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Q99569

- PKP4_HUMAN

UniProt

Q99569 - PKP4_HUMAN

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Protein

Plakophilin-4

Gene

PKP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques.1 Publication

GO - Biological processi

  1. cell-cell junction assembly Source: UniProtKB
  2. cell-cell signaling Source: UniProtKB
  3. positive regulation of cytokinesis Source: UniProtKB
  4. positive regulation of gene expression Source: UniProtKB
  5. positive regulation of Rho GTPase activity Source: UniProtKB
  6. regulation of cell adhesion Source: UniProtKB
  7. single organismal cell-cell adhesion Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

SignaLinkiQ99569.

Names & Taxonomyi

Protein namesi
Recommended name:
Plakophilin-4
Alternative name(s):
p0071
Gene namesi
Name:PKP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9026. PKP4.

Subcellular locationi

Cell junctiondesmosome 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Midbody 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
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.

GO - Cellular componenti

  1. cell-cell junction Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic side of plasma membrane Source: UniProtKB
  4. cytoskeleton Source: UniProtKB
  5. desmosome Source: UniProtKB
  6. midbody Source: UniProtKB
  7. mitotic spindle Source: UniProtKB
  8. perinuclear region of cytoplasm Source: UniProtKB
  9. plasma membrane Source: UniProtKB
  10. spindle midzone Source: UniProtKB
  11. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33359.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11921192Plakophilin-4PRO_0000064289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei221 – 2211Phosphoserine1 Publication
Modified residuei231 – 2311Phosphoserine1 Publication
Modified residuei273 – 2731Phosphoserine1 Publication
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei314 – 3141Phosphoserine7 Publications
Modified residuei327 – 3271Phosphoserine1 Publication
Modified residuei372 – 3721PhosphotyrosineBy similarity
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei406 – 4061Phosphoserine2 Publications
Modified residuei415 – 4151Phosphotyrosine2 Publications
Modified residuei478 – 4781PhosphotyrosineBy similarity
Cross-linki611 – 611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei776 – 7761Phosphoserine1 Publication
Modified residuei1135 – 11351PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ99569.
PaxDbiQ99569.
PRIDEiQ99569.

PTM databases

PhosphoSiteiQ99569.

Expressioni

Gene expression databases

BgeeiQ99569.
CleanExiHS_PKP4.
ExpressionAtlasiQ99569. baseline and differential.
GenevestigatoriQ99569.

Organism-specific databases

HPAiCAB037334.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2IPQ96RT13EBI-726447,EBI-993903
ERBB2IPQ96RT1-23EBI-726447,EBI-8449250

Protein-protein interaction databases

BioGridi114074. 18 interactions.
IntActiQ99569. 12 interactions.
MINTiMINT-88417.
STRINGi9606.ENSP00000374409.

Structurei

3D structure databases

ProteinModelPortaliQ99569.
SMRiQ99569. Positions 525-1011.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati415 – 45541ARM 1Add
BLAST
Repeati518 – 55740ARM 2Add
BLAST
Repeati560 – 59940ARM 3Add
BLAST
Repeati604 – 64441ARM 4Add
BLAST
Repeati660 – 70243ARM 5Add
BLAST
Repeati706 – 75146ARM 6Add
BLAST
Repeati815 – 85541ARM 7Add
BLAST
Repeati862 – 90140ARM 8Add
BLAST
Repeati950 – 99344ARM 9Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili36 – 7035Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi788 – 7947Poly-Lys

Sequence similaritiesi

Belongs to the beta-catenin family.Curated
Contains 9 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG276924.
GeneTreeiENSGT00760000119167.
HOGENOMiHOG000231863.
HOVERGENiHBG004284.
InParanoidiQ99569.
OMAiGIGNLQR.
OrthoDBiEOG7X6KZB.
PhylomeDBiQ99569.
TreeFamiTF321877.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR028443. Plakophilin-4.
IPR028435. Plakophilin/d_Catenin.
[Graphical view]
PANTHERiPTHR10372. PTHR10372. 1 hit.
PTHR10372:SF8. PTHR10372:SF8. 1 hit.
PfamiPF00514. Arm. 3 hits.
[Graphical view]
SMARTiSM00185. ARM. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99569-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPAPEQASLV EEGQPQTRQE AASTGPGMEP ETTATTILAS VKEQELQFQR
60 70 80 90 100
LTRELEVERQ IVASQLERCR LGAESPSIAS TSSTEKSFPW RSTDVPNTGV
110 120 130 140 150
SKPRVSDAVQ PNNYLIRTEP EQGTLYSPEQ TSLHESEGSL GNSRSSTQMN
160 170 180 190 200
SYSDSGYQEA GSFHNSQNVS KADNRQQHSF IGSTNNHVVR NSRAEGQTLV
210 220 230 240 250
QPSVANRAMR RVSSVPSRAQ SPSYVISTGV SPSRGSLRTS LGSGFGSPSV
260 270 280 290 300
TDPRPLNPSA YSSTTLPAAR AASPYSQRPA SPTAIRRIGS VTSRQTSNPN
310 320 330 340 350
GPTPQYQTTA RVGSPLTLTD AQTRVASPSQ GQVGSSSPKR SGMTAVPQHL
360 370 380 390 400
GPSLQRTVHD MEQFGQQQYD IYERMVPPRP DSLTGLRSSY ASQHSQLGQD
410 420 430 440 450
LRSAVSPDLH ITPIYEGRTY YSPVYRSPNH GTVELQGSQT ALYRTGSVGI
460 470 480 490 500
GNLQRTSSQR STLTYQRNNY ALNTTATYAE PYRPIQYRVQ ECNYNRLQHA
510 520 530 540 550
VPADDGTTRS PSIDSIQKDP REFAWRDPEL PEVIHMLQHQ FPSVQANAAA
560 570 580 590 600
YLQHLCFGDN KVKMEVCRLG GIKHLVDLLD HRVLEVQKNA CGALRNLVFG
610 620 630 640 650
KSTDENKIAM KNVGGIPALL RLLRKSIDAE VRELVTGVLW NLSSCDAVKM
660 670 680 690 700
TIIRDALSTL TNTVIVPHSG WNNSSFDDDH KIKFQTSLVL RNTTGCLRNL
710 720 730 740 750
SSAGEEARKQ MRSCEGLVDS LLYVIHTCVN TSDYDSKTVE NCVCTLRNLS
760 770 780 790 800
YRLELEVPQA RLLGLNELDD LLGKESPSKD SEPSCWGKKK KKKKRTPQED
810 820 830 840 850
QWDGVGPIPG LSKSPKGVEM LWHPSVVKPY LTLLAESSNP ATLEGSAGSL
860 870 880 890 900
QNLSAGNWKF AAYIRAAVRK EKGLPILVEL LRMDNDRVVS SVATALRNMA
910 920 930 940 950
LDVRNKELIG KYAMRDLVNR LPGGNGPSVL SDETMAAICC ALHEVTSKNM
960 970 980 990 1000
ENAKALADSG GIEKLVNITK GRGDRSSLKV VKAAAQVLNT LWQYRDLRSI
1010 1020 1030 1040 1050
YKKDGWNQNH FITPVSTLER DRFKSHPSLS TTNQQMSPII QSVGSTSSSP
1060 1070 1080 1090 1100
ALLGIRDPRS EYDRTQPPMQ YYNSQGDATH KGLYPGSSKP SPIYISSYSS
1110 1120 1130 1140 1150
PAREQNRRLQ HQQLYYSQDD SNRKNFDAYR LYLQSPHSYE DPYFDDRVHF
1160 1170 1180 1190
PASTDYSTQY GLKSTTNYVD FYSTKRPSYR AEQYPGSPDS WV
Length:1,192
Mass (Da):131,868
Last modified:November 30, 2010 - v2
Checksum:i48EA1579E323E019
GO
Isoform 2 (identifier: Q99569-2) [UniParc]FASTAAdd to Basket

Also known as: Short

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

Show »
Length:1,149
Mass (Da):127,144
Checksum:i060914C3E7947CB2
GO

Sequence cautioni

The sequence CAA57478.1 differs from that shown. Reason: Frameshift at positions 334, 337, 864 and 874.
The sequence CAA57478.1 differs from that shown. Reason: Erroneous termination at position 1193. Translated as stop.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411V → M in AAH50308. (PubMed:15489334)Curated
Sequence conflicti223 – 2231S → Y in AAH50308. (PubMed:15489334)Curated
Sequence conflicti235 – 2351G → W in AAH50308. (PubMed:15489334)Curated
Sequence conflicti335 – 3351S → V in CAA57478. (PubMed:8937994)Curated
Sequence conflicti336 – 3361S → V in CAA57478. (PubMed:8937994)Curated
Sequence conflicti447 – 4471S → V in CAA57478. (PubMed:8937994)Curated
Sequence conflicti448 – 4481V → S in CAA57478. (PubMed:8937994)Curated
Sequence conflicti538 – 5381Q → E in CAA57478. (PubMed:8937994)Curated
Sequence conflicti701 – 7011S → T in CAA57478. (PubMed:8937994)Curated
Sequence conflicti766 – 7661N → D in AAH50308. (PubMed:15489334)Curated
Sequence conflicti856 – 8561G → S in CAA57478. (PubMed:8937994)Curated
Sequence conflicti865 – 8651R → G in CAA57478. (PubMed:8937994)Curated
Sequence conflicti892 – 8921V → G in CAA57478. (PubMed:8937994)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1043 – 108543Missing in isoform 2. 2 PublicationsVSP_006737Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81889 mRNA. Translation: CAA57478.1. Sequence problems.
AC005042 Genomic DNA. No translation available.
AC008070 Genomic DNA. No translation available.
BC050308 mRNA. Translation: AAH50308.1.
CCDSiCCDS33305.1. [Q99569-1]
CCDS33306.1. [Q99569-2]
RefSeqiNP_001005476.1. NM_001005476.1. [Q99569-2]
NP_003619.2. NM_003628.3. [Q99569-1]
UniGeneiHs.407580.

Genome annotation databases

EnsembliENST00000389757; ENSP00000374407; ENSG00000144283. [Q99569-2]
ENST00000389759; ENSP00000374409; ENSG00000144283. [Q99569-1]
GeneIDi8502.
KEGGihsa:8502.
UCSCiuc002tzt.1. human. [Q99569-1]
uc002tzw.3. human. [Q99569-2]

Polymorphism databases

DMDMi313104155.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81889 mRNA. Translation: CAA57478.1 . Sequence problems.
AC005042 Genomic DNA. No translation available.
AC008070 Genomic DNA. No translation available.
BC050308 mRNA. Translation: AAH50308.1 .
CCDSi CCDS33305.1. [Q99569-1 ]
CCDS33306.1. [Q99569-2 ]
RefSeqi NP_001005476.1. NM_001005476.1. [Q99569-2 ]
NP_003619.2. NM_003628.3. [Q99569-1 ]
UniGenei Hs.407580.

3D structure databases

ProteinModelPortali Q99569.
SMRi Q99569. Positions 525-1011.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114074. 18 interactions.
IntActi Q99569. 12 interactions.
MINTi MINT-88417.
STRINGi 9606.ENSP00000374409.

PTM databases

PhosphoSitei Q99569.

Polymorphism databases

DMDMi 313104155.

Proteomic databases

MaxQBi Q99569.
PaxDbi Q99569.
PRIDEi Q99569.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389757 ; ENSP00000374407 ; ENSG00000144283 . [Q99569-2 ]
ENST00000389759 ; ENSP00000374409 ; ENSG00000144283 . [Q99569-1 ]
GeneIDi 8502.
KEGGi hsa:8502.
UCSCi uc002tzt.1. human. [Q99569-1 ]
uc002tzw.3. human. [Q99569-2 ]

Organism-specific databases

CTDi 8502.
GeneCardsi GC02P159313.
H-InvDB HIX0002526.
HGNCi HGNC:9026. PKP4.
HPAi CAB037334.
MIMi 604276. gene.
neXtProti NX_Q99569.
PharmGKBi PA33359.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG276924.
GeneTreei ENSGT00760000119167.
HOGENOMi HOG000231863.
HOVERGENi HBG004284.
InParanoidi Q99569.
OMAi GIGNLQR.
OrthoDBi EOG7X6KZB.
PhylomeDBi Q99569.
TreeFami TF321877.

Enzyme and pathway databases

SignaLinki Q99569.

Miscellaneous databases

ChiTaRSi PKP4. human.
GeneWikii PKP4.
GenomeRNAii 8502.
NextBioi 31815.
PROi Q99569.
SOURCEi Search...

Gene expression databases

Bgeei Q99569.
CleanExi HS_PKP4.
ExpressionAtlasi Q99569. baseline and differential.
Genevestigatori Q99569.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR028443. Plakophilin-4.
IPR028435. Plakophilin/d_Catenin.
[Graphical view ]
PANTHERi PTHR10372. PTHR10372. 1 hit.
PTHR10372:SF8. PTHR10372:SF8. 1 hit.
Pfami PF00514. Arm. 3 hits.
[Graphical view ]
SMARTi SM00185. ARM. 6 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50176. ARM_REPEAT. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPKP4_HUMAN
AccessioniPrimary (citable) accession number: Q99569
Secondary accession number(s): Q86W91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3