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Q96RT1

- LAP2_HUMAN

UniProt

Q96RT1 - LAP2_HUMAN

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Protein

Protein LAP2

Gene

ERBB2IP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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. signal transduction Source: ProtInc
Complete GO annotation...

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. nucleus Source: UniProtKB
  6. plasma membrane Source: HPA
Complete GO annotation...

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

BgeeiQ96RT1.
CleanExiHS_ERBB2IP.
ExpressionAtlasiQ96RT1. baseline and differential.
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-993903,EBI-726447

Protein-protein interaction databases

BioGridi120997. 75 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 26-456, 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.
GeneTreeiENSGT00760000118833.
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

        10         20         30         40         50
MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE
60 70 80 90 100
LYLDANQIEE LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS
110 120 130 140 150
KNGIQEFPEN IKNCKVLTIV EASVNPISKL PDGFSQLLNL TQLYLNDAFL
160 170 180 190 200
EFLPANFGRL TKLQILELRE NQLKMLPKTM NRLTQLERLD LGSNEFTEVP
210 220 230 240 250
EVLEQLSGLK EFWMDANRLT FIPGFIGSLK QLTYLDVSKN NIEMVEEGIS
260 270 280 290 300
TCENLQDLLL SSNSLQQLPE TIGSLKNITT LKIDENQLMY LPDSIGGLIS
310 320 330 340 350
VEELDCSFNE VEALPSSIGQ LTNLRTFAAD HNYLQQLPPE IGSWKNITVL
360 370 380 390 400
FLHSNKLETL PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD
410 420 430 440 450
NQSKPLIPLQ KETDSETQKM VLTNYMFPQQ PRTEDVMFIS DNESFNPSLW
460 470 480 490 500
EEQRKQRAQV AFECDEDKDE REAPPREGNL KRYPTPYPDE LKNMVKTVQT
510 520 530 540 550
IVHRLKDEET NEDSGRDLKP HEDQQDINKD VGVKTSESTT TVKSKVDERE
560 570 580 590 600
KYMIGNSVQK ISEPEAEISP GSLPVTANMK ASENLKHIVN HDDVFEESEE
610 620 630 640 650
LSSDEEMKMA EMRPPLIETS INQPKVVALS NNKKDDTKET DSLSDEVTHN
660 670 680 690 700
SNQNNSNCSS PSRMSDSVSL NTDSSQDTSL CSPVKQTHID INSKIRQEDE
710 720 730 740 750
NFNSLLQNGD ILNSSTEEKF KAHDKKDFNL PEYDLNVEER LVLIEKSVDS
760 770 780 790 800
TATADDTHKL DHINMNLNKL ITNDTFQPEI MERSKTQDIV LGTSFLSINS
810 820 830 840 850
KEETEHLENG NKYPNLESVN KVNGHSEETS QSPNRTEPHD SDCSVDLGIS
860 870 880 890 900
KSTEDLSPQK SGPVGSVVKS HSITNMEIGG LKIYDILSDN GPQQPSTTVK
910 920 930 940 950
ITSAVDGKNI VRSKSATLLY DQPLQVFTGS SSSSDLISGT KAIFKFDSNH
960 970 980 990 1000
NPEEPNIIRG PTSGPQSAPQ IYGPPQYNIQ YSSSAAVKDT LWHSKQNPQI
1010 1020 1030 1040 1050
DHASFPPQLL PRSESTENQS YAKHSANMNF SNHNNVRANT AYHLHQRLGP
1060 1070 1080 1090 1100
ARHGEMWAIS PNDRLIPAVT RSTIQRQSSV SSTASVNLGD PGSTRRAQIP
1110 1120 1130 1140 1150
EGDYLSYREF HSAGRTPPMM PGSQRPLSAR TYSIDGPNAS RPQSARPSIN
1160 1170 1180 1190 1200
EIPERTMSVS DFNYSRTSPS KRPNARVGSE HSLLDPPGKS KVPRDWREQV
1210 1220 1230 1240 1250
LRHIEAKKLE KKHPQTSSSG DPCQDGIFIS GQQNYSSATL SHKDVPPDSL
1260 1270 1280 1290 1300
MKMPLSNGQM GQPLRPQANY SQIHHPPQAS VARHPSREQL IDYLMLKVAH
1310 1320 1330 1340 1350
QPPYTQPHCS PRQGHELAKQ EIRVRVEKDP ELGFSISGGV GGRGNPFRPD
1360 1370 1380 1390 1400
DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG YSFINIEHGQ AVSLLKTFQN
1410
TVELIIVREV SS
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 26-456, 1283-1412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120997. 75 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 GC05P065223.
HGNCi HGNC:15842. ERBB2IP.
HPAi HPA048606.
MIMi 606944. gene.
neXtProti NX_Q96RT1.
PharmGKBi PA27845.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00760000118833.
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

Bgeei Q96RT1.
CleanExi HS_ERBB2IP.
ExpressionAtlasi Q96RT1. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 136 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