Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96RT1 (LAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

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

Names and origin

Protein namesRecommended name:
Protein LAP2
Alternative name(s):
Densin-180-like protein
Erbb2-interacting protein
Short name=Erbin
Gene names
Name:ERBB2IP
Synonyms:ERBIN, KIAA1225, LAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1412 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 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state. Ref.1

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 Isoform 3 (via N-terminus). Ref.1 Ref.2 Ref.8

Subcellular location

Cell junctionhemidesmosome. 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. Ref.1 Ref.2

Tissue specificity

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

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 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.

Ontologies

Keywords
   Cellular componentCell junction
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainLeucine-rich repeat
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbasal protein localization

Non-traceable author statement Ref.2. Source: UniProtKB

cell adhesion

Non-traceable author statement Ref.2. Source: UniProtKB

cell cycle

Non-traceable author statement Ref.2. Source: UniProtKB

cell growth

Non-traceable author statement Ref.2. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement Ref.2. Source: UniProtKB

establishment or maintenance of epithelial cell apical/basal polarity

Non-traceable author statement Ref.2. Source: UniProtKB

integrin-mediated signaling pathway

Non-traceable author statement Ref.2. Source: UniProtKB

intermediate filament cytoskeleton organization

Non-traceable author statement Ref.2. Source: UniProtKB

protein targeting

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentbasal plasma membrane

Non-traceable author statement Ref.2. Source: UniProtKB

basement membrane

Traceable author statement Ref.1. Source: ProtInc

cytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

hemidesmosome

Inferred from direct assay Ref.2. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionErbB-2 class receptor binding

Traceable author statement Ref.2. Source: UniProtKB

integrin binding

Inferred from physical interaction Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12047349. Source: IntAct

structural constituent of cytoskeleton

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKP4Q995693EBI-8449250,EBI-726447

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96RT1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96RT1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1252: Missing.
Isoform 3 (identifier: Q96RT1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1252: Missing.
     1268-1278: Missing.
Isoform 4 (identifier: Q96RT1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1252: Missing.
     1353-1377: Missing.
Isoform 5 (identifier: Q96RT1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1252: Missing.
     1253-1267: Missing.
Isoform 6 (identifier: Q96RT1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1252: Missing.
     1322-1352: Missing.
Isoform 7 (identifier: Q96RT1-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1252: Missing.
     1253-1267: Missing.
     1268-1278: Missing.
     1279-1321: Missing.
Isoform 8 (identifier: Q96RT1-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1252: KHPQTSSSGD...KDVPPDSLMK → SMLSRSFNSN...RRGSGGHIFR
Note: No experimental confirmation available.
Isoform 9 (identifier: Q96RT1-9)

The sequence of this isoform differs from the canonical sequence as follows:
     531-534: Missing.
     1212-1252: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14121412Protein LAP2
PRO_0000188301

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
Domain1321 – 141090PDZ
Compositional bias930 – 9345Poly-Ser

Amino acid modifications

Modified residue4401Phosphoserine Ref.11
Modified residue5691Phosphoserine Ref.13 Ref.15
Modified residue6021Phosphoserine Ref.15
Modified residue6031Phosphoserine Ref.15
Modified residue7151Phosphoserine By similarity
Modified residue8571Phosphoserine Ref.13
Modified residue8721Phosphoserine Ref.14
Modified residue9171Phosphothreonine Ref.13 Ref.14
Modified residue9201Phosphotyrosine Ref.9
Modified residue9311Phosphoserine Ref.14
Modified residue9721Phosphotyrosine Ref.10
Modified residue11041Phosphotyrosine By similarity
Modified residue11581Phosphoserine Ref.14
Modified residue12861Phosphoserine Ref.13

Natural variations

Alternative sequence531 – 5344Missing in isoform 9.
VSP_047389
Alternative sequence1212 – 125241Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 9.
VSP_010802
Alternative sequence1212 – 125241KHPQT…DSLMK → SMLSRSFNSNFTTVSSFHCG SSRDLHGSQGSLALSVADRR GSGGHIFR in isoform 8.
VSP_044536
Alternative sequence1253 – 126715Missing in isoform 5 and isoform 7.
VSP_010803
Alternative sequence1268 – 127811Missing in isoform 3 and isoform 7.
VSP_010804
Alternative sequence1279 – 132143Missing in isoform 7.
VSP_010805
Alternative sequence1322 – 135231Missing in isoform 6.
VSP_010806
Alternative sequence1353 – 137725Missing in isoform 4.
VSP_010807
Natural variant2741S → L. Ref.7
Corresponds to variant rs3213837 [ dbSNP | Ensembl ].
VAR_019346
Natural variant3131A → V. Ref.7
Corresponds to variant rs191137999 [ dbSNP | Ensembl ].
VAR_068905
Natural variant7461K → E.
Corresponds to variant rs16894812 [ dbSNP | Ensembl ].
VAR_028304
Natural variant9141K → R.
Corresponds to variant rs34521887 [ dbSNP | Ensembl ].
VAR_046673
Natural variant10891G → V.
Corresponds to variant rs35601230 [ dbSNP | Ensembl ].
VAR_046674
Natural variant11121S → L.
Corresponds to variant rs3805466 [ dbSNP | Ensembl ].
VAR_019347
Natural variant12071K → E. Ref.2
VAR_019348

Experimental info

Sequence conflict2711T → P in AAI15013. Ref.7
Sequence conflict5471D → G in AAI15013. Ref.7
Sequence conflict8051E → G in BAA91538. Ref.5
Sequence conflict8131Y → C in AAK69431. Ref.2
Sequence conflict8481G → C in BAG65463. Ref.5
Sequence conflict10471R → S in BAG65463. Ref.5
Sequence conflict12051E → G in AAI15013. Ref.7
Sequence conflict12671Q → P in AAI15013. Ref.7
Sequence conflict13281K → R in AAI15013. Ref.7

Secondary structure

.................... 1412
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: 304DFC81578CF671

FASTA1,412158,298
        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 EVLEQLSGLK EFWMDANRLT FIPGFIGSLK QLTYLDVSKN 

       250        260        270        280        290        300 
NIEMVEEGIS TCENLQDLLL SSNSLQQLPE TIGSLKNITT LKIDENQLMY LPDSIGGLIS 

       310        320        330        340        350        360 
VEELDCSFNE VEALPSSIGQ LTNLRTFAAD HNYLQQLPPE IGSWKNITVL FLHSNKLETL 

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

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

       490        500        510        520        530        540 
KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEDSGRDLKP HEDQQDINKD VGVKTSESTT 

       550        560        570        580        590        600 
TVKSKVDERE KYMIGNSVQK ISEPEAEISP GSLPVTANMK ASENLKHIVN HDDVFEESEE 

       610        620        630        640        650        660 
LSSDEEMKMA EMRPPLIETS INQPKVVALS NNKKDDTKET DSLSDEVTHN SNQNNSNCSS 

       670        680        690        700        710        720 
PSRMSDSVSL NTDSSQDTSL CSPVKQTHID INSKIRQEDE NFNSLLQNGD ILNSSTEEKF 

       730        740        750        760        770        780 
KAHDKKDFNL PEYDLNVEER LVLIEKSVDS TATADDTHKL DHINMNLNKL ITNDTFQPEI 

       790        800        810        820        830        840 
MERSKTQDIV LGTSFLSINS KEETEHLENG NKYPNLESVN KVNGHSEETS QSPNRTEPHD 

       850        860        870        880        890        900 
SDCSVDLGIS KSTEDLSPQK SGPVGSVVKS HSITNMEIGG LKIYDILSDN GPQQPSTTVK 

       910        920        930        940        950        960 
ITSAVDGKNI VRSKSATLLY DQPLQVFTGS SSSSDLISGT KAIFKFDSNH NPEEPNIIRG 

       970        980        990       1000       1010       1020 
PTSGPQSAPQ IYGPPQYNIQ YSSSAAVKDT LWHSKQNPQI DHASFPPQLL PRSESTENQS 

      1030       1040       1050       1060       1070       1080 
YAKHSANMNF SNHNNVRANT AYHLHQRLGP ARHGEMWAIS PNDRLIPAVT RSTIQRQSSV 

      1090       1100       1110       1120       1130       1140 
SSTASVNLGD PGSTRRAQIP EGDYLSYREF HSAGRTPPMM PGSQRPLSAR TYSIDGPNAS 

      1150       1160       1170       1180       1190       1200 
RPQSARPSIN EIPERTMSVS DFNYSRTSPS KRPNARVGSE HSLLDPPGKS KVPRDWREQV 

      1210       1220       1230       1240       1250       1260 
LRHIEAKKLE KKHPQTSSSG DPCQDGIFIS GQQNYSSATL SHKDVPPDSL MKMPLSNGQM 

      1270       1280       1290       1300       1310       1320 
GQPLRPQANY SQIHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTQPHCS PRQGHELAKQ 

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

      1390       1400       1410 
YSFINIEHGQ AVSLLKTFQN TVELIIVREV SS 

« Hide

Isoform 2 [UniParc].

Checksum: C8F24683B0C4324D
Show »

FASTA1,371153,926
Isoform 3 [UniParc].

Checksum: A56B9384680DA710
Show »

FASTA1,360152,653
Isoform 4 [UniParc].

Checksum: 19D7B81B5A934C2E
Show »

FASTA1,346151,252
Isoform 5 [UniParc].

Checksum: 9662C85F03C8F08B
Show »

FASTA1,356152,290
Isoform 6 [UniParc].

Checksum: 12B24ADE16A5F537
Show »

FASTA1,340150,602
Isoform 7 [UniParc].

Checksum: E436063ACDA2C1A4
Show »

FASTA1,302146,086
Isoform 8 [UniParc].

Checksum: 9E18163421DBE278
Show »

FASTA1,419159,024
Isoform 9 [UniParc].

Checksum: C1F031AD4CA0746B
Show »

FASTA1,367153,543

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34172.1. [Q96RT1-7]
CCDS3990.1. [Q96RT1-2]
CCDS58951.1. [Q96RT1-9]
CCDS58952.1. [Q96RT1-8]
CCDS58953.1. [Q96RT1-1]
CCDS58954.1. [Q96RT1-4]
RefSeqNP_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]
UniGeneHs.591774.
Hs.597241.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ96RT1.
SMRQ96RT1. Positions 26-455, 1283-1412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120997. 70 interactions.
IntActQ96RT1. 14 interactions.
MINTMINT-199447.
STRING9606.ENSP00000370330.

PTM databases

PhosphoSiteQ96RT1.

Polymorphism databases

DMDM116242614.

Proteomic databases

MaxQBQ96RT1.
PaxDbQ96RT1.
PRIDEQ96RT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284037; ENSP00000284037; ENSG00000112851. [Q96RT1-1]
ENST00000380935; ENSP00000370322; ENSG00000112851. [Q96RT1-7]
ENST00000380936; ENSP00000370323; ENSG00000112851. [Q96RT1-6]
ENST00000380938; ENSP00000370325; ENSG00000112851. [Q96RT1-4]
ENST00000380939; ENSP00000370326; ENSG00000112851. [Q96RT1-3]
ENST00000380943; ENSP00000370330; ENSG00000112851. [Q96RT1-2]
ENST00000506030; ENSP00000426632; ENSG00000112851. [Q96RT1-8]
ENST00000508515; ENSP00000422015; ENSG00000112851. [Q96RT1-7]
ENST00000511297; ENSP00000422766; ENSG00000112851. [Q96RT1-9]
GeneID55914.
KEGGhsa:55914.
UCSCuc003jui.2. human. [Q96RT1-2]
uc003juj.2. human. [Q96RT1-7]
uc003juk.2. human. [Q96RT1-1]
uc011cqy.2. human. [Q96RT1-4]

Organism-specific databases

CTD55914.
GeneCardsGC05P065258.
HGNCHGNC:15842. ERBB2IP.
HPAHPA048606.
MIM606944. gene.
neXtProtNX_Q96RT1.
PharmGKBPA27845.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000060229.
HOVERGENHBG052305.
InParanoidQ96RT1.
KOK12796.
OMASDEEMKM.
OrthoDBEOG72C501.
PhylomeDBQ96RT1.
TreeFamTF351429.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ96RT1.

Gene expression databases

ArrayExpressQ96RT1.
BgeeQ96RT1.
CleanExHS_ERBB2IP.
GenevestigatorQ96RT1.

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.
PF13855. LRR_8. 2 hits.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS51450. LRR. 15 hits.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERBB2IP. human.
EvolutionaryTraceQ96RT1.
GeneWikiErbin_(protein).
GenomeRNAi55914.
NextBio61305.
PROQ96RT1.
SOURCESearch...

Entry information

Entry nameLAP2_HUMAN
AccessionPrimary (citable) accession number: Q96RT1
Secondary accession number(s): A0AVR1 expand/collapse secondary AC list , B4E3F1, B7ZLV9, E7EQW9, E9PCR8, Q1RMD0, Q86W38, Q9NR18, Q9NW48, Q9ULJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM