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Q8TEW0 (PARD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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:
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
Name:PARD3
Synonyms:PAR3, PAR3A
OrganismHomo sapiens (Human) [Reference 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. 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. Directly interacts with TIAM1 and TIAM2. Interacts with ECT2 and FBF1. Ref.1 Ref.4 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.20 Ref.24

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. 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

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Tight junction
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapical constriction

Inferred from electronic annotation. Source: Ensembl

asymmetric cell division

Traceable author statement Ref.1. Source: ProtInc

axonogenesis

Traceable author statement PubMed 14676191. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

centrosome localization

Inferred from electronic annotation. Source: Ensembl

establishment of epithelial cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

establishment or maintenance of cell polarity

Traceable author statement PubMed 14676191. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

myelination in peripheral nervous system

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myelination

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex assembly

Traceable author statement Ref.1. Source: ProtInc

protein kinase C-activating G-protein coupled receptor signaling pathway

Traceable author statement PubMed 11260256. Source: UniProtKB

protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of actin filament-based process

Inferred from electronic annotation. Source: Ensembl

regulation of cellular localization

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

wound healing, spreading of cells

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

axonal growth cone

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from direct assay. Source: HPA

cell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay Ref.20. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

internode region of axon

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

protein complex

Inferred from electronic annotation. Source: Ensembl

spindle

Inferred from electronic annotation. Source: Ensembl

tight junction

Inferred from direct assay PubMed 14676191. Source: UniProtKB

   Molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3-phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 19893486. Source: IntAct

Complete GO annotation...

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 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 PRKCI and 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 residue3831Phosphoserine Ref.16 Ref.17 Ref.19 Ref.21 Ref.23
Modified residue6921Phosphoserine Ref.17
Modified residue6951Phosphoserine Ref.16 Ref.17
Modified residue7281Phosphoserine Ref.17 Ref.19 Ref.21
Modified residue8091Phosphoserine Ref.17
Modified residue8271Phosphoserine By similarity
Modified residue8521Phosphoserine Ref.17 Ref.19 Ref.21 Ref.23
Modified residue8731Phosphoserine Ref.17 Ref.21 Ref.23
Modified residue9621Phosphoserine; by AURKA Ref.18

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, isoform 9 and isoform 11.
VSP_007463
Alternative sequence740 – 7423Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.
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.
Corresponds to variant rs1436731 [ dbSNP | Ensembl ].
VAR_015663
Natural variant5751D → N.
Corresponds to variant rs3758459 [ dbSNP | Ensembl ].
VAR_050453

Experimental info

Mutagenesis9621S → A: Abolishes phosphorylation by AURKA. Ref.18
Mutagenesis11271Y → F: Delayed epithelial tight junction assembly.
Sequence conflict1901T → A in BAB55330. Ref.8
Sequence conflict2331L → Q in BAB55330. Ref.8
Sequence conflict5941N → S in BAB55330. Ref.8
Sequence conflict7641D → N in AAH71566. Ref.7
Sequence conflict996 – 10005GKEKK → VELHE in BAA91366. Ref.8

Secondary structure

................. 1356
Helix Strand Turn

Details...

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) [UniParc].

Checksum: BC531577B9C31AE3
Show »

FASTA1,353151,150
Isoform 3 (C) [UniParc].

Checksum: 92DF51B68081A4A2
Show »

FASTA1,266141,072
Isoform 4 (D) [UniParc].

Checksum: F5FBF3CE4E67163B
Show »

FASTA1,319146,877
Isoform 5 (E) [UniParc].

Checksum: C3C156C8811D49C2
Show »

FASTA1,244138,332
Isoform 6 (F) [UniParc].

Checksum: 57361092A273AC60
Show »

FASTA1,310146,276
Isoform 7 (Lb) [UniParc].

Checksum: 53C1A94D8CB7341E
Show »

FASTA1,273141,730
Isoform 8 (Sa) [UniParc].

Checksum: 40DD593636EAE999
Show »

FASTA1,031113,419
Isoform 9 (Sb) [UniParc].

Checksum: 89F2139B096F7F7F
Show »

FASTA988108,545
Isoform 10 [UniParc].

Checksum: 135A54F80C144606
Show »

FASTA1,000109,917
Isoform 11 [UniParc].

Checksum: 3DAB16557C6BBA86
Show »

FASTA1,340149,695

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. 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] [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. 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]"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. 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] 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"High-resolution structure of the Tiam1 PHn-CC-Ex domain."
Joshi M., Gakhar L., Fuentes E.J.
Acta Crystallogr. F 69:744-752(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIAM1.
[25]"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 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: CAH71165.1.
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: CAH73528.1.
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: CAI15039.1.
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: CAI16988.1.
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: CAI17308.1.
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: CAI17331.1.
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.
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.
CCDSCCDS53509.1. [Q8TEW0-5]
CCDS53510.1. [Q8TEW0-3]
CCDS53511.1. [Q8TEW0-11]
CCDS53512.1. [Q8TEW0-6]
CCDS53513.1. [Q8TEW0-9]
CCDS53514.1. [Q8TEW0-4]
CCDS53515.1. [Q8TEW0-2]
CCDS53516.1. [Q8TEW0-8]
CCDS7178.1. [Q8TEW0-1]
RefSeqNP_001171714.1. NM_001184785.1. [Q8TEW0-2]
NP_001171715.1. NM_001184786.1. [Q8TEW0-11]
NP_001171716.1. NM_001184787.1. [Q8TEW0-4]
NP_001171717.1. NM_001184788.1. [Q8TEW0-6]
NP_001171718.1. NM_001184789.1. [Q8TEW0-7]
NP_001171719.1. NM_001184790.1. [Q8TEW0-3]
NP_001171720.1. NM_001184791.1. [Q8TEW0-5]
NP_001171721.1. NM_001184792.1. [Q8TEW0-8]
NP_001171722.1. NM_001184793.1. [Q8TEW0-10]
NP_001171723.1. NM_001184794.1. [Q8TEW0-9]
NP_062565.2. NM_019619.3. [Q8TEW0-1]
UniGeneHs.131489.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KOMNMR-A451-549[»]
ProteinModelPortalQ8TEW0.
SMRQ8TEW0. Positions 2-82, 272-358, 451-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121134. 47 interactions.
DIPDIP-31315N.
IntActQ8TEW0. 38 interactions.
MINTMINT-7711810.

PTM databases

PhosphoSiteQ8TEW0.

Polymorphism databases

DMDM30913162.

Proteomic databases

MaxQBQ8TEW0.
PaxDbQ8TEW0.
PRIDEQ8TEW0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340077; ENSP00000341844; ENSG00000148498. [Q8TEW0-8]
ENST00000346874; ENSP00000340591; ENSG00000148498. [Q8TEW0-4]
ENST00000350537; ENSP00000311986; ENSG00000148498. [Q8TEW0-6]
ENST00000374776; ENSP00000363908; ENSG00000148498. [Q8TEW0-9]
ENST00000374788; ENSP00000363920; ENSG00000148498. [Q8TEW0-2]
ENST00000374789; ENSP00000363921; ENSG00000148498. [Q8TEW0-1]
ENST00000374794; ENSP00000363926; ENSG00000148498. [Q8TEW0-5]
ENST00000545260; ENSP00000440857; ENSG00000148498. [Q8TEW0-3]
ENST00000545693; ENSP00000443147; ENSG00000148498. [Q8TEW0-11]
GeneID56288.
KEGGhsa:56288.
UCSCuc001ixp.2. human. [Q8TEW0-10]
uc001ixq.2. human. [Q8TEW0-9]
uc001ixr.2. human. [Q8TEW0-8]
uc010qej.2. human. [Q8TEW0-1]
uc010qek.2. human. [Q8TEW0-2]
uc010qel.2. human. [Q8TEW0-4]
uc010qen.2. human. [Q8TEW0-6]
uc010qeo.2. human. [Q8TEW0-7]
uc010qep.2. human. [Q8TEW0-3]
uc010qeq.2. human. [Q8TEW0-5]

Organism-specific databases

CTD56288.
GeneCardsGC10M034438.
HGNCHGNC:16051. PARD3.
HPAHPA030443.
MIM606745. gene.
neXtProtNX_Q8TEW0.
PharmGKBPA32936.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268288.
HOVERGENHBG053508.
InParanoidQ8TEW0.
KOK04237.
OMADEQDPHH.
OrthoDBEOG7WHH92.
PhylomeDBQ8TEW0.
TreeFamTF323729.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
SignaLinkQ8TEW0.

Gene expression databases

ArrayExpressQ8TEW0.
BgeeQ8TEW0.
GenevestigatorQ8TEW0.

Family and domain databases

Gene3D2.30.42.10. 3 hits.
InterProIPR021922. DUF3534.
IPR001478. PDZ.
[Graphical view]
PfamPF12053. DUF3534. 1 hit.
PF00595. PDZ. 3 hits.
[Graphical view]
SMARTSM00228. PDZ. 3 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 3 hits.
PROSITEPS50106. PDZ. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPARD3. human.
EvolutionaryTraceQ8TEW0.
GeneWikiPARD3.
GenomeRNAi56288.
NextBio61959.
PROQ8TEW0.
SOURCESearch...

Entry information

Entry namePARD3_HUMAN
AccessionPrimary (citable) accession number: Q8TEW0
Secondary accession number(s): F5H5T0 expand/collapse secondary AC list , Q5T2U1, Q5VUA2, Q5VUA3, Q5VWV0, Q5VWV1, Q5VWV3, Q5VWV4, Q5VWV5, Q6IQ47, Q8TCZ9, 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: July 9, 2014
This is version 134 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 10

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