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Q99569 (PKP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Plakophilin-4
Alternative name(s):
p0071
Gene names
Name:PKP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques. Ref.6

Subunit structure

Interacts with PDZD2 By similarity. Interacts (via the C-terminus) with FRMPD2 (via the PDZ 2 domain). Interacts with RHOA; the interaction is detected at the midbody. Interacts with ECT2; the interaction is detected at the midbody. Ref.6 Ref.12

Subcellular location

Cell junctiondesmosome. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Midbody. Cell membrane; Peripheral membrane protein. Note: Associated with the pericentrosomal region in interphase and with spindle poles during mitosis. In anaphase, during chromosome segregation, is recruited to the central microtubule bundle, focussed at the spindle midzone and ultimately localizes to the midbody at cytokinesis. Constituent of the midbody cytoskeletal matrix. Colocalized with desmoplakin at desmosomal junctional plaques in cultured epithelial cells. Ref.6

Sequence similarities

Belongs to the beta-catenin family.

Contains 9 ARM repeats.

Sequence caution

The sequence CAA57478.1 differs from that shown. Reason: Erroneous termination at position 1193. Translated as stop.

The sequence CAA57478.1 differs from that shown. Reason: Frameshift at positions 334, 337, 864 and 874.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell adhesion

Inferred from electronic annotation. Source: InterPro

cell-cell junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell signaling

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of Rho GTPase activity

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of cytokinesis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentcell-cell junction

Inferred from direct assay Ref.1. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 22965878. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from direct assay Ref.6. Source: UniProtKB

cytoskeleton

Inferred from direct assay Ref.1. Source: UniProtKB

desmosome

Inferred from direct assay Ref.1. Source: UniProtKB

midbody

Inferred from direct assay Ref.6. Source: UniProtKB

mitotic spindle

Inferred from direct assay Ref.6. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

spindle midzone

Inferred from direct assay Ref.6. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERBB2IPQ96RT13EBI-726447,EBI-993903
ERBB2IPQ96RT1-23EBI-726447,EBI-8449250

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99569-1)

Also known as: Long;

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: Q99569-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1043-1085: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11921192Plakophilin-4
PRO_0000064289

Regions

Repeat415 – 45541ARM 1
Repeat518 – 55740ARM 2
Repeat560 – 59940ARM 3
Repeat604 – 64441ARM 4
Repeat660 – 70243ARM 5
Repeat706 – 75146ARM 6
Repeat815 – 85541ARM 7
Repeat862 – 90140ARM 8
Repeat950 – 99344ARM 9
Coiled coil36 – 7035 Potential
Compositional bias788 – 7947Poly-Lys

Amino acid modifications

Modified residue2211Phosphoserine Ref.15
Modified residue2311Phosphoserine Ref.15
Modified residue2731Phosphoserine Ref.10
Modified residue2811Phosphoserine Ref.10
Modified residue3141Phosphoserine Ref.4 Ref.5 Ref.8 Ref.9 Ref.10 Ref.13 Ref.16
Modified residue3271Phosphoserine Ref.10
Modified residue3721Phosphotyrosine By similarity
Modified residue4031Phosphoserine Ref.8
Modified residue4061Phosphoserine Ref.4 Ref.8
Modified residue4151Phosphotyrosine Ref.4 Ref.14
Modified residue4781Phosphotyrosine By similarity
Modified residue7761Phosphoserine Ref.15
Modified residue11351Phosphoserine By similarity
Cross-link611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Natural variations

Alternative sequence1043 – 108543Missing in isoform 2.
VSP_006737

Experimental info

Sequence conflict411V → M in AAH50308. Ref.3
Sequence conflict2231S → Y in AAH50308. Ref.3
Sequence conflict2351G → W in AAH50308. Ref.3
Sequence conflict3351S → V in CAA57478. Ref.1
Sequence conflict3361S → V in CAA57478. Ref.1
Sequence conflict4471S → V in CAA57478. Ref.1
Sequence conflict4481V → S in CAA57478. Ref.1
Sequence conflict5381Q → E in CAA57478. Ref.1
Sequence conflict7011S → T in CAA57478. Ref.1
Sequence conflict7661N → D in AAH50308. Ref.3
Sequence conflict8561G → S in CAA57478. Ref.1
Sequence conflict8651R → G in CAA57478. Ref.1
Sequence conflict8921V → G in CAA57478. Ref.1

Sequences

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

Last modified November 30, 2010. Version 2.
Checksum: 48EA1579E323E019

FASTA1,192131,868
        10         20         30         40         50         60 
MPAPEQASLV EEGQPQTRQE AASTGPGMEP ETTATTILAS VKEQELQFQR LTRELEVERQ 

        70         80         90        100        110        120 
IVASQLERCR LGAESPSIAS TSSTEKSFPW RSTDVPNTGV SKPRVSDAVQ PNNYLIRTEP 

       130        140        150        160        170        180 
EQGTLYSPEQ TSLHESEGSL GNSRSSTQMN SYSDSGYQEA GSFHNSQNVS KADNRQQHSF 

       190        200        210        220        230        240 
IGSTNNHVVR NSRAEGQTLV QPSVANRAMR RVSSVPSRAQ SPSYVISTGV SPSRGSLRTS 

       250        260        270        280        290        300 
LGSGFGSPSV TDPRPLNPSA YSSTTLPAAR AASPYSQRPA SPTAIRRIGS VTSRQTSNPN 

       310        320        330        340        350        360 
GPTPQYQTTA RVGSPLTLTD AQTRVASPSQ GQVGSSSPKR SGMTAVPQHL GPSLQRTVHD 

       370        380        390        400        410        420 
MEQFGQQQYD IYERMVPPRP DSLTGLRSSY ASQHSQLGQD LRSAVSPDLH ITPIYEGRTY 

       430        440        450        460        470        480 
YSPVYRSPNH GTVELQGSQT ALYRTGSVGI GNLQRTSSQR STLTYQRNNY ALNTTATYAE 

       490        500        510        520        530        540 
PYRPIQYRVQ ECNYNRLQHA VPADDGTTRS PSIDSIQKDP REFAWRDPEL PEVIHMLQHQ 

       550        560        570        580        590        600 
FPSVQANAAA YLQHLCFGDN KVKMEVCRLG GIKHLVDLLD HRVLEVQKNA CGALRNLVFG 

       610        620        630        640        650        660 
KSTDENKIAM KNVGGIPALL RLLRKSIDAE VRELVTGVLW NLSSCDAVKM TIIRDALSTL 

       670        680        690        700        710        720 
TNTVIVPHSG WNNSSFDDDH KIKFQTSLVL RNTTGCLRNL SSAGEEARKQ MRSCEGLVDS 

       730        740        750        760        770        780 
LLYVIHTCVN TSDYDSKTVE NCVCTLRNLS YRLELEVPQA RLLGLNELDD LLGKESPSKD 

       790        800        810        820        830        840 
SEPSCWGKKK KKKKRTPQED QWDGVGPIPG LSKSPKGVEM LWHPSVVKPY LTLLAESSNP 

       850        860        870        880        890        900 
ATLEGSAGSL QNLSAGNWKF AAYIRAAVRK EKGLPILVEL LRMDNDRVVS SVATALRNMA 

       910        920        930        940        950        960 
LDVRNKELIG KYAMRDLVNR LPGGNGPSVL SDETMAAICC ALHEVTSKNM ENAKALADSG 

       970        980        990       1000       1010       1020 
GIEKLVNITK GRGDRSSLKV VKAAAQVLNT LWQYRDLRSI YKKDGWNQNH FITPVSTLER 

      1030       1040       1050       1060       1070       1080 
DRFKSHPSLS TTNQQMSPII QSVGSTSSSP ALLGIRDPRS EYDRTQPPMQ YYNSQGDATH 

      1090       1100       1110       1120       1130       1140 
KGLYPGSSKP SPIYISSYSS PAREQNRRLQ HQQLYYSQDD SNRKNFDAYR LYLQSPHSYE 

      1150       1160       1170       1180       1190 
DPYFDDRVHF PASTDYSTQY GLKSTTNYVD FYSTKRPSYR AEQYPGSPDS WV 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 060914C3E7947CB2
Show »

FASTA1,149127,144

References

« Hide 'large scale' references
[1]"Cloning and characterization of a new armadillo family member, p0071, associated with the junctional plaque: evidence for a subfamily of closely related proteins."
Hatzfeld M., Nachtsheim C.
J. Cell Sci. 109:2767-2778(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Frontal cortex.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2).
Tissue: Brain.
[4]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-406 AND TYR-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"The armadillo protein p0071 regulates Rho signalling during cytokinesis."
Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M.
Nat. Cell Biol. 8:1432-1440(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ECT2 AND RHOA, SUBCELLULAR LOCATION.
[7]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-611.
Tissue: Mammary cancer.
[8]"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-314; SER-403 AND SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-273; SER-281; SER-314 AND SER-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"PDZ-domain-directed basolateral targeting of the peripheral membrane protein FRMPD2 in epithelial cells."
Stenzel N., Fetzer C.P., Heumann R., Erdmann K.S.
J. Cell Sci. 122:3374-3384(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FRMPD2.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; SER-231 AND SER-776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81889 mRNA. Translation: CAA57478.1. Sequence problems.
AC005042 Genomic DNA. No translation available.
AC008070 Genomic DNA. No translation available.
BC050308 mRNA. Translation: AAH50308.1.
RefSeqNP_001005476.1. NM_001005476.1.
NP_003619.2. NM_003628.3.
UniGeneHs.407580.

3D structure databases

ProteinModelPortalQ99569.
SMRQ99569. Positions 525-1011.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114074. 16 interactions.
IntActQ99569. 12 interactions.
MINTMINT-88417.
STRING9606.ENSP00000374409.

PTM databases

PhosphoSiteQ99569.

Polymorphism databases

DMDM313104155.

Proteomic databases

PaxDbQ99569.
PRIDEQ99569.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389757; ENSP00000374407; ENSG00000144283. [Q99569-2]
ENST00000389759; ENSP00000374409; ENSG00000144283. [Q99569-1]
GeneID8502.
KEGGhsa:8502.
UCSCuc002tzt.1. human. [Q99569-1]
uc002tzw.3. human. [Q99569-2]

Organism-specific databases

CTD8502.
GeneCardsGC02P159313.
H-InvDBHIX0002526.
HGNCHGNC:9026. PKP4.
HPACAB037334.
MIM604276. gene.
neXtProtNX_Q99569.
PharmGKBPA33359.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276924.
HOGENOMHOG000231863.
HOVERGENHBG004284.
InParanoidQ99569.
OMAGIGNLQR.
OrthoDBEOG7X6KZB.
PhylomeDBQ99569.
TreeFamTF321877.

Enzyme and pathway databases

SignaLinkQ99569.

Gene expression databases

ArrayExpressQ99569.
BgeeQ99569.
CleanExHS_PKP4.
GenevestigatorQ99569.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR028443. Plakophilin-4.
IPR028435. Plakophilin/d_Catenin.
[Graphical view]
PANTHERPTHR10372. PTHR10372. 1 hit.
PTHR10372:SF8. PTHR10372:SF8. 1 hit.
PfamPF00514. Arm. 3 hits.
[Graphical view]
SMARTSM00185. ARM. 6 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPKP4. human.
GeneWikiPKP4.
GenomeRNAi8502.
NextBio31815.
PROQ99569.
SOURCESearch...

Entry information

Entry namePKP4_HUMAN
AccessionPrimary (citable) accession number: Q99569
Secondary accession number(s): Q86W91
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 127 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

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM