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Q80TH2 (LAP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein LAP2
Alternative name(s):
Densin-180-like protein
Erbb2-interacting protein
Short name=Erbin
Gene names
Name:Erbb2ip
Synonyms:Erbin, Kiaa1225, Lap2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1402 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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 (via N-terminus) By similarity.

Subcellular location

Cell junctionhemidesmosome By similarity. Nucleus membrane. 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 By similarity. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. Ref.8

Post-translational modification

Isoform 2 is phosphorylated on Ser-1231 and Ser-1234.

Sequence similarities

Belongs to the LAP (LRR and PDZ) protein family.

Contains 17 LRR (leucine-rich) repeats.

Contains 1 PDZ (DHR) domain.

Sequence caution

The sequence BAC65755.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell junction
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainLeucine-rich repeat
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein targeting

Inferred from direct assay Ref.5. Source: MGI

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay Ref.5. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: Ensembl

hemidesmosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q80TH2-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: Q80TH2-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1243-1268: Missing.
Isoform 2 (identifier: Q80TH2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1203-1203: K → KSMLSRSFNSNLTAVSSSHYGSSRDLHGSQGSLALSVADGRGSGGHIFR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14021402Protein LAP2
PRO_0000188302

Regions

Repeat23 – 4422LRR 1
Repeat47 – 6822LRR 2
Repeat70 – 9122LRR 3
Repeat93 – 11422LRR 4
Repeat116 – 13722LRR 5
Repeat139 – 16123LRR 6
Repeat162 – 18322LRR 7
Repeat185 – 20622LRR 8
Repeat208 – 22922LRR 9
Repeat231 – 25222LRR 10
Repeat254 – 27522LRR 11
Repeat277 – 29822LRR 12
Repeat300 – 32122LRR 13
Repeat323 – 34422LRR 14
Repeat346 – 36722LRR 15
Repeat369 – 39123LRR 16
Repeat392 – 41322LRR 17
Domain1311 – 140090PDZ
Compositional bias928 – 9314Poly-Ser

Amino acid modifications

Modified residue4401Phosphoserine By similarity
Modified residue5991Phosphoserine Ref.7 Ref.9
Modified residue6001Phosphoserine Ref.7 Ref.9
Modified residue7121Phosphoserine Ref.9
Modified residue8541Phosphoserine Ref.9
Modified residue8691Phosphoserine By similarity
Modified residue9141Phosphothreonine By similarity
Modified residue9171Phosphotyrosine By similarity
Modified residue9281Phosphoserine By similarity
Modified residue9701Phosphotyrosine By similarity
Modified residue10971Phosphotyrosine Ref.6
Modified residue11501Phosphoserine By similarity
Modified residue12761Phosphoserine By similarity

Natural variations

Alternative sequence12031K → KSMLSRSFNSNLTAVSSSHY GSSRDLHGSQGSLALSVADG RGSGGHIFR in isoform 2.
VSP_010808
Alternative sequence1243 – 126826Missing in isoform 1.
VSP_010809

Experimental info

Sequence conflict2551L → P in BAC65755. Ref.1
Sequence conflict721 – 7233DKK → HAS in AAH28256. Ref.4
Sequence conflict908 – 9103VRS → ASG in AAF77047. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: DBAFF4BD1BC48019

FASTA1,402157,248
        10         20         30         40         50         60 
MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE LYLDANQIEE 

        70         80         90        100        110        120 
LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS KNGIQEFPEN IKNCKVLTIV 

       130        140        150        160        170        180 
EASVNPISKL PDGFSQLLNL TQLYLNDAFL EFLPANFGRL TKLQILELRE NQLKMLPKTM 

       190        200        210        220        230        240 
NRLTQLERLD LGSNEFTEVP EVLEQLSGLR EFWMDGNRLT FIPGFIGSLR QLTYLDVSKN 

       250        260        270        280        290        300 
NIEMVEEGIS TCENLQDFLL SSNSLQQLPE TIGSLKNVTT LKIDENQLMY LPDSIGGLRS 

       310        320        330        340        350        360 
IEELDCSFNE IEALPSSIGQ LTNMRTFAAD HNYLQQLPPE IGNWKNITVL FLHCNKLETL 

       370        380        390        400        410        420 
PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD NQSKPLIPLQ KETDTETQKM 

       430        440        450        460        470        480 
VLTNYMFPQQ PRTEDVMFIS DNESFNPALW EEQRKQRAQV AFECDEDKDE REAPPREGNL 

       490        500        510        520        530        540 
KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEESGRDLKQ HEDQQVVNKD KCVKTSESTT 

       550        560        570        580        590        600 
TKSKLDEREK YMNSVQKMSE PEAETNGGNL PVTASMKLSG NLKHIVNHDD VFEESEELSS 

       610        620        630        640        650        660 
DEEMKMAEMR PPLIESSINQ PKVVALSNNK KDDAKDADSL SDEVTHNSNQ NNSNCSSPSR 

       670        680        690        700        710        720 
MSDSVSLNTD SSQDTSLCSP VKQTPVDSNS KVRQEDENFN SLLQNGVNLN NSPEEKFKIN 

       730        740        750        760        770        780 
DKKDFKLPEY DLNIEEQLVL IEKDIDSKAT SDDSRQLDHI NMNINKLVTN NIFQPEVMER 

       790        800        810        820        830        840 
SKMQDIVLGT GFLSIHPKNE AEHIENGAKF PNLESINKVN GLCEDTAPSP GRVEPQKASS 

       850        860        870        880        890        900 
SADVGISKST EDLSPQRSGP TGAVVKSHSI TNMETGGLKI YDILGDDGPQ PPSAAVKIAS 

       910        920        930        940        950        960 
AVDGKNIVRS KSATLLYDQP LQVFTAASSS SELLSGTKAV FKFDSNHNPE EPDIIRAATV 

       970        980        990       1000       1010       1020 
SGPQSTPHLY GPPQYNVQYS GSATVKDTLW HPKQNPQIDP VSFPPQRLPR SESAENHSYA 

      1030       1040       1050       1060       1070       1080 
KHSANMNFSN HNNVRANTGY HLQQRLAPAR HGEMWAISPN DRLVPAVTRT TIQRQSSVSS 

      1090       1100       1110       1120       1130       1140 
TASVNLGDPT RRTEGDYLSY RELHSMGRTP VMSGSQRPLS ARAYSIDGPN TSRPQSARPS 

      1150       1160       1170       1180       1190       1200 
INEIPERTMS VSDFNYSRTS PSKRPNTRVG SEHSLLDPPG KSKVPHDWRE QVLRHIEAKK 

      1210       1220       1230       1240       1250       1260 
LEKHPQTSSP GECCQDDRFM SEEQNHPSGA LSHRGLPDSL MKMPLSNGQM GQPLRPQAHY 

      1270       1280       1290       1300       1310       1320 
SQTHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTHPHCS PRQGHELAKQ EIRVRVEKDP 

      1330       1340       1350       1360       1370       1380 
ELGFSISGGV GGRGNPFRPD DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG YSFINIEHGQ 

      1390       1400 
AVSLLKTFHN AVDLIIVREV SS 

« Hide

Isoform 1 [UniParc].

Checksum: 97A2B69F116DB166
Show »

FASTA1,376154,328
Isoform 2 [UniParc].

Checksum: 4D8113A7636EE4DC
Show »

FASTA1,450162,183

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-1376 (ISOFORMS 2 AND 3).
Strain: C57BL/6J.
Tissue: Skin and Spinal ganglion.
[4]"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 721-1402 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1160-1402 (ISOFORM 1).
Tissue: Colon and Mammary tumor.
[5]"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] OF 908-1402 (ISOFORM 3).
[6]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1097, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599 AND SER-600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Nuclear alpha1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytes."
Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., O'Connell T.D.
Circ. Res. 103:992-1000(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-600; SER-712 AND SER-854, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK122473 mRNA. Translation: BAC65755.1. Different initiation.
AC154310 Genomic DNA. No translation available.
CT009728 Genomic DNA. No translation available.
AK029054 mRNA. Translation: BAC26267.1.
AK051733 mRNA. Translation: BAC34742.1.
BC005691 mRNA. Translation: AAH05691.3.
BC028256 mRNA. Translation: AAH28256.1.
AF263743 mRNA. Translation: AAF77047.1.
UniGeneMm.277354.

3D structure databases

ProteinModelPortalQ80TH2.
SMRQ80TH2. Positions 26-460, 1273-1402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208523. 1 interaction.
IntActQ80TH2. 1 interaction.
MINTMINT-138078.

PTM databases

PhosphoSiteQ80TH2.

Proteomic databases

PaxDbQ80TH2.
PRIDEQ80TH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022222; ENSMUSP00000022222; ENSMUSG00000021709. [Q80TH2-1]
ENSMUST00000053927; ENSMUSP00000057956; ENSMUSG00000021709. [Q80TH2-2]
ENSMUST00000091269; ENSMUSP00000088813; ENSMUSG00000021709. [Q80TH2-3]
KEGGmmu:59079.
UCSCuc007rsk.2. mouse. [Q80TH2-3]
uc007rsm.1. mouse. [Q80TH2-1]

Organism-specific databases

CTD55914.
MGIMGI:1890169. Erbb2ip.
RougeSearch...

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00750000117705.
HOVERGENHBG052305.
KOK12796.
OMASDEEMKM.
OrthoDBEOG72C501.
TreeFamTF351429.

Gene expression databases

ArrayExpressQ80TH2.
BgeeQ80TH2.
CleanExMM_ERBB2IP.
GenevestigatorQ80TH2.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR001478. PDZ.
[Graphical view]
PfamPF12799. LRR_4. 2 hits.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS51450. LRR. 13 hits.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio314720.
PROQ80TH2.
SOURCESearch...

Entry information

Entry nameLAP2_MOUSE
AccessionPrimary (citable) accession number: Q80TH2
Secondary accession number(s): E9QND6 expand/collapse secondary AC list , Q8BQ14, Q8CE41, Q8K171, Q99JU3, Q9JI47
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot