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Q96RT1

- LAP2_HUMAN

UniProt

Q96RT1 - LAP2_HUMAN

Protein

Protein LAP2

Gene

ERBB2IP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state.1 Publication

    GO - Molecular functioni

    1. ErbB-2 class receptor binding Source: UniProtKB
    2. integrin binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. structural constituent of cytoskeleton Source: UniProtKB

    GO - Biological processi

    1. basal protein localization Source: UniProtKB
    2. cell adhesion Source: UniProtKB
    3. cell cycle Source: UniProtKB
    4. cell growth Source: UniProtKB
    5. epidermal growth factor receptor signaling pathway Source: UniProtKB
    6. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
    7. integrin-mediated signaling pathway Source: UniProtKB
    8. intermediate filament cytoskeleton organization Source: UniProtKB
    9. protein targeting Source: Ensembl
    10. signal transduction Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_115755. Signaling by ERBB2.
    SignaLinkiQ96RT1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein LAP2
    Alternative name(s):
    Densin-180-like protein
    Erbb2-interacting protein
    Short name:
    Erbin
    Gene namesi
    Name:ERBB2IP
    Synonyms:ERBIN, KIAA1225, LAP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:15842. ERBB2IP.

    Subcellular locationi

    Cell junctionhemidesmosome 2 Publications. Nucleus membrane By similarity
    Note: Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes By similarity.By similarity

    GO - Cellular componenti

    1. basal plasma membrane Source: UniProtKB
    2. basement membrane Source: ProtInc
    3. cytoplasm Source: UniProtKB
    4. hemidesmosome Source: UniProtKB
    5. nuclear membrane Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cell junction, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27845.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14121412Protein LAP2PRO_0000188301Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei440 – 4401Phosphoserine1 Publication
    Modified residuei569 – 5691Phosphoserine2 Publications
    Modified residuei602 – 6021Phosphoserine1 Publication
    Modified residuei603 – 6031Phosphoserine1 Publication
    Modified residuei715 – 7151PhosphoserineBy similarity
    Modified residuei857 – 8571Phosphoserine1 Publication
    Modified residuei872 – 8721Phosphoserine1 Publication
    Modified residuei917 – 9171Phosphothreonine2 Publications
    Modified residuei920 – 9201Phosphotyrosine1 Publication
    Modified residuei931 – 9311Phosphoserine1 Publication
    Modified residuei972 – 9721Phosphotyrosine1 Publication
    Modified residuei1104 – 11041PhosphotyrosineBy similarity
    Modified residuei1158 – 11581Phosphoserine1 Publication
    Modified residuei1286 – 12861Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96RT1.
    PaxDbiQ96RT1.
    PRIDEiQ96RT1.

    PTM databases

    PhosphoSiteiQ96RT1.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, heart, kidney, muscle and stomach, followed by liver, spleen and intestine.1 Publication

    Gene expression databases

    ArrayExpressiQ96RT1.
    BgeeiQ96RT1.
    CleanExiHS_ERBB2IP.
    GenevestigatoriQ96RT1.

    Organism-specific databases

    HPAiHPA048606.

    Interactioni

    Subunit structurei

    Interacts with ERBB2, BPAG1 and ITGB4. May favor the localization of ERBB2, by restricting its presence to the basolateral membrane of epithelial cells. Also found to interact with ARVCF and delta catenin. Interacts (via C-terminus) with DST Isoform 3 (via N-terminus).5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PKP4Q995693EBI-8449250,EBI-726447

    Protein-protein interaction databases

    BioGridi120997. 69 interactions.
    IntActiQ96RT1. 14 interactions.
    MINTiMINT-199447.
    STRINGi9606.ENSP00000370330.

    Structurei

    Secondary structure

    1
    1412
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1318 – 132710
    Beta strandi1329 – 13313
    Beta strandi1333 – 13386
    Turni1339 – 13424
    Beta strandi1346 – 13483
    Beta strandi1353 – 13597
    Turni1364 – 13685
    Beta strandi1374 – 13785
    Helixi1388 – 139710
    Beta strandi1400 – 141011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MFGX-ray1.25A1321-1412[»]
    1MFLX-ray1.88A1321-1412[»]
    1N7TNMR-A1314-1412[»]
    2H3LX-ray1.00A/B1314-1412[»]
    2QBWX-ray1.80A1330-1410[»]
    3CH8X-ray1.90A1330-1410[»]
    ProteinModelPortaliQ96RT1.
    SMRiQ96RT1. Positions 26-455, 1283-1412.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96RT1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati23 – 4422LRR 1Add
    BLAST
    Repeati47 – 6822LRR 2Add
    BLAST
    Repeati70 – 9122LRR 3Add
    BLAST
    Repeati93 – 11422LRR 4Add
    BLAST
    Repeati116 – 13722LRR 5Add
    BLAST
    Repeati139 – 16123LRR 6Add
    BLAST
    Repeati162 – 18322LRR 7Add
    BLAST
    Repeati185 – 20622LRR 8Add
    BLAST
    Repeati208 – 22922LRR 9Add
    BLAST
    Repeati231 – 25222LRR 10Add
    BLAST
    Repeati254 – 27522LRR 11Add
    BLAST
    Repeati277 – 29822LRR 12Add
    BLAST
    Repeati300 – 32122LRR 13Add
    BLAST
    Repeati323 – 34422LRR 14Add
    BLAST
    Repeati346 – 36722LRR 15Add
    BLAST
    Repeati369 – 39123LRR 16Add
    BLAST
    Repeati392 – 41322LRR 17Add
    BLAST
    Domaini1321 – 141090PDZPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi930 – 9345Poly-Ser

    Sequence similaritiesi

    Belongs to the LAP (LRR and PDZ) protein family.Curated
    Contains 17 LRR (leucine-rich) repeats.Curated
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000060229.
    HOVERGENiHBG052305.
    InParanoidiQ96RT1.
    KOiK12796.
    OMAiSDEEMKM.
    OrthoDBiEOG72C501.
    PhylomeDBiQ96RT1.
    TreeFamiTF351429.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    InterProiIPR001611. Leu-rich_rpt.
    IPR025875. Leu-rich_rpt_4.
    IPR001478. PDZ.
    [Graphical view]
    PfamiPF12799. LRR_4. 2 hits.
    PF13855. LRR_8. 2 hits.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    SMARTiSM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS51450. LRR. 15 hits.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequences (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96RT1-1) [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

    MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE     50
    LYLDANQIEE LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS 100
    KNGIQEFPEN IKNCKVLTIV EASVNPISKL PDGFSQLLNL TQLYLNDAFL 150
    EFLPANFGRL TKLQILELRE NQLKMLPKTM NRLTQLERLD LGSNEFTEVP 200
    EVLEQLSGLK EFWMDANRLT FIPGFIGSLK QLTYLDVSKN NIEMVEEGIS 250
    TCENLQDLLL SSNSLQQLPE TIGSLKNITT LKIDENQLMY LPDSIGGLIS 300
    VEELDCSFNE VEALPSSIGQ LTNLRTFAAD HNYLQQLPPE IGSWKNITVL 350
    FLHSNKLETL PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD 400
    NQSKPLIPLQ KETDSETQKM VLTNYMFPQQ PRTEDVMFIS DNESFNPSLW 450
    EEQRKQRAQV AFECDEDKDE REAPPREGNL KRYPTPYPDE LKNMVKTVQT 500
    IVHRLKDEET NEDSGRDLKP HEDQQDINKD VGVKTSESTT TVKSKVDERE 550
    KYMIGNSVQK ISEPEAEISP GSLPVTANMK ASENLKHIVN HDDVFEESEE 600
    LSSDEEMKMA EMRPPLIETS INQPKVVALS NNKKDDTKET DSLSDEVTHN 650
    SNQNNSNCSS PSRMSDSVSL NTDSSQDTSL CSPVKQTHID INSKIRQEDE 700
    NFNSLLQNGD ILNSSTEEKF KAHDKKDFNL PEYDLNVEER LVLIEKSVDS 750
    TATADDTHKL DHINMNLNKL ITNDTFQPEI MERSKTQDIV LGTSFLSINS 800
    KEETEHLENG NKYPNLESVN KVNGHSEETS QSPNRTEPHD SDCSVDLGIS 850
    KSTEDLSPQK SGPVGSVVKS HSITNMEIGG LKIYDILSDN GPQQPSTTVK 900
    ITSAVDGKNI VRSKSATLLY DQPLQVFTGS SSSSDLISGT KAIFKFDSNH 950
    NPEEPNIIRG PTSGPQSAPQ IYGPPQYNIQ YSSSAAVKDT LWHSKQNPQI 1000
    DHASFPPQLL PRSESTENQS YAKHSANMNF SNHNNVRANT AYHLHQRLGP 1050
    ARHGEMWAIS PNDRLIPAVT RSTIQRQSSV SSTASVNLGD PGSTRRAQIP 1100
    EGDYLSYREF HSAGRTPPMM PGSQRPLSAR TYSIDGPNAS RPQSARPSIN 1150
    EIPERTMSVS DFNYSRTSPS KRPNARVGSE HSLLDPPGKS KVPRDWREQV 1200
    LRHIEAKKLE KKHPQTSSSG DPCQDGIFIS GQQNYSSATL SHKDVPPDSL 1250
    MKMPLSNGQM GQPLRPQANY SQIHHPPQAS VARHPSREQL IDYLMLKVAH 1300
    QPPYTQPHCS PRQGHELAKQ EIRVRVEKDP ELGFSISGGV GGRGNPFRPD 1350
    DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG YSFINIEHGQ AVSLLKTFQN 1400
    TVELIIVREV SS 1412
    Length:1,412
    Mass (Da):158,298
    Last modified:October 17, 2006 - v2
    Checksum:i304DFC81578CF671
    GO
    Isoform 2 (identifier: Q96RT1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1212-1252: Missing.

    Show »
    Length:1,371
    Mass (Da):153,926
    Checksum:iC8F24683B0C4324D
    GO
    Isoform 3 (identifier: Q96RT1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1212-1252: Missing.
         1268-1278: Missing.

    Show »
    Length:1,360
    Mass (Da):152,653
    Checksum:iA56B9384680DA710
    GO
    Isoform 4 (identifier: Q96RT1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1212-1252: Missing.
         1353-1377: Missing.

    Show »
    Length:1,346
    Mass (Da):151,252
    Checksum:i19D7B81B5A934C2E
    GO
    Isoform 5 (identifier: Q96RT1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1212-1252: Missing.
         1253-1267: Missing.

    Show »
    Length:1,356
    Mass (Da):152,290
    Checksum:i9662C85F03C8F08B
    GO
    Isoform 6 (identifier: Q96RT1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1212-1252: Missing.
         1322-1352: Missing.

    Show »
    Length:1,340
    Mass (Da):150,602
    Checksum:i12B24ADE16A5F537
    GO
    Isoform 7 (identifier: Q96RT1-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1212-1252: Missing.
         1253-1267: Missing.
         1268-1278: Missing.
         1279-1321: Missing.

    Show »
    Length:1,302
    Mass (Da):146,086
    Checksum:iE436063ACDA2C1A4
    GO
    Isoform 8 (identifier: Q96RT1-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1212-1252: KHPQTSSSGD...KDVPPDSLMK → SMLSRSFNSN...RRGSGGHIFR

    Note: No experimental confirmation available.

    Show »
    Length:1,419
    Mass (Da):159,024
    Checksum:i9E18163421DBE278
    GO
    Isoform 9 (identifier: Q96RT1-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         531-534: Missing.
         1212-1252: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,367
    Mass (Da):153,543
    Checksum:iC1F031AD4CA0746B
    GO

    Sequence cautioni

    The sequence AAH50692.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAA91538.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti271 – 2711T → P in AAI15013. (PubMed:15489334)Curated
    Sequence conflicti547 – 5471D → G in AAI15013. (PubMed:15489334)Curated
    Sequence conflicti805 – 8051E → G in BAA91538. (PubMed:14702039)Curated
    Sequence conflicti813 – 8131Y → C in AAK69431. (PubMed:11375975)Curated
    Sequence conflicti848 – 8481G → C in BAG65463. (PubMed:14702039)Curated
    Sequence conflicti1047 – 10471R → S in BAG65463. (PubMed:14702039)Curated
    Sequence conflicti1205 – 12051E → G in AAI15013. (PubMed:15489334)Curated
    Sequence conflicti1267 – 12671Q → P in AAI15013. (PubMed:15489334)Curated
    Sequence conflicti1328 – 13281K → R in AAI15013. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti274 – 2741S → L.1 Publication
    Corresponds to variant rs3213837 [ dbSNP | Ensembl ].
    VAR_019346
    Natural varianti313 – 3131A → V.1 Publication
    Corresponds to variant rs191137999 [ dbSNP | Ensembl ].
    VAR_068905
    Natural varianti746 – 7461K → E.
    Corresponds to variant rs16894812 [ dbSNP | Ensembl ].
    VAR_028304
    Natural varianti914 – 9141K → R.
    Corresponds to variant rs34521887 [ dbSNP | Ensembl ].
    VAR_046673
    Natural varianti1089 – 10891G → V.
    Corresponds to variant rs35601230 [ dbSNP | Ensembl ].
    VAR_046674
    Natural varianti1112 – 11121S → L.
    Corresponds to variant rs3805466 [ dbSNP | Ensembl ].
    VAR_019347
    Natural varianti1207 – 12071K → E.1 Publication
    VAR_019348

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei531 – 5344Missing in isoform 9. 1 PublicationVSP_047389
    Alternative sequencei1212 – 125241Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 9. 5 PublicationsVSP_010802Add
    BLAST
    Alternative sequencei1212 – 125241KHPQT…DSLMK → SMLSRSFNSNFTTVSSFHCG SSRDLHGSQGSLALSVADRR GSGGHIFR in isoform 8. 1 PublicationVSP_044536Add
    BLAST
    Alternative sequencei1253 – 126715Missing in isoform 5 and isoform 7. 1 PublicationVSP_010803Add
    BLAST
    Alternative sequencei1268 – 127811Missing in isoform 3 and isoform 7. 1 PublicationVSP_010804Add
    BLAST
    Alternative sequencei1279 – 132143Missing in isoform 7. 1 PublicationVSP_010805Add
    BLAST
    Alternative sequencei1322 – 135231Missing in isoform 6. 1 PublicationVSP_010806Add
    BLAST
    Alternative sequencei1353 – 137725Missing in isoform 4. 2 PublicationsVSP_010807Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263744 mRNA. Translation: AAF77048.1.
    AF276423 mRNA. Translation: AAK69431.1.
    AB033051 mRNA. Translation: BAA86539.2.
    AK001180 mRNA. Translation: BAA91538.1. Different initiation.
    AK304693 mRNA. Translation: BAG65463.1.
    AC010359 Genomic DNA. No translation available.
    AC025442 Genomic DNA. No translation available.
    BC050692 mRNA. Translation: AAH50692.1. Sequence problems.
    BC115012 mRNA. Translation: AAI15013.1.
    BC126464 mRNA. Translation: AAI26465.1.
    BC144075 mRNA. Translation: AAI44076.1.
    CCDSiCCDS34172.1. [Q96RT1-7]
    CCDS3990.1. [Q96RT1-2]
    CCDS58951.1. [Q96RT1-9]
    CCDS58952.1. [Q96RT1-8]
    CCDS58953.1. [Q96RT1-1]
    CCDS58954.1. [Q96RT1-4]
    RefSeqiNP_001006600.1. NM_001006600.2. [Q96RT1-7]
    NP_001240626.1. NM_001253697.1. [Q96RT1-1]
    NP_001240627.1. NM_001253698.1. [Q96RT1-4]
    NP_001240628.1. NM_001253699.1. [Q96RT1-8]
    NP_001240630.1. NM_001253701.1. [Q96RT1-9]
    NP_061165.1. NM_018695.3. [Q96RT1-2]
    UniGeneiHs.591774.
    Hs.597241.

    Genome annotation databases

    EnsembliENST00000284037; ENSP00000284037; ENSG00000112851. [Q96RT1-1]
    ENST00000380935; ENSP00000370322; ENSG00000112851. [Q96RT1-7]
    ENST00000380938; ENSP00000370325; ENSG00000112851. [Q96RT1-4]
    ENST00000380943; ENSP00000370330; ENSG00000112851. [Q96RT1-2]
    ENST00000506030; ENSP00000426632; ENSG00000112851. [Q96RT1-8]
    ENST00000508515; ENSP00000422015; ENSG00000112851. [Q96RT1-7]
    ENST00000511297; ENSP00000422766; ENSG00000112851. [Q96RT1-9]
    GeneIDi55914.
    KEGGihsa:55914.
    UCSCiuc003jui.2. human. [Q96RT1-2]
    uc003juj.2. human. [Q96RT1-7]
    uc003juk.2. human. [Q96RT1-1]
    uc011cqy.2. human. [Q96RT1-4]

    Polymorphism databases

    DMDMi116242614.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263744 mRNA. Translation: AAF77048.1 .
    AF276423 mRNA. Translation: AAK69431.1 .
    AB033051 mRNA. Translation: BAA86539.2 .
    AK001180 mRNA. Translation: BAA91538.1 . Different initiation.
    AK304693 mRNA. Translation: BAG65463.1 .
    AC010359 Genomic DNA. No translation available.
    AC025442 Genomic DNA. No translation available.
    BC050692 mRNA. Translation: AAH50692.1 . Sequence problems.
    BC115012 mRNA. Translation: AAI15013.1 .
    BC126464 mRNA. Translation: AAI26465.1 .
    BC144075 mRNA. Translation: AAI44076.1 .
    CCDSi CCDS34172.1. [Q96RT1-7 ]
    CCDS3990.1. [Q96RT1-2 ]
    CCDS58951.1. [Q96RT1-9 ]
    CCDS58952.1. [Q96RT1-8 ]
    CCDS58953.1. [Q96RT1-1 ]
    CCDS58954.1. [Q96RT1-4 ]
    RefSeqi NP_001006600.1. NM_001006600.2. [Q96RT1-7 ]
    NP_001240626.1. NM_001253697.1. [Q96RT1-1 ]
    NP_001240627.1. NM_001253698.1. [Q96RT1-4 ]
    NP_001240628.1. NM_001253699.1. [Q96RT1-8 ]
    NP_001240630.1. NM_001253701.1. [Q96RT1-9 ]
    NP_061165.1. NM_018695.3. [Q96RT1-2 ]
    UniGenei Hs.591774.
    Hs.597241.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MFG X-ray 1.25 A 1321-1412 [» ]
    1MFL X-ray 1.88 A 1321-1412 [» ]
    1N7T NMR - A 1314-1412 [» ]
    2H3L X-ray 1.00 A/B 1314-1412 [» ]
    2QBW X-ray 1.80 A 1330-1410 [» ]
    3CH8 X-ray 1.90 A 1330-1410 [» ]
    ProteinModelPortali Q96RT1.
    SMRi Q96RT1. Positions 26-455, 1283-1412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120997. 69 interactions.
    IntActi Q96RT1. 14 interactions.
    MINTi MINT-199447.
    STRINGi 9606.ENSP00000370330.

    PTM databases

    PhosphoSitei Q96RT1.

    Polymorphism databases

    DMDMi 116242614.

    Proteomic databases

    MaxQBi Q96RT1.
    PaxDbi Q96RT1.
    PRIDEi Q96RT1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284037 ; ENSP00000284037 ; ENSG00000112851 . [Q96RT1-1 ]
    ENST00000380935 ; ENSP00000370322 ; ENSG00000112851 . [Q96RT1-7 ]
    ENST00000380938 ; ENSP00000370325 ; ENSG00000112851 . [Q96RT1-4 ]
    ENST00000380943 ; ENSP00000370330 ; ENSG00000112851 . [Q96RT1-2 ]
    ENST00000506030 ; ENSP00000426632 ; ENSG00000112851 . [Q96RT1-8 ]
    ENST00000508515 ; ENSP00000422015 ; ENSG00000112851 . [Q96RT1-7 ]
    ENST00000511297 ; ENSP00000422766 ; ENSG00000112851 . [Q96RT1-9 ]
    GeneIDi 55914.
    KEGGi hsa:55914.
    UCSCi uc003jui.2. human. [Q96RT1-2 ]
    uc003juj.2. human. [Q96RT1-7 ]
    uc003juk.2. human. [Q96RT1-1 ]
    uc011cqy.2. human. [Q96RT1-4 ]

    Organism-specific databases

    CTDi 55914.
    GeneCardsi GC05P065258.
    HGNCi HGNC:15842. ERBB2IP.
    HPAi HPA048606.
    MIMi 606944. gene.
    neXtProti NX_Q96RT1.
    PharmGKBi PA27845.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000060229.
    HOVERGENi HBG052305.
    InParanoidi Q96RT1.
    KOi K12796.
    OMAi SDEEMKM.
    OrthoDBi EOG72C501.
    PhylomeDBi Q96RT1.
    TreeFami TF351429.

    Enzyme and pathway databases

    Reactomei REACT_115755. Signaling by ERBB2.
    SignaLinki Q96RT1.

    Miscellaneous databases

    ChiTaRSi ERBB2IP. human.
    EvolutionaryTracei Q96RT1.
    GeneWikii Erbin_(protein).
    GenomeRNAii 55914.
    NextBioi 61305.
    PROi Q96RT1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96RT1.
    Bgeei Q96RT1.
    CleanExi HS_ERBB2IP.
    Genevestigatori Q96RT1.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR001611. Leu-rich_rpt.
    IPR025875. Leu-rich_rpt_4.
    IPR001478. PDZ.
    [Graphical view ]
    Pfami PF12799. LRR_4. 2 hits.
    PF13855. LRR_8. 2 hits.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS51450. LRR. 15 hits.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ERBIN: a basolateral PDZ protein that interacts with the mammalian ERBB2/HER2 receptor."
      Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V., Jaulin-Bastard F., Saito H., Fournier E., Adelaide J., Margolis B., Birnbaum D.
      Nat. Cell Biol. 2:407-414(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH ERBB2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
      Tissue: B-cell.
    2. "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression."
      Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H., Sonnenberg A., Borradori L.
      J. Biol. Chem. 276:32427-32436(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), INTERACTION WITH BPAG1; DST AND ITGB4, SUBCELLULAR LOCATION, VARIANT GLU-1207.
    3. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-1206 (ISOFORM 1).
      Tissue: Teratocarcinoma and Uterus.
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 2; 8 AND 9), VARIANTS LEU-274 AND VAL-313.
      Tissue: Cerebellum and Skin.
    8. "The Erbin PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF."
      Laura R.P., Witt A.S., Held H.A., Gerstner R., Deshayes K., Koehler M.F.T., Kosik K.S., Sidhu S.S., Lasky L.A.
      J. Biol. Chem. 277:12906-12914(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DELTA CATENIN AND ARVCF.
    9. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-920, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-972, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-857; THR-917 AND SER-1286, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; THR-917; SER-931 AND SER-1158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-569; SER-602 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Novel mode of ligand recognition by the Erbin PDZ domain."
      Birrane G., Chung J., Ladias J.A.
      J. Biol. Chem. 278:1399-1402(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1321-1412 IN COMPLEX WITH ERBB2 C-TERMINUS.
    18. "Origins of PDZ domain ligand specificity. Structure determination and mutagenesis of the Erbin PDZ domain."
      Skelton N.J., Koehler M.F.T., Zobel K., Wong W.L., Yeh S., Pisabarro M.T., Yin J.P., Lasky L.A., Sidhu S.S.
      J. Biol. Chem. 278:7645-7654(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1314-1412 IN COMPLEX WITH PHAGE-DERIVED PEPTIDE.
    19. "Comparative structural analysis of the erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity."
      Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J., Sidhu S.S., Wiesmann C.
      J. Biol. Chem. 281:22312-22320(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1314-1412.

    Entry informationi

    Entry nameiLAP2_HUMAN
    AccessioniPrimary (citable) accession number: Q96RT1
    Secondary accession number(s): A0AVR1
    , B4E3F1, B7ZLV9, E7EQW9, E9PCR8, Q1RMD0, Q86W38, Q9NR18, Q9NW48, Q9ULJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 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 5
      Human chromosome 5: 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