Q99569 (PKP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plakophilin-4

Alternative name(s):
p0071

Gene names

Name:

PKP4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1192 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
Subcellular location	Cell junction › desmosome. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle 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 process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW 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 cell cycle 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_component	desmosome Inferred from direct assay Ref.1. Source: UniProtKB internal side of plasma membrane Inferred from direct assay Ref.6. 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 spindle midzone Inferred from direct assay Ref.6. Source: UniProtKB spindle pole Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1192	1192	Plakophilin-4		PRO_0000064289
Regions
	Repeat	415 – 455	41	ARM 1
	Repeat	518 – 557	40	ARM 2
	Repeat	560 – 599	40	ARM 3
	Repeat	604 – 644	41	ARM 4
	Repeat	660 – 702	43	ARM 5
	Repeat	706 – 751	46	ARM 6
	Repeat	815 – 855	41	ARM 7
	Repeat	862 – 901	40	ARM 8
	Repeat	950 – 993	44	ARM 9
	Coiled coil	36 – 70	35	Potential
	Compositional bias	788 – 794	7	Poly-Lys
Amino acid modifications
	Modified residue	132	1	Phosphoserine By similarity
	Modified residue	221	1	Phosphoserine Ref.14
	Modified residue	231	1	Phosphoserine Ref.14
	Modified residue	233	1	Phosphoserine By similarity
	Modified residue	273	1	Phosphoserine Ref.10
	Modified residue	275	1	Phosphotyrosine By similarity
	Modified residue	281	1	Phosphoserine Ref.10
	Modified residue	290	1	Phosphoserine By similarity
	Modified residue	314	1	Phosphoserine Ref.4 Ref.5 Ref.8 Ref.9 Ref.10 Ref.12 Ref.15
	Modified residue	327	1	Phosphoserine Ref.10
	Modified residue	336	1	Phosphoserine By similarity
	Modified residue	337	1	Phosphoserine By similarity
	Modified residue	372	1	Phosphotyrosine By similarity
	Modified residue	403	1	Phosphoserine Ref.8
	Modified residue	406	1	Phosphoserine Ref.4 Ref.8
	Modified residue	415	1	Phosphotyrosine Ref.4 Ref.13
	Modified residue	422	1	Phosphoserine By similarity
	Modified residue	447	1	Phosphoserine By similarity
	Modified residue	478	1	Phosphotyrosine By similarity
	Modified residue	510	1	Phosphoserine By similarity
	Modified residue	512	1	Phosphoserine By similarity
	Modified residue	515	1	Phosphoserine By similarity
	Modified residue	776	1	Phosphoserine Ref.14
	Modified residue	1048	1	Phosphoserine By similarity
	Modified residue	1049	1	Phosphoserine By similarity
	Modified residue	1135	1	Phosphoserine By similarity
	Modified residue	1138	1	Phosphoserine By similarity
	Cross-link	611		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Natural variations
	Alternative sequence	1043 – 1085	43	Missing in isoform 2.		VSP_006737
Experimental info
	Sequence conflict	41	1	V → M in AAH50308. Ref.3
	Sequence conflict	223	1	S → Y in AAH50308. Ref.3
	Sequence conflict	235	1	G → W in AAH50308. Ref.3
	Sequence conflict	335	1	S → V in CAA57478. Ref.1
	Sequence conflict	336	1	S → V in CAA57478. Ref.1
	Sequence conflict	447	1	S → V in CAA57478. Ref.1
	Sequence conflict	448	1	V → S in CAA57478. Ref.1
	Sequence conflict	538	1	Q → E in CAA57478. Ref.1
	Sequence conflict	701	1	S → T in CAA57478. Ref.1
	Sequence conflict	766	1	N → D in AAH50308. Ref.3
	Sequence conflict	856	1	G → S in CAA57478. Ref.1
	Sequence conflict	865	1	R → G in CAA57478. Ref.1
	Sequence conflict	892	1	V → G in CAA57478. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified November 30, 2010. Version 2. Checksum: 48EA1579E323E019	FASTA	1,192	131,868
	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
	Isoform 2 (Short) [UniParc]. Checksum: 060914C3E7947CB2	FASTA	1,149	127,144
	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 QSGSSKPSPI YISSYSSPAR EQNRRLQHQQ LYYSQDDSNR 1090 1100 1110 1120 1130 1140 KNFDAYRLYL QSPHSYEDPY FDDRVHFPAS TDYSTQYGLK STTNYVDFYS TKRPSYRAEQ YPGSPDSWV

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00021076. IPI00334400.
RefSeq	NP_001005476.1. NM_001005476.1. NP_003619.2. NM_003628.3.
UniGene	Hs.407580.
3D structure databases
ProteinModelPortal	Q99569.
SMR	Q99569. Positions 525-1011.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99569. 5 interactions.
MINT	MINT-88417.
STRING	9606.ENSP00000374409.
PTM databases
PhosphoSite	Q99569.
Polymorphism databases
DMDM	20139104.
Proteomic databases
PaxDb	Q99569.
PRIDE	Q99569.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000389757; ENSP00000374407; ENSG00000144283. ENST00000389759; ENSP00000374409; ENSG00000144283.
GeneID	8502.
KEGG	hsa:8502.
UCSC	uc002tzt.1. human. uc002tzw.3. human.
Organism-specific databases
CTD	8502.
GeneCards	GC02P159313.
H-InvDB	HIX0002526.
HGNC	HGNC:9026. PKP4.
HPA	CAB037334.
MIM	604276. gene.
neXtProt	NX_Q99569.
PharmGKB	PA33359.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG276924.
HOGENOM	HOG000231863.
HOVERGEN	HBG004284.
InParanoid	Q99569.
OMA	QQLYYSQ.
Gene expression databases
ArrayExpress	Q99569.
Bgee	Q99569.
CleanEx	HS_PKP4.
Genevestigator	Q99569.
GermOnline	ENSG00000144283. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 2 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000225. Armadillo. [Graphical view]
Pfam	PF00514. Arm. 3 hits. [Graphical view]
SMART	SM00185. ARM. 6 hits. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50176. ARM_REPEAT. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PKP4. human.
GenomeRNAi	8502.
NextBio	31815.
SOURCE	Search...

Entry information

Entry name

PKP4_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete 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.