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Reviewed, UniProtKB/Swiss-Prot Q8TEW0 (PARD3_HUMAN)

Last modified February 9, 2010. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Partitioning defective 3 homolog
      Short name=PARD-3
      Short name=PAR-3
Alternative name(s):
    Atypical PKC isotype-specific-interacting protein
      Short name=ASIP
    CTCL tumor antigen se2-5
    PAR3-alpha
Gene names
Name: PARD3
Synonyms: PAR3, PAR3A
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins.

Subunit structure

Interacts with PARD6A and PARD6B. Isoform 2, but not at least isoform 3 interacts with PRKCZ. Interacts with PRCKI By similarity. Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Interacts with F11R/JAM1 By similarity. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with LIMK2. Ref.1 Ref.4 Ref.10 Ref.11 Ref.16

Subcellular location

Endomembrane system. Cell junction. Cell junctiontight junction. Cell membrane. Cytoplasmcell cortex By similarity. Cytoplasmcytoskeleton. Note: Localized along the cell-cell contact region. Colocalizes with PARD6A and PRKCI at epithelial tight junctions. Colocalizes with the cortical actin that overlays the meiotic spindle during metaphase I and metaphase II By similarity.

Tissue specificity

Widely expressed. Ref.4

Domain

Contains a conserved N-terminal oligomerization domain (NTD) that is involved in oligomerization and is essential for proper subapical membrane localization By similarity.

Post-translational modification

Phosphorylated by PRKCZ. EGF-induced Tyr-1127 phosphorylation mediates dissociation from LIMK2. Ref.16 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Miscellaneous

Antibodies against PARD3 are present in sera from patients with cutaneous T-cell lymphomas.

Sequence similarities

Belongs to the PAR3 family.

Contains 3 PDZ (DHR) domains.

Sequence caution

The sequence AAG33676.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TEW0-1)

Also known as: A;

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: Q8TEW0-2)

Also known as: B; La;

The sequence of this isoform differs from the canonical sequence as follows:
     740-742: Missing.
Isoform 3 (identifier: Q8TEW0-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     195-238: Missing.
     557-569: Missing.
     740-742: Missing.
     827-856: Missing.
Isoform 4 (identifier: Q8TEW0-4)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     1025-1061: Missing.
Isoform 5 (identifier: Q8TEW0-5)

Also known as: E;

The sequence of this isoform differs from the canonical sequence as follows:
     195-238: Missing.
     557-569: Missing.
     740-742: Missing.
     857-857: I → S
     858-872: Missing.
     1025-1061: Missing.
Isoform 6 (identifier: Q8TEW0-6)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     557-569: Missing.
     740-742: Missing.
     827-856: Missing.
Isoform 7 (identifier: Q8TEW0-7)

Also known as: Lb;

The sequence of this isoform differs from the canonical sequence as follows:
     557-569: Missing.
     740-742: Missing.
     827-856: Missing.
     1025-1061: Missing.
Isoform 8 (identifier: Q8TEW0-8)

Also known as: Sa;

The sequence of this isoform differs from the canonical sequence as follows:
     740-742: Missing.
     1025-1034: RFGKHRKDDK → SLAKLKPEKR
     1035-1356: Missing.
Isoform 9 (identifier: Q8TEW0-9)

Also known as: Sb;

The sequence of this isoform differs from the canonical sequence as follows:
     557-569: Missing.
     740-742: Missing.
     827-856: Missing.
     1025-1034: RFGKHRKDDK → SLAKLKPEKR
     1035-1356: Missing.
Isoform 10 (identifier: Q8TEW0-10)

The sequence of this isoform differs from the canonical sequence as follows:
     740-742: Missing.
     827-856: Missing.
     857-858: IA → T
     1025-1034: RFGKHRKDDK → SLAKLKPEKR
     1035-1356: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13561356Partitioning defective 3 homolog
PRO_0000185069

Regions

Domain271 – 35989PDZ 1
Domain461 – 54686PDZ 2
Domain590 – 67788PDZ 3
Region712 – 936225Interacts with PRKCZ By similarity
Coiled coil1049 – 107729 Potential
Coiled coil1151 – 117424 Potential
Coiled coil1201 – 122424 Potential
Coiled coil1280 – 130122 Potential
Compositional bias984 – 104259Lys-rich

Amino acid modifications

Modified residue1431Phosphoserine Ref.20
Modified residue1441Phosphoserine Ref.15 Ref.20
Modified residue1741Phosphoserine Ref.22
Modified residue3831Phosphoserine Ref.12 Ref.18 Ref.20 Ref.21 Ref.24
Modified residue3881Phosphotyrosine Ref.23 Ref.24
Modified residue4891Phosphotyrosine Ref.17 Ref.23
Modified residue6921Phosphoserine Ref.21
Modified residue6951Phosphoserine Ref.20 Ref.21
Modified residue7151Phosphoserine Ref.20
Modified residue7171Phosphoserine Ref.20
Modified residue7191Phosphotyrosine Ref.23
Modified residue7281Phosphoserine Ref.20 Ref.21 Ref.24
Modified residue8091Phosphoserine Ref.21
Modified residue8271Phosphoserine By similarity
Modified residue8521Phosphoserine Ref.19 Ref.21 Ref.24
Modified residue8731Phosphoserine Ref.21
Modified residue10051N6-acetyllysine Ref.25
Modified residue10801Phosphotyrosine Ref.23
Modified residue11271Phosphotyrosine Ref.16 Ref.13 Ref.23

Natural variations

Alternative sequence195 – 23844Missing in isoform 3 and isoform 5.
VSP_007462
Alternative sequence557 – 56913Missing in isoform 3, isoform 5, isoform 6, isoform 7 and isoform 9.
VSP_007463
Alternative sequence740 – 7423Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10.
VSP_007464
Alternative sequence827 – 85630Missing in isoform 3, isoform 6, isoform 7, isoform 9 and isoform 10.
VSP_007465
Alternative sequence857 – 8582IA → T in isoform 10.
VSP_007467
Alternative sequence8571I → S in isoform 5.
VSP_007466
Alternative sequence858 – 87215Missing in isoform 5.
VSP_007468
Alternative sequence1025 – 106137Missing in isoform 4, isoform 5 and isoform 7.
VSP_007469
Alternative sequence1025 – 103410RFGKHRKDDK → SLAKLKPEKR in isoform 8, isoform 9 and isoform 10.
VSP_007470
Alternative sequence1035 – 1356322Missing in isoform 8, isoform 9 and isoform 10.
VSP_007471
Natural variant1071E → D: dbSNP rs1436731.
VAR_015663
Natural variant5751D → N: dbSNP rs3758459.
VAR_050453

Experimental info

Mutagenesis11271Y → F: Delayed epithelial tight junction assembly. Ref.16
Sequence conflict1901T → A in BAB55330. Ref.7
Sequence conflict2331L → Q in BAB55330. Ref.7
Sequence conflict5941N → S in BAB55330. Ref.7
Sequence conflict996 – 10005GKEKK → VELHE in BAA91366. Ref.7

Sequences

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

Last modified May 16, 2003. Version 2.
Checksum: A4FD3F4F9AD8B92A

FASTA1,356151,423
        10         20         30         40         50         60 
MKVTVCFGRT RVVVPCGDGH MKVFSLIQQA VTRYRKAIAK DPNYWIQVHR LEHGDGGILD 

        70         80         90        100        110        120 
LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS PEIFGSELGT NNVSAFQPYQ 

       130        140        150        160        170        180 
ATSEIEVTPS VLRANMPLHV RRSSDPALIG LSTSVSDSNF SSEEPSRKNP TRWSTTAGFL 

       190        200        210        220        230        240 
KQNTAGSPKT CDRKKDENYR SLPRDTSNWS NQFQRDNARS SLSASHPMVG KWLEKQEQDE 

       250        260        270        280        290        300 
DGTEEDNSRV EPVGHADTGL EHIPNFSLDD MVKLVEVPND GGPLGIHVVP FSARGGRTLG 

       310        320        330        340        350        360 
LLVKRLEKGG KAEHENLFRE NDCIVRINDG DLRNRRFEQA QHMFRQAMRT PIIWFHVVPA 

       370        380        390        400        410        420 
ANKEQYEQLS QSEKNNYYSS RFSPDSQYID NRSVNSAGLH TVQRAPRLNH PPEQIDSHSR 

       430        440        450        460        470        480 
LPHSAHPSGK PPSAPASAPQ NVFSTTVSSG YNTKKIGKRL NIQLKKGTEG LGFSITSRDV 

       490        500        510        520        530        540 
TIGGSAPIYV KNILPRGAAI QDGRLKAGDR LIEVNGVDLV GKSQEEVVSL LRSTKMEGTV 

       550        560        570        580        590        600 
SLLVFRQEDA FHPRELNAEP SQMQIPKETK AEDEDIVLTP DGTREFLTFE VPLNDSGSAG 

       610        620        630        640        650        660 
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL LGKTNQDAME 

       670        680        690        700        710        720 
TLRRSMSTEG NKRGMIQLIV ARRISKCNEL KSPGSPPGPE LPIETALDDR ERRISHSLYS 

       730        740        750        760        770        780 
GIEGLDESPS RNAALSRIMG ESGKYQLSPT VNMPQDDTVI IEDDRLPVLP PHLSDQSSSS 

       790        800        810        820        830        840 
SHDDVGFVTA DAGTWAKAAI SDSADCSLSP DVDPVLAFQR EGFGRQSMSE KRTKQFSDAS 

       850        860        870        880        890        900 
QLDFVKTRKS KSMDLGIADE TKLNTVDDQK AGSPSRDVGP SLGLKKSSSL ESLQTAVAEV 

       910        920        930        940        950        960 
TLNGDIPFHR PRPRIIRGRG CNESFRAAID KSYDKPAVDD DDEGMETLEE DTEESSRSGR 

       970        980        990       1000       1010       1020 
ESVSTASDQP SHSLERQMNG NQEKGDKTDR KKDKTGKEKK KDRDKEKDKM KAKKGMLKGL 

      1030       1040       1050       1060       1070       1080 
GDMFRFGKHR KDDKIEKTGK IKIQESFTSE EERIRMKQEQ ERIQAKTREF RERQARERDY 

      1090       1100       1110       1120       1130       1140 
AEIQDFHRTF GCDDELMYGG VSSYEGSMAL NARPQSPREG HMMDALYAQV KKPRNSKPSP 

      1150       1160       1170       1180       1190       1200 
VDSNRSTPSN HDRIQRLRQE FQQAKQDEDV EDRRRTYSFE QPWPNARPAT QSGRHSVSVE 

      1210       1220       1230       1240       1250       1260 
VQMQRQRQEE RESSQQAQRQ YSSLPRQSRK NASSVSQDSW EQNYSPGEGF QSAKENPRYS 

      1270       1280       1290       1300       1310       1320 
SYQGSRNGYL GGHGFNARVM LETQELLRQE QRRKEQQMKK QPPSEGPSNY DSYKKVQDPS 

      1330       1340       1350 
YAPPKGPFRQ DVPPSPSQVA RLNRLQTPEK GRPFYS 

« Hide

Isoform 2 (B) (La).

Checksum: BC531577B9C31AE3
Show »

FASTA1,353151,150
Isoform 3 (C).

Checksum: 92DF51B68081A4A2
Show »

FASTA1,266141,072
Isoform 4 (D).

Checksum: F5FBF3CE4E67163B
Show »

FASTA1,319146,877
Isoform 5 (E).

Checksum: C3C156C8811D49C2
Show »

FASTA1,244138,332
Isoform 6 (F).

Checksum: 57361092A273AC60
Show »

FASTA1,310146,276
Isoform 7 (Lb).

Checksum: 53C1A94D8CB7341E
Show »

FASTA1,273141,730
Isoform 8 (Sa).

Checksum: 40DD593636EAE999
Show »

FASTA1,031113,419
Isoform 9 (Sb).

Checksum: 89F2139B096F7F7F
Show »

FASTA988108,545
Isoform 10.

Checksum: 135A54F80C144606
Show »

FASTA1,000109,917

References

« Hide 'large scale' references
[1]"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
Joberty G., Petersen C., Gao L., Macara I.G.
Nat. Cell Biol. 2:531-539(2000) [PubMed: 10934474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH PARD6B.
Tissue: Kidney.
[2]"Down-regulated expression of atypical PKC-binding domain deleted asip isoforms in human hepatocellular carcinomas."
Fang C.M., Xu Y.H.
Cell Res. 11:223-229(2001) [PubMed: 11642408] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 7; 8 AND 9).
[3]"PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions."
Kohjima M., Noda Y., Takeya R., Saito N., Takeuchi K., Sumimoto H.
Biochem. Biophys. Res. Commun. 299:641-646(2002) [PubMed: 12459187] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[4]"Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties."
Gao L., Macara I.G., Joberty G.
Gene 294:99-107(2002) [PubMed: 12234671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), INTERACTION WITH PARD6B AND PRKCZ, TISSUE SPECIFICITY.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-1356 (ISOFORM 10).
Tissue: Hepatoma and Ovarian carcinoma.
[8]"Serological detection of cutaneous T-cell lymphoma-associated antigens."
Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.
Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001) [PubMed: 11149944] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 313-992.
Tissue: Testis.
[9]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1356.
Tissue: Lung.
[10]"The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1."
Johansson A.-S., Driessens M., Aspenstroem P.
J. Cell Sci. 113:3267-3275(2000) [PubMed: 10954424] [Abstract]
Cited for: INTERACTION WITH PARD6A.
[11]"Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures."
Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., Ohno S.
J. Cell Biol. 152:1183-1196(2001) [PubMed: 11257119] [Abstract]
Cited for: SUBUNIT OF A COMPLEX CONTAINING PARD6B AND PRKCI.
Tissue: Kidney.
[12]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1127, MASS SPECTROMETRY.
Tissue: Epithelium.
[14]"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
Cell 125:535-548(2006) [PubMed: 16678097] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; AMOT; MPP5 AND INADL.
[15]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling."
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.
EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1127, MASS SPECTROMETRY, INTERACTION WITH LIMK2, MUTAGENESIS OF TYR-1127.
[17]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-489, MASS SPECTROMETRY.
[18]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, MASS SPECTROMETRY.
Tissue: Epithelium.
[19]"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: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, MASS SPECTROMETRY.
Tissue: Platelet.
[20]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-144; SER-383; SER-695; SER-715; SER-717 AND SER-728, MASS SPECTROMETRY.
[21]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-692; SER-695; SER-728; SER-809; SER-852 AND SER-873, MASS SPECTROMETRY.
[22]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, MASS SPECTROMETRY.
[23]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-388; TYR-489; TYR-719; TYR-1080 AND TYR-1127, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[24]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; TYR-388; SER-728 AND SER-852, MASS SPECTROMETRY.
Tissue: T-cell.
[25]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1005, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF252293 mRNA. Translation: AAF71530.1.
AF196185 mRNA. Translation: AAK27891.1.
AF196186 mRNA. Translation: AAK27892.1.
AF332592 mRNA. Translation: AAK69192.1.
AF332593 mRNA. Translation: AAK69193.1.
AB073671 mRNA. Translation: BAC54037.1.
AF467002 mRNA. Translation: AAL76042.1.
AF467003 mRNA. Translation: AAL76043.1.
AF467004 mRNA. Translation: AAL76044.1.
AF467005 mRNA. Translation: AAL76045.1.
AF467006 mRNA. Translation: AAL76046.1.
AL360233 expand/collapse EMBL AC list , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71161.1.
AL360233 expand/collapse EMBL AC list , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71162.1.
AL360233 expand/collapse EMBL AC list , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71163.1.
AL360233 expand/collapse EMBL AC list , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71166.1.
AL360233 expand/collapse EMBL AC list , AL138768, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71167.1.
AL160409 expand/collapse EMBL AC list , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73524.1.
AL160409 expand/collapse EMBL AC list , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73525.1.
AL160409 expand/collapse EMBL AC list , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73526.1.
AL160409 expand/collapse EMBL AC list , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73529.1.
AL450337 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15036.1.
AL450337 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15037.1.
AL450337 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15038.1.
AL450337 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15040.1.
AL450337 expand/collapse EMBL AC list , AL138768, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15041.1.
AL138768 expand/collapse EMBL AC list , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16985.1.
AL138768 expand/collapse EMBL AC list , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16986.1.
AL138768 expand/collapse EMBL AC list , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16987.1.
AL138768 expand/collapse EMBL AC list , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16989.1.
AL138768 expand/collapse EMBL AC list , AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16991.1.
AL390766 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17304.1.
AL390766 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17305.1.
AL390766 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17306.1.
AL390766 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17309.1.
AL390766 expand/collapse EMBL AC list , AL138768, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17310.1.
AL392123 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17327.1.
AL392123 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17328.1.
AL392123 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17329.1.
AL392123 expand/collapse EMBL AC list , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17332.1.
AL392123 expand/collapse EMBL AC list , AL138768, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17333.1.
AK000761 mRNA. Translation: BAA91366.1. Different initiation.
AK027735 mRNA. Translation: BAB55330.1. Different initiation.
AF177228 mRNA. Translation: AAG33676.1. Sequence problems.
CH471072 Genomic DNA. Translation: EAW85932.1.
BC011711 mRNA. Translation: AAH11711.2.
IPIIPI00045423.
IPI00154915.
IPI00163607.
IPI00163608.
IPI00165621.
IPI00179063.
IPI00294934.
IPI00301595.
IPI00301597.
IPI00301605.
RefSeqNP_062565.2.
UniGeneHs.131489

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KOMNMR-A451-549[»]
SMRQ8TEW0. Positions 2-83, 269-363, 279-549, 458-682, 582-685.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8TEW0. 18 interactions.
STRINGQ8TEW0.

PTM databases

PhosphoSiteQ8TEW0.

Proteomic databases

PRIDEQ8TEW0.

Genome annotation databases

EnsemblENST00000374789; ENSP00000363921; ENSG00000148498; Homo sapiens. [Genome view]
GeneID56288.
KEGGhsa:56288.
UCSCuc001ixg.1. human.
uc001ixh.1. human.
uc001ixi.1. human.
uc001ixk.1. human.
uc001ixl.1. human.
uc001ixm.1. human.
uc001ixn.1. human.
uc001ixp.1. human.
uc001ixq.1. human.
uc001ixr.1. human.

Organism-specific databases

CTD56288.
GeneCardsGC10M034438.
H-InvDBHIX0008758.
HIX0035395.
HGNCHGNC:16051. PARD3.
MIM606745. gene.
PharmGKBPA32936.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8TEW0.
InParanoidQ8TEW0.
OMARTKQFSD.
PhylomeDBQ8TEW0.

Enzyme and pathway databases

ReactomeREACT_20676. Cell junction organization.

Gene expression databases

ArrayExpressQ8TEW0.
BgeeQ8TEW0.
GenevestigatorQ8TEW0.
GermOnlineENSG00000148498. Homo sapiens.

Family and domain databases

InterProIPR001478. PDZ/DHR/GLGF.
[Graphical view]
PfamPF00595. PDZ. 3 hits.
[Graphical view]
SMARTSM00228. PDZ. 3 hits.
[Graphical view]
PROSITEPS50106. PDZ. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio61959.
SOURCESearch...

Entry information

Entry namePARD3_HUMAN
AccessionPrimary (citable) accession number: Q8TEW0
Secondary accession number(s): Q5T2U1 expand/collapse secondary AC list , Q5VWV0, Q5VWV3, Q5VWV4, Q5VWV5, Q8TEW1, Q8TEW2, Q8TEW3, Q96K28, Q96RM6, Q96RM7, Q9BY57, Q9BY58, Q9HC48, Q9NWL4, Q9NYE6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: February 9, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents