL353802, AL449143, AL590374 Genomic DNA. Translation: CAI21734.1.
    AL136458
    , AC097064, AL353802, AL449143, AL590374 Genomic DNA. Translation: CAI21737.1.
    BC021135 mRNA. Translation: AAH21135.1.
    CCDSiCCDS617.2. [Q8NI35-1]
    RefSeqiNP_795352.2. NM_176877.2.
    UniGeneiHs.478125.

    Genome annotation databases

    EnsembliENST00000316485; ENSP00000326199; ENSG00000132849. [Q8NI35-2]
    ENST00000371158; ENSP00000360200; ENSG00000132849. [Q8NI35-1]
    ENST00000484937; ENSP00000433669; ENSG00000132849. [Q8NI35-5]
    GeneIDi10207.
    KEGGihsa:10207.
    UCSCiuc001daa.2. human. [Q8NI35-4]
    uc001dab.3. human. [Q8NI35-1]
    uc009waf.1. human. [Q8NI35-2]

    Polymorphism databases

    DMDMi116242542.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001306 mRNA. Translation: CAA04666.1 .
    AJ224747 mRNA. Translation: CAA12112.1 .
    AJ224748 mRNA. Translation: CAA12113.1 .
    AB044807 mRNA. Translation: BAB19683.1 .
    AF397170 mRNA. Translation: AAM28433.1 .
    AL590374 , AL136458 , AL353802 Genomic DNA. Translation: CAH70416.1 . Sequence problems.
    AL590374
    , AC097064 , AL136458 , AL353802 , AL449143 Genomic DNA. Translation: CAH70418.1 .
    AL590374
    , AC097064 , AL136458 , AL353802 , AL449143 Genomic DNA. Translation: CAH70420.1 .
    AL353802 , AL136458 , AL590374 Genomic DNA. Translation: CAI22258.1 . Sequence problems.
    AL353802
    , AC097064 , AL136458 , AL449143 , AL590374 Genomic DNA. Translation: CAI22260.1 .
    AL353802
    , AC097064 , AL136458 , AL449143 , AL590374 Genomic DNA. Translation: CAI22262.1 .
    AL449143
    , AC097064 , AL136458 , AL353802 , AL590374 Genomic DNA. Translation: CAI15923.1 .
    AL449143
    , AC097064 , AL136458 , AL353802 , AL590374 Genomic DNA. Translation: CAI15925.1 .
    AL136458 , AL353802 , AL590374 Genomic DNA. Translation: CAI21733.1 . Sequence problems.
    AL136458
    , AC097064 , AL353802 , AL449143 , AL590374 Genomic DNA. Translation: CAI21734.1 .
    AL136458
    , AC097064 , AL353802 , AL449143 , AL590374 Genomic DNA. Translation: CAI21737.1 .
    BC021135 mRNA. Translation: AAH21135.1 .
    CCDSi CCDS617.2. [Q8NI35-1 ]
    RefSeqi NP_795352.2. NM_176877.2.
    UniGenei Hs.478125.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VF6 X-ray 2.10 A/B 9-67 [» ]
    2D92 NMR - A 676-770 [» ]
    2DAZ NMR - A 1219-1329 [» ]
    2DB5 NMR - A 114-228 [» ]
    2DLU NMR - A 238-335 [» ]
    2DM8 NMR - A 1425-1527 [» ]
    2DMZ NMR - A 355-470 [» ]
    2EHR NMR - A 1058-1167 [» ]
    ProteinModelPortali Q8NI35.
    SMRi Q8NI35. Positions 10-67, 116-473, 569-638, 675-770, 1054-1198, 1219-1332, 1389-1765.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115502. 20 interactions.
    IntActi Q8NI35. 19 interactions.
    MINTi MINT-237883.

    PTM databases

    PhosphoSitei Q8NI35.

    Polymorphism databases

    DMDMi 116242542.

    Proteomic databases

    MaxQBi Q8NI35.
    PaxDbi Q8NI35.
    PRIDEi Q8NI35.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316485 ; ENSP00000326199 ; ENSG00000132849 . [Q8NI35-2 ]
    ENST00000371158 ; ENSP00000360200 ; ENSG00000132849 . [Q8NI35-1 ]
    ENST00000484937 ; ENSP00000433669 ; ENSG00000132849 . [Q8NI35-5 ]
    GeneIDi 10207.
    KEGGi hsa:10207.
    UCSCi uc001daa.2. human. [Q8NI35-4 ]
    uc001dab.3. human. [Q8NI35-1 ]
    uc009waf.1. human. [Q8NI35-2 ]

    Organism-specific databases

    CTDi 10207.
    GeneCardsi GC01P062208.
    HGNCi HGNC:28881. INADL.
    MIMi 603199. gene.
    neXtProti NX_Q8NI35.
    PharmGKBi PA134919267.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252837.
    HOVERGENi HBG080134.
    KOi K06092.
    OMAi EAWEMHE.
    OrthoDBi EOG72ZCD0.
    PhylomeDBi Q8NI35.
    TreeFami TF330709.

    Enzyme and pathway databases

    Reactomei REACT_19373. Tight junction interactions.
    SignaLinki Q8NI35.

    Miscellaneous databases

    ChiTaRSi INADL. human.
    EvolutionaryTracei Q8NI35.
    GeneWikii INADL.
    GenomeRNAii 10207.
    NextBioi 38644.
    PROi Q8NI35.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NI35.
    Bgeei Q8NI35.
    Genevestigatori Q8NI35.

    Family and domain databases

    Gene3Di 2.30.42.10. 10 hits.
    InterProi IPR004172. L27.
    IPR015132. L27_2.
    IPR001478. PDZ.
    [Graphical view ]
    Pfami PF09045. L27_2. 1 hit.
    PF00595. PDZ. 10 hits.
    [Graphical view ]
    SMARTi SM00569. L27. 1 hit.
    SM00228. PDZ. 10 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 10 hits.
    PROSITEi PS51022. L27. 1 hit.
    PS50106. PDZ. 10 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of a novel PDZ domain protein with homology to INAD from Drosophila melanogaster."
      Philipp S., Flockerzi V.
      FEBS Lett. 413:243-248(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY, VARIANTS ARG-744; MET-870; HIS-1282 AND LEU-1360.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANTS MET-870; HIS-1282 AND LEU-1360.
    3. "The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost."
      Roh M.H., Makarova O., Liu C.-J., Shin K., Lee S., Laurinec S., Goyal M., Wiggins R., Margolis B.
      J. Cell Biol. 157:161-172(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MPP5 AND CRB1, SUBCELLULAR LOCATION, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, VARIANTS MET-870 AND SER-1178.
      Tissue: Kidney.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1456-1801 (ISOFORM 1).
      Tissue: Skin.
    6. "hINADl/PATJ, a homolog of discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells."
      Lemmers C., Medina E., Delgrossi M.-H., Michel D., Arsanto J.-P., Le Bivic A.
      J. Biol. Chem. 277:25408-25415(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH CRB1 AND CRB3.
    7. "The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions."
      Roh M.H., Liu C.-J., Laurinec S., Margolis B.
      J. Biol. Chem. 277:27501-27509(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAINS, INTERACTION WITH TJP3 AND CLDN1.
    8. "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
      Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
      Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; AMOT; MPP5 AND PARD3, INTERACTION WITH MPP7.
    9. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WWC1.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1209 AND SER-1212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-645; SER-1212 AND THR-1508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes."
      Li Y., Karnak D., Demeler B., Margolis B., Lavie A.
      EMBO J. 23:2723-2733(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 9-67, MUTAGENESIS OF LEU-19 AND PHE-38.
    16. "Solution structure of PDZ domains of INAD-like protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 114-470; 675-770 AND 1219-1527.

    Entry informationi

    Entry nameiINADL_HUMAN
    AccessioniPrimary (citable) accession number: Q8NI35
    Secondary accession number(s): O15249
    , O43742, O60833, Q5VUA5, Q5VUA6, Q5VUA7, Q5VUA8, Q5VUA9, Q5VUB0, Q8WU78, Q9H3N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 112 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3