Q8TEW0 (PARD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 121.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Partitioning defective 3 homolog Short name=PAR-3 Short name=PARD-3 Alternative name(s): Atypical PKC isotype-specific-interacting protein Short name=ASIP CTCL tumor antigen se2-5 PAR3-alpha | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1356 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. Targets the phosphatase PTEN to cell junctions By similarity. 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. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons. Ref.18 |
| Subunit structure | Interacts (via PDZ 1 domain) with F11R/JAM1, PARD6A and PARD6B. Isoform 2, but not at least isoform 3 interacts with PRKCZ. Interacts with PRCKI and CDH5. Interacts (via PDZ 3 domain) with PTEN (via C-terminus) By similarity. Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with LIMK2, AURKA and AURKB. Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with ECT2 and FBF1. Ref.1 Ref.4 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.20 |
| Subcellular location | Endomembrane system. Cell junction. Cell junction › tight junction. Cell membrane. Cytoplasm › cell cortex By similarity. Cytoplasm › cytoskeleton. 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. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. Ref.20 |
| 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. The second PDZ domain mediates interaction with membranes containing phosphoinositol lipids By similarity. |
| Post-translational modification | Phosphorylation at Ser-827 by PRKCZ and PRKCI occurs at the most apical tip of epithelial cell-cell contacts during the initial phase of tight junction formation and may promote dissociation of the complex with PARD6. EGF-induced Tyr-1127 phosphorylation mediates dissociation from LIMK2 By similarity. Phosphorylation by AURKA at Ser-962 is required for the normal establishment of neuronal polarity. |
| 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: Contaminating sequence. Potential poly-A sequence. The sequence BAA91366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55330.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| PARD6A | Q9NPB6 | 7 | EBI-81968,EBI-81876 | |
| PARD6B | Q9BYG5 | 4 | EBI-81968,EBI-295391 | |
| Pard6b | Q9JK83 | 2 | EBI-81968,EBI-81861 | From a different organism. |
| PARD6G | Q9BYG4 | 3 | EBI-81968,EBI-295417 | |
| PNMA1 | Q8ND90 | 4 | EBI-81968,EBI-302345 | |
| PRKCI | P41743 | 3 | EBI-81968,EBI-286199 | |
| YWHAH | Q04917 | 6 | EBI-81968,EBI-306940 | |
| YWHAZ | P63104 | 3 | EBI-81968,EBI-347088 |
Alternative products
| This entry describes 11 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. | ||||||
| Isoform 11 (identifier: Q8TEW0-11) The sequence of this isoform differs from the canonical sequence as follows: 557-569: Missing. 740-742: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1356 | 1356 | Partitioning defective 3 homolog | PRO_0000185069 | |||||||||||||||||||||
Regions | |||||||||||||||||||||||||
| Domain | 271 – 359 | 89 | PDZ 1 | ||||||||||||||||||||||
| Domain | 461 – 546 | 86 | PDZ 2 | ||||||||||||||||||||||
| Domain | 590 – 677 | 88 | PDZ 3 | ||||||||||||||||||||||
| Region | 712 – 936 | 225 | Interacts with PRKCI and PRKCZ By similarity | ||||||||||||||||||||||
| Coiled coil | 1049 – 1077 | 29 | Potential | ||||||||||||||||||||||
| Coiled coil | 1151 – 1174 | 24 | Potential | ||||||||||||||||||||||
| Coiled coil | 1201 – 1224 | 24 | Potential | ||||||||||||||||||||||
| Coiled coil | 1280 – 1301 | 22 | Potential | ||||||||||||||||||||||
| Compositional bias | 984 – 1042 | 59 | Lys-rich | ||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||
| Modified residue | 144 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 383 | 1 | Phosphoserine Ref.16 Ref.17 Ref.19 Ref.21 Ref.23 | ||||||||||||||||||||||
| Modified residue | 692 | 1 | Phosphoserine Ref.17 | ||||||||||||||||||||||
| Modified residue | 695 | 1 | Phosphoserine Ref.16 Ref.17 | ||||||||||||||||||||||
| Modified residue | 717 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 728 | 1 | Phosphoserine Ref.17 Ref.19 Ref.21 | ||||||||||||||||||||||
| Modified residue | 809 | 1 | Phosphoserine Ref.17 | ||||||||||||||||||||||
| Modified residue | 827 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 852 | 1 | Phosphoserine Ref.17 Ref.19 Ref.21 Ref.23 | ||||||||||||||||||||||
| Modified residue | 873 | 1 | Phosphoserine Ref.17 Ref.21 Ref.23 | ||||||||||||||||||||||
| Modified residue | 962 | 1 | Phosphoserine; by AURKA Ref.18 | ||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||
| Alternative sequence | 195 – 238 | 44 | Missing in isoform 3 and isoform 5. | VSP_007462 | |||||||||||||||||||||
| Alternative sequence | 557 – 569 | 13 | Missing in isoform 3, isoform 5, isoform 6, isoform 7, isoform 9 and isoform 11. | VSP_007463 | |||||||||||||||||||||
| Alternative sequence | 740 – 742 | 3 | Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11. | VSP_007464 | |||||||||||||||||||||
| Alternative sequence | 827 – 856 | 30 | Missing in isoform 3, isoform 6, isoform 7, isoform 9 and isoform 10. | VSP_007465 | |||||||||||||||||||||
| Alternative sequence | 857 – 858 | 2 | IA → T in isoform 10. | VSP_007467 | |||||||||||||||||||||
| Alternative sequence | 857 | 1 | I → S in isoform 5. | VSP_007466 | |||||||||||||||||||||
| Alternative sequence | 858 – 872 | 15 | Missing in isoform 5. | VSP_007468 | |||||||||||||||||||||
| Alternative sequence | 1025 – 1061 | 37 | Missing in isoform 4, isoform 5 and isoform 7. | VSP_007469 | |||||||||||||||||||||
| Alternative sequence | 1025 – 1034 | 10 | RFGKHRKDDK → SLAKLKPEKR in isoform 8, isoform 9 and isoform 10. | VSP_007470 | |||||||||||||||||||||
| Alternative sequence | 1035 – 1356 | 322 | Missing in isoform 8, isoform 9 and isoform 10. | VSP_007471 | |||||||||||||||||||||
| Natural variant | 107 | 1 | E → D. Corresponds to variant rs1436731 [ dbSNP | Ensembl ]. | VAR_015663 | |||||||||||||||||||||
| Natural variant | 575 | 1 | D → N. Corresponds to variant rs3758459 [ dbSNP | Ensembl ]. | VAR_050453 | |||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||
| Mutagenesis | 962 | 1 | S → A: Abolishes phosphorylation by AURKA. Ref.18 | ||||||||||||||||||||||
| Mutagenesis | 1127 | 1 | Y → F: Delayed epithelial tight junction assembly. | ||||||||||||||||||||||
| Sequence conflict | 190 | 1 | T → A in BAB55330. Ref.8 | ||||||||||||||||||||||
| Sequence conflict | 233 | 1 | L → Q in BAB55330. Ref.8 | ||||||||||||||||||||||
| Sequence conflict | 594 | 1 | N → S in BAB55330. Ref.8 | ||||||||||||||||||||||
| Sequence conflict | 764 | 1 | D → N in AAH71566. Ref.7 | ||||||||||||||||||||||
| Sequence conflict | 996 – 1000 | 5 | GKEKK → VELHE in BAA91366. Ref.8 | ||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||
| Beta strand | 458 – 465 | 8 | |||||||||||||||||||||||
| Beta strand | 473 – 476 | 4 | |||||||||||||||||||||||
| Beta strand | 481 – 485 | 5 | |||||||||||||||||||||||
| Beta strand | 488 – 493 | 6 | |||||||||||||||||||||||
| Helix | 498 – 501 | 4 | |||||||||||||||||||||||
| Beta strand | 507 – 514 | 8 | |||||||||||||||||||||||
| Helix | 524 – 533 | 10 | |||||||||||||||||||||||
| Beta strand | 539 – 546 | 8 | |||||||||||||||||||||||
Sequences
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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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. Rogers J.Nature 429:375-381(2004) [PubMed] [Europe PMC] [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. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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] (ISOFORM 11), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1356 (ISOFORM 1). Tissue: Lung and Placenta. |
| [8] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 955-1356 (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-1356 (ISOFORM 10). Tissue: Hepatoma and Ovarian carcinoma. |
| [9] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 313-992. Tissue: Testis. |
| [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SUBUNIT OF A COMPLEX CONTAINING PARD6B AND PRKCI. Tissue: Kidney. |
| [12] | "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell. |
| [13] | "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity." Liu X.F., Ishida H., Raziuddin R., Miki T. Mol. Cell. Biol. 24:6665-6675(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ECT2. |
| [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; AMOT; MPP5 AND INADL. |
| [15] | "The keratin-binding protein Albatross regulates polarization of epithelial cells." Sugimoto M., Inoko A., Shiromizu T., Nakayama M., Zou P., Yonemura S., Hayashi Y., Izawa I., Sasoh M., Uji Y., Kaibuchi K., Kiyono T., Inagaki M. J. Cell Biol. 183:19-28(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FBF1. |
| [16] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-695, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "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-383; SER-692; SER-695; SER-728; SER-809; SER-852 AND SER-873, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "Phosphorylation of the par polarity complex protein Par3 at serine 962 is mediated by aurora A and regulates its function in neuronal polarity." Khazaei M.R., Puschel A.W. J. Biol. Chem. 284:33571-33579(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AURKA AND AURKB, FUNCTION, MUTAGENESIS OF SER-962, PHOSPHORYLATION AT SER-962. |
| [19] | "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-383; SER-728 AND SER-852, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [20] | "CCM1 regulates vascular-lumen organization by inducing endothelial polarity." Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G., Chapon F., Dejana E. J. Cell Sci. 123:1073-1080(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT. |
| [21] | "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-383; SER-728; SER-852 AND SER-873, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [22] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [23] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-852 AND SER-873, MASS SPECTROMETRY. |
| [24] | "Rapid, robotic, small-scale protein production for NMR screening and structure determination." Jensen D.R., Woytovich C., Li M., Duvnjak P., Cassidy M.S., Frederick R.O., Bergeman L.F., Peterson F.C., Volkman B.F. Protein Sci. 19:570-578(2010) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 451-549. |
| + | 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 AL450337 Genomic DNA. Translation: CAH71161.1.AL360233 AL450337 Genomic DNA. Translation: CAH71162.1.AL360233 AL450337 Genomic DNA. Translation: CAH71163.1.AL360233 AL450337 Genomic DNA. Translation: CAH71165.1.AL360233 AL450337 Genomic DNA. Translation: CAH71166.1.AL360233 AL450337 Genomic DNA. Translation: CAH71167.1.AL160409 AL450337 Genomic DNA. Translation: CAH73524.1.AL160409 AL450337 Genomic DNA. Translation: CAH73525.1.AL160409 AL450337 Genomic DNA. Translation: CAH73526.1.AL160409 AL450337 Genomic DNA. Translation: CAH73528.1.AL160409 AL450337 Genomic DNA. Translation: CAH73529.1.AL450337 AL392123 Genomic DNA. Translation: CAI15036.1.AL450337 AL392123 Genomic DNA. Translation: CAI15037.1.AL450337 AL392123 Genomic DNA. Translation: CAI15038.1.AL450337 AL392123 Genomic DNA. Translation: CAI15039.1.AL450337 AL392123 Genomic DNA. Translation: CAI15040.1.AL450337 AL392123 Genomic DNA. Translation: CAI15041.1.AL138768 AL450337 Genomic DNA. Translation: CAI16985.1.AL138768 AL450337 Genomic DNA. Translation: CAI16986.1.AL138768 AL450337 Genomic DNA. Translation: CAI16987.1.AL138768 AL450337 Genomic DNA. Translation: CAI16988.1.AL138768 AL450337 Genomic DNA. Translation: CAI16989.1.AL138768 AL450337 Genomic DNA. Translation: CAI16991.1.AL390766 AL450337 Genomic DNA. Translation: CAI17304.1.AL390766 AL450337 Genomic DNA. Translation: CAI17305.1.AL390766 AL450337 Genomic DNA. Translation: CAI17306.1.AL390766 AL450337 Genomic DNA. Translation: CAI17308.1.AL390766 AL450337 Genomic DNA. Translation: CAI17309.1.AL390766 AL450337 Genomic DNA. Translation: CAI17310.1.AL392123 AL450337 Genomic DNA. Translation: CAI17327.1.AL392123 AL450337 Genomic DNA. Translation: CAI17328.1.AL392123 AL450337 Genomic DNA. Translation: CAI17329.1.AL392123 AL450337 Genomic DNA. Translation: CAI17331.1.AL392123 AL450337 Genomic DNA. Translation: CAI17332.1.AL392123 AL450337 Genomic DNA. Translation: CAI17333.1.CH471072 Genomic DNA. Translation: EAW85932.1. CH471072 Genomic DNA. Translation: EAW85934.1. BC011711 mRNA. Translation: AAH11711.2. BC071566 mRNA. Translation: AAH71566.1. AK000761 mRNA. Translation: BAA91366.1. Different initiation. AK027735 mRNA. Translation: BAB55330.1. Different initiation. AF177228 mRNA. Translation: AAG33676.1. Sequence problems. | ||||||||||||
| IPI | IPI00045423. IPI00154915. IPI00163607. IPI00163608. IPI00165621. IPI00179063. IPI00294934. IPI00301595. IPI00301597. IPI00301605. IPI00984283. | ||||||||||||
| RefSeq | NP_001171714.1. NM_001184785.1. NP_001171715.1. NM_001184786.1. NP_001171716.1. NM_001184787.1. NP_001171717.1. NM_001184788.1. NP_001171718.1. NM_001184789.1. NP_001171719.1. NM_001184790.1. NP_001171720.1. NM_001184791.1. NP_001171721.1. NM_001184792.1. NP_001171722.1. NM_001184793.1. NP_001171723.1. NM_001184794.1. NP_062565.2. NM_019619.3. | ||||||||||||
| UniGene | Hs.131489. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q8TEW0. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-31315N. | ||||||||||||
| IntAct | Q8TEW0. 17 interactions. | ||||||||||||
| MINT | MINT-1342655. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q8TEW0. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 30913162. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q8TEW0. | ||||||||||||
| PRIDE | Q8TEW0. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000340077; ENSP00000341844; ENSG00000148498. ENST00000346874; ENSP00000340591; ENSG00000148498. ENST00000350537; ENSP00000311986; ENSG00000148498. ENST00000374776; ENSP00000363908; ENSG00000148498. ENST00000374788; ENSP00000363920; ENSG00000148498. ENST00000374789; ENSP00000363921; ENSG00000148498. ENST00000374794; ENSP00000363926; ENSG00000148498. ENST00000545260; ENSP00000440857; ENSG00000148498. ENST00000545693; ENSP00000443147; ENSG00000148498. | ||||||||||||
| GeneID | 56288. | ||||||||||||
| KEGG | hsa:56288. | ||||||||||||
| UCSC | uc001ixp.2. human. uc001ixq.2. human. uc001ixr.2. human. uc010qej.2. human. uc010qek.2. human. uc010qel.2. human. uc010qen.2. human. uc010qeo.2. human. uc010qep.2. human. uc010qeq.2. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 56288. | ||||||||||||
| GeneCards | GC10M034438. | ||||||||||||
| HGNC | HGNC:16051. PARD3. | ||||||||||||
| HPA | HPA030443. | ||||||||||||
| MIM | 606745. gene. | ||||||||||||
| neXtProt | NX_Q8TEW0. | ||||||||||||
| PharmGKB | PA32936. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG268288. | ||||||||||||
| HOVERGEN | HBG053508. | ||||||||||||
| InParanoid | Q8TEW0. | ||||||||||||
| KO | K04237. | ||||||||||||
| OMA | DEQDPHH. | ||||||||||||
| OrthoDB | EOG4C2H8V. | ||||||||||||
| PhylomeDB | Q8TEW0. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Reactome | REACT_111102. Signal Transduction. REACT_111155. Cell-Cell communication. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q8TEW0. | ||||||||||||
| Bgee | Q8TEW0. | ||||||||||||
| Genevestigator | Q8TEW0. | ||||||||||||
| GermOnline | ENSG00000148498. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR021922. DUF3534. IPR001478. PDZ. [Graphical view] | ||||||||||||
| Pfam | PF12053. DUF3534. 1 hit. PF00595. PDZ. 2 hits. [Graphical view] | ||||||||||||
| SMART | SM00228. PDZ. 3 hits. [Graphical view] | ||||||||||||
| SUPFAM | SSF50156. PDZ. 3 hits. | ||||||||||||
| PROSITE | PS50106. PDZ. 3 hits. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| ChiTaRS | PARD3. human. | ||||||||||||
| EvolutionaryTrace | Q8TEW0. | ||||||||||||
| GenomeRNAi | 56288. | ||||||||||||
| NextBio | 61959. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | PARD3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8TEW0 Secondary accession number(s): F5H5T0 Q9NYE6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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 |

Clusters with
