SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8NI35

- INADL_HUMAN

UniProt

Q8NI35 - INADL_HUMAN

(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)

Protein
InaD-like protein
Gene
INADL, PATJ
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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.4 Publications

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
Complete GO annotation...

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 protein
PRO_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).5 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

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.

Miscellaneous databases

EvolutionaryTraceiQ8NI35.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565L27
Add
BLAST
Domaini134 – 22188PDZ 1
Add
BLAST
Domaini248 – 32881PDZ 2
Add
BLAST
Domaini365 – 45389PDZ 3
Add
BLAST
Domaini553 – 63987PDZ 4
Add
BLAST
Domaini686 – 77287PDZ 5
Add
BLAST
Domaini1068 – 116093PDZ 6
Add
BLAST
Domaini1239 – 132284PDZ 7
Add
BLAST
Domaini1437 – 152084PDZ 8
Add
BLAST
Domaini1533 – 161583PDZ 9
Add
BLAST
Domaini1676 – 176287PDZ 10
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 L27 domain.
Contains 10 PDZ (DHR) domains.

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.

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.
VSP_014204Add
BLAST
Alternative sequencei1459 – 14591L → LFWRLGSPRAWSQHLVRAFM LHHPVTEVEGQ in isoform 2.
VSP_014205
Alternative sequencei1460 – 148728Missing in isoform 4.
VSP_014206Add
BLAST
Alternative sequencei1553 – 1801249Missing in isoform 2, isoform 3 and isoform 4.
VSP_014207Add
BLAST
Alternative sequencei1631 – 167545GSQQS…DMEPR → SAECTQQLSSLLRSCHHWPA KPGWHKKSFRSFPEKFRHRY GTKDC in isoform 5.
VSP_014208Add
BLAST
Alternative sequencei1676 – 1801126Missing in isoform 5.
VSP_014209Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1443 – 14431G → R in CAA04666. 1 Publication
Sequence conflicti1699 – 16991L → I in AAM28433. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 111 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

Similar proteinsi