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Q8NI35 (INADL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:INADL
Synonyms:PATJ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1801 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

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). Ref.3 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

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. Ref.3 Ref.6 Ref.7 Ref.9

Tissue specificity

Expressed in bladder, testis, ovary, small intestine, colon, heart, skeletal muscle, pancreas and cerebellum in the brain. Ref.1 Ref.6

Domain

The L27 domain (also called Maguk recruitment domain) is required for interaction with MPP5 and CRB3, and MPP5 localization to tight junctions. Ref.3 Ref.6 Ref.7

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. Ref.3 Ref.6 Ref.7

Sequence similarities

Contains 1 L27 domain.

Contains 10 PDZ (DHR) domains.

Sequence caution

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.

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NI35-1)

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.
Isoform 2 (identifier: Q8NI35-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1459-1459: L → LFWRLGSPRAWSQHLVRAFMLHHPVTEVEGQ
     1553-1801: Missing.
Isoform 3 (identifier: Q8NI35-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1553-1801: Missing.
Isoform 4 (identifier: Q8NI35-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1460-1487: Missing.
     1553-1801: Missing.
Isoform 5 (identifier: Q8NI35-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18011801InaD-like protein
PRO_0000094592

Regions

Domain1 – 6565L27
Domain134 – 22188PDZ 1
Domain248 – 32881PDZ 2
Domain365 – 45389PDZ 3
Domain553 – 63987PDZ 4
Domain686 – 77287PDZ 5
Domain1068 – 116093PDZ 6
Domain1239 – 132284PDZ 7
Domain1437 – 152084PDZ 8
Domain1533 – 161583PDZ 9
Domain1676 – 176287PDZ 10

Amino acid modifications

Modified residue5221Phosphoserine Ref.12
Modified residue6451Phosphoserine Ref.12
Modified residue12091Phosphothreonine Ref.10
Modified residue12121Phosphoserine Ref.10 Ref.12 Ref.13
Modified residue15081Phosphothreonine Ref.12

Natural variations

Alternative sequence1 – 541541Missing in isoform 5.
VSP_014204
Alternative sequence14591L → LFWRLGSPRAWSQHLVRAFM LHHPVTEVEGQ in isoform 2.
VSP_014205
Alternative sequence1460 – 148728Missing in isoform 4.
VSP_014206
Alternative sequence1553 – 1801249Missing in isoform 2, isoform 3 and isoform 4.
VSP_014207
Alternative sequence1631 – 167545GSQQS…DMEPR → SAECTQQLSSLLRSCHHWPA KPGWHKKSFRSFPEKFRHRY GTKDC in isoform 5.
VSP_014208
Alternative sequence1676 – 1801126Missing in isoform 5.
VSP_014209
Natural variant3031G → R.
Corresponds to variant rs3762321 [ dbSNP | Ensembl ].
VAR_027988
Natural variant3621E → A.
Corresponds to variant rs1286823 [ dbSNP | Ensembl ].
VAR_027989
Natural variant4001I → V.
Corresponds to variant rs7516332 [ dbSNP | Ensembl ].
VAR_027990
Natural variant5991Q → H.
Corresponds to variant rs1286812 [ dbSNP | Ensembl ].
VAR_027991
Natural variant7441C → R. Ref.1
Corresponds to variant rs1134764 [ dbSNP | Ensembl ].
VAR_022695
Natural variant7791E → K.
Corresponds to variant rs12141598 [ dbSNP | Ensembl ].
VAR_027992
Natural variant7801E → K.
Corresponds to variant rs12141599 [ dbSNP | Ensembl ].
VAR_027993
Natural variant8701I → M. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2799627 [ dbSNP | Ensembl ].
VAR_027994
Natural variant11781G → S. Ref.3
Corresponds to variant rs1056513 [ dbSNP | Ensembl ].
VAR_027995
Natural variant12821R → H. Ref.1 Ref.2
Corresponds to variant rs1134767 [ dbSNP | Ensembl ].
VAR_027996
Natural variant13601V → L. Ref.1 Ref.2
Corresponds to variant rs2498982 [ dbSNP | Ensembl ].
VAR_027997
Natural variant15041A → P.
Corresponds to variant rs13376115 [ dbSNP | Ensembl ].
VAR_027998

Experimental info

Mutagenesis191L → W: Reduces L27 domain binding affinity to MPP5 L27 domain. Ref.15
Mutagenesis381F → W: Reduces L27 domain binding affinity to MPP5 L27 domain. Ref.15
Sequence conflict14431G → R in CAA04666. Ref.1
Sequence conflict16991L → I in AAM28433. Ref.3

Secondary structure

................................................................................................................................. 1801
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 313DD1F12B6AD80A

FASTA1,801196,368
        10         20         30         40         50         60 
MPENPATDKL QVLQVLDRLK MKLQEKGDTS QNEKLSMFYE TLKSPLFNQI LTLQQSIKQL 

        70         80         90        100        110        120 
KGQLNHIPSD CSANFDFSRK GLLVFTDGSI TNGNVHRPSN NSTVSGLFPW TPKLGNEDFN 

       130        140        150        160        170        180 
SVIQQMAQGR QIEYIDIERP STGGLGFSVV ALRSQNLGKV DIFVKDVQPG SVADRDQRLK 

       190        200        210        220        230        240 
ENDQILAINH TPLDQNISHQ QAIALLQQTT GSLRLIVARE PVHTKSSTSS SLNDTTLPET 

       250        260        270        280        290        300 
VCWGHVEEVE LINDGSGLGF GIVGGKTSGV VVRTIVPGGL ADRDGRLQTG DHILKIGGTN 

       310        320        330        340        350        360 
VQGMTSEQVA QVLRNCGNSV RMLVARDPAG DISVTPPAPA ALPVALPTVA SKGPGSDSSL 

       370        380        390        400        410        420 
FETYNVELVR KDGQSLGIRI VGYVGTSHTG EASGIYVKSI IPGSAAYHNG HIQVNDKIVA 

       430        440        450        460        470        480 
VDGVNIQGFA NHDVVEVLRN AGQVVHLTLV RRKTSSSTSP LEPPSDRGTV VEPLKPPALF 

       490        500        510        520        530        540 
LTGAVETETN VDGEDEEIKE RIDTLKNDNI QALEKLEKVP DSPENELKSR WENLLGPDYE 

       550        560        570        580        590        600 
VMVATLDTQI ADDAELQKYS KLLPIHTLRL GVEVDSFDGH HYISSIVSGG PVDTLGLLQP 

       610        620        630        640        650        660 
EDELLEVNGM QLYGKSRREA VSFLKEVPPP FTLVCCRRLF DDEASVDEPR RTETSLPETE 

       670        680        690        700        710        720 
VDHNMDVNTE EDDDGELALW SPEVKIVELV KDCKGLGFSI LDYQDPLDPT RSVIVIRSLV 

       730        740        750        760        770        780 
ADGVAERSGG LLPGDRLVSV NEYCLDNTSL AEAVEILKAV PPGLVHLGIC KPLVEDNEEE 

       790        800        810        820        830        840 
SCYILHSSSN EDKTEFSGTI HDINSSLILE APKGFRDEPY FKEELVDEPF LDLGKSFHSQ 

       850        860        870        880        890        900 
QKEIEQSKEA WEMHEFLTPR LQEMDEEREI LVDEEYELYQ DPSPSMELYP LSHIQEATPV 

       910        920        930        940        950        960 
PSVNELHFGT QWLHDNEPSE SQEARTGRTV YSQEAQPYGY CPENVMKENF VMESLPSVPS 

       970        980        990       1000       1010       1020 
TEGNSQQGRF DDLENLNSLA KTSLDLGMIP NDVQGPSLLI DLPVVAQRRE QEDLPLYQHQ 

      1030       1040       1050       1060       1070       1080 
ATRVISKASA YTGMLSSRYA TDTCELPERE EGEGEETPNF SHWGPPRIVE IFREPNVSLG 

      1090       1100       1110       1120       1130       1140 
ISIVGGQTVI KRLKNGEELK GIFIKQVLED SPAGKTNALK TGDKILEVSG VDLQNASHSE 

      1150       1160       1170       1180       1190       1200 
AVEAIKNAGN PVVFIVQSLS STPRVIPNVH NKANKITGNQ NQDTQEKKEK RQGTAPPPMK 

      1210       1220       1230       1240       1250       1260 
LPPPYKALTD DSDENEEEDA FTDQKIRQRY ADLPGELHII ELEKDKNGLG LSLAGNKDRS 

      1270       1280       1290       1300       1310       1320 
RMSIFVVGIN PEGPAAADGR MRIGDELLEI NNQILYGRSH QNASAIIKTA PSKVKLVFIR 

      1330       1340       1350       1360       1370       1380 
NEDAVNQMAV TPFPVPSSSP SSIEDQSGTE PISSEEDGSV EVGIKQLPES ESFKLAVSQM 

      1390       1400       1410       1420       1430       1440 
KQQKYPTKVS FSSQEIPLAP ASSYHSTDAD FTGYGGFQAP LSVDPATCPI VPGQEMIIEI 

      1450       1460       1470       1480       1490       1500 
SKGRSGLGLS IVGGKDTPLN AIVIHEVYEE GAAARDGRLW AGDQILEVNG VDLRNSSHEE 

      1510       1520       1530       1540       1550       1560 
AITALRQTPQ KVRLVVYRDE AHYRDEENLE IFPVDLQKKA GRGLGLSIVG KRNGSGVFIS 

      1570       1580       1590       1600       1610       1620 
DIVKGGAADL DGRLIQGDQI LSVNGEDMRN ASQETVATIL KCAQGLVQLE IGRLRAGSWT 

      1630       1640       1650       1660       1670       1680 
SARTTSQNSQ GSQQSAHSSC HPSFAPVITG LQNLVGTKRV SDPSQKNSGT DMEPRTVEIN 

      1690       1700       1710       1720       1730       1740 
RELSDALGIS IAGGRGSPLG DIPVFIAMIQ ASGVAARTQK LKVGDRIVSI NGQPLDGLSH 

      1750       1760       1770       1780       1790       1800 
ADVVNLLKNA YGRIILQVVA DTNISAIAAQ LENMSTGYHL GSPTAEHHPE DTEEQLQMTA 


D 

« Hide

Isoform 2 [UniParc].

Checksum: 9444B48DB84DE81E
Show »

FASTA1,582173,793
Isoform 3 [UniParc].

Checksum: 646145A57C61152A
Show »

FASTA1,552170,238
Isoform 4 [UniParc].

Checksum: 5203884719B4B152
Show »

FASTA1,524167,159
Isoform 5 [UniParc].

Checksum: 2717B2D492419866
Show »

FASTA1,134125,231

References

« Hide 'large scale' references
[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]"Isolation of novel heart-specific genes using the BodyMap database."
Soejima H., Kawamoto S., Akai J., Miyoshi O., Arai Y., Morohka T., Matsuo S., Niikawa N., Kimura A., Okubo K., Mukai T.
Genomics 74:115-120(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"KIBRA modulates directional migration of podocytes."
Duning K., Schurek E.M., Schlueter M., Bayer M., Reinhardt H.C., Schwab A., Schaefer L., Benzing T., Schermer B., Saleem M.A., Huber T.B., Bachmann S., Kremerskothen J., Weide T., Pavenstaedt H.
J. Am. Soc. Nephrol. 19:1891-1903(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WWC1.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AC097064, AL136458, AL353802, AL449143 Genomic DNA. Translation: CAH70418.1.
AL590374 expand/collapse EMBL AC list , AC097064, AL136458, AL353802, AL449143 Genomic DNA. Translation: CAH70420.1.
AL353802, AL136458, AL590374 Genomic DNA. Translation: CAI22258.1. Sequence problems.
AL353802 expand/collapse EMBL AC list , AC097064, AL136458, AL449143, AL590374 Genomic DNA. Translation: CAI22260.1.
AL353802 expand/collapse EMBL AC list , AC097064, AL136458, AL449143, AL590374 Genomic DNA. Translation: CAI22262.1.
AL449143 expand/collapse EMBL AC list , AC097064, AL136458, AL353802, AL590374 Genomic DNA. Translation: CAI15923.1.
AL449143 expand/collapse EMBL AC list , AC097064, AL136458, AL353802, AL590374 Genomic DNA. Translation: CAI15925.1.
AL136458, AL353802, AL590374 Genomic DNA. Translation: CAI21733.1. Sequence problems.
AL136458 expand/collapse EMBL AC list , AC097064, AL353802, AL449143, AL590374 Genomic DNA. Translation: CAI21734.1.
AL136458 expand/collapse EMBL AC list , AC097064, AL353802, AL449143, AL590374 Genomic DNA. Translation: CAI21737.1.
BC021135 mRNA. Translation: AAH21135.1.
CCDSCCDS617.2. [Q8NI35-1]
RefSeqNP_795352.2. NM_176877.2.
UniGeneHs.478125.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ8NI35.
SMRQ8NI35. Positions 10-67, 116-473, 569-638, 675-770, 1054-1198, 1219-1332, 1389-1765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115502. 19 interactions.
IntActQ8NI35. 19 interactions.
MINTMINT-237883.

PTM databases

PhosphoSiteQ8NI35.

Polymorphism databases

DMDM116242542.

Proteomic databases

MaxQBQ8NI35.
PaxDbQ8NI35.
PRIDEQ8NI35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316485; ENSP00000326199; ENSG00000132849. [Q8NI35-2]
ENST00000371158; ENSP00000360200; ENSG00000132849. [Q8NI35-1]
ENST00000484937; ENSP00000433669; ENSG00000132849. [Q8NI35-5]
GeneID10207.
KEGGhsa:10207.
UCSCuc001daa.2. human. [Q8NI35-4]
uc001dab.3. human. [Q8NI35-1]
uc009waf.1. human. [Q8NI35-2]

Organism-specific databases

CTD10207.
GeneCardsGC01P062208.
HGNCHGNC:28881. INADL.
MIM603199. gene.
neXtProtNX_Q8NI35.
PharmGKBPA134919267.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252837.
HOVERGENHBG080134.
KOK06092.
OMAEAWEMHE.
OrthoDBEOG72ZCD0.
PhylomeDBQ8NI35.
TreeFamTF330709.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
SignaLinkQ8NI35.

Gene expression databases

ArrayExpressQ8NI35.
BgeeQ8NI35.
GenevestigatorQ8NI35.

Family and domain databases

Gene3D2.30.42.10. 10 hits.
InterProIPR004172. L27.
IPR015132. L27_2.
IPR001478. PDZ.
[Graphical view]
PfamPF09045. L27_2. 1 hit.
PF00595. PDZ. 10 hits.
[Graphical view]
SMARTSM00569. L27. 1 hit.
SM00228. PDZ. 10 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 10 hits.
PROSITEPS51022. L27. 1 hit.
PS50106. PDZ. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINADL. human.
EvolutionaryTraceQ8NI35.
GeneWikiINADL.
GenomeRNAi10207.
NextBio38644.
PROQ8NI35.
SOURCESearch...

Entry information

Entry nameINADL_HUMAN
AccessionPrimary (citable) accession number: Q8NI35
Secondary accession number(s): O15249 expand/collapse secondary AC list , O43742, O60833, Q5VUA5, Q5VUA6, Q5VUA7, Q5VUA8, Q5VUA9, Q5VUB0, Q8WU78, Q9H3N9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM