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Protein

Periphilin-1

Gene

PPHLN1

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

Functioni

Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (Probable).1 Publication3 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Keratinization, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Periphilin-11 Publication
Alternative name(s):
CDC7 expression repressor1 Publication
Short name:
CR1 Publication
Gastric cancer antigen Ga501 Publication
Gene namesi
Name:PPHLN1Imported
ORF Names:HSPC206, HSPC232
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:19369. PPHLN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134881011.

Polymorphism and mutation databases

BioMutaiPPHLN1.
DMDMi46396942.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Periphilin-1PRO_0000058537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineCombined sources
Modified residuei161 – 1611PhosphoserineCombined sources
Modified residuei167 – 1671PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineCombined sources
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei235 – 2351N6-acetyllysineCombined sources
Modified residuei240 – 2401N6-acetyllysine; alternateCombined sources
Cross-linki240 – 240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei325 – 3251PhosphoserineCombined sources
Cross-linki453 – 453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Substrate of transglutaminase (in vitro).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8NEY8.
MaxQBiQ8NEY8.
PaxDbiQ8NEY8.
PeptideAtlasiQ8NEY8.
PRIDEiQ8NEY8.

PTM databases

iPTMnetiQ8NEY8.
PhosphoSiteiQ8NEY8.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8NEY8.
CleanExiHS_PPHLN1.
ExpressionAtlasiQ8NEY8. baseline and differential.
GenevisibleiQ8NEY8. HS.

Organism-specific databases

HPAiHPA038902.
HPA038903.

Interactioni

Subunit structurei

Homodimer (PubMed:12853457). Component of the HUSH complex; at least composed of FAM208A/TASOR, PPHLN1 and MPHOSPH8 (PubMed:26022416). Interacts with SIN3A and HDAC1 (PubMed:17963697). Interacts with PPL (PubMed:12853457).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC57Q2TAC23EBI-474076,EBI-2808286
MTUS2Q5JR593EBI-474076,EBI-742948
TSGA10Q9BZW73EBI-474076,EBI-744794

Protein-protein interaction databases

BioGridi119596. 59 interactions.
DIPiDIP-49051N.
IntActiQ8NEY8. 35 interactions.
MINTiMINT-1431126.
STRINGi9606.ENSP00000378935.

Structurei

3D structure databases

ProteinModelPortaliQ8NEY8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi103 – 1097Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi140 – 21576Ser-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IFSB. Eukaryota.
ENOG4111JYA. LUCA.
GeneTreeiENSGT00390000016228.
HOVERGENiHBG053653.
InParanoidiQ8NEY8.
PhylomeDBiQ8NEY8.
TreeFamiTF335813.

Family and domain databases

InterProiIPR028851. Pphln1.
[Graphical view]
PANTHERiPTHR15836:SF2. PTHR15836:SF2. 1 hit.

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NEY8-1) [UniParc]FASTAAdd to basket

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
MWSEGRYEYE RIPRERAPPR SHPSDGYNRL VNIVPKKPPL LDRPGEGSYN
60 70 80 90 100
RYYSHVDYRD YDEGRSFSHD RRSGPPHRGD ESGYRWTRDD HSASRQPEYR
110 120 130 140 150
DMRDGFRRKS FYSSHYARER SPYKRDNTFF RESPVGRKDS PHSRSGSSVS
160 170 180 190 200
SRSYSPERSK SYSFHQSQHR KSVRPGASYK RQNEGNPERD KERPVQSLKT
210 220 230 240 250
SRDTSPSSGS AVSSSKVLDK PSRLTEKELA EAASKWAAEK LEKSDESNLP
260 270 280 290 300
EISEYEAGST APLFTDQPEE PESNTTHGIE LFEDSQLTTR SKAIASKTKE
310 320 330 340 350
IEQVYRQDCE TFGMVVKMLI EKDPSLEKSI QFALRQNLHE IESAGQTWQQ
360 370 380 390 400
VPPVRNTEMD HDGTPENEGE ETAQSAPQPP QAPQPLQPRK KRVRRTTQLR
410 420 430 440 450
RTTGAPDITW GMLKKTTQEA ERILLRTQTP FTPENLFLAM LSVVHCNSRK

DVKPENKQ
Length:458
Mass (Da):52,737
Last modified:April 13, 2004 - v2
Checksum:iFE5AAC9A6875A455
GO
Isoform 2 (identifier: Q8NEY8-2) [UniParc]FASTAAdd to basket

Also known as: CR1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAYRRDEM
     342-367: ESAGQTWQQVPPVRNTEMDHDGTPEN → GERCVEELKHFIAEYDTSTQDFGEPF
     368-458: Missing.

Show »
Length:374
Mass (Da):43,397
Checksum:iE21175738E0BBB10
GO
Isoform 3 (identifier: Q8NEY8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     25-79: Missing.
     376-376: A → ALFGFQHDASNHTIVGLGPNQVPEMKETTLQA

Note: No experimental confirmation available.Curated
Show »
Length:434
Mass (Da):49,655
Checksum:i125A3F59421D07F5
GO
Isoform 5 (identifier: Q8NEY8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAYRRDEM
     25-79: Missing.
     305-306: YR → RV
     307-458: Missing.

Note: No experimental confirmation available. May be due to intron retention.
Show »
Length:258
Mass (Da):29,784
Checksum:i40A8EA59BEE07615
GO
Isoform 6 (identifier: Q8NEY8-6) [UniParc]FASTAAdd to basket

Also known as: CR-S1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAYRRDEM
     25-79: Missing.
     342-367: ESAGQTWQQVPPVRNTEMDHDGTPEN → GERCVEELKHFIAEYDTSTQDFGEPF
     368-458: Missing.

Show »
Length:319
Mass (Da):36,952
Checksum:i2A6B2C5E297CD8D9
GO
Isoform 7 (identifier: Q8NEY8-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.
     185-189: GNPER → MFSYI
     305-306: YR → RV
     307-458: Missing.

Note: No experimental confirmation available. May be due to intron retention.
Show »
Length:122
Mass (Da):13,452
Checksum:iBABAE17D379F93C2
GO
Isoform 8 (identifier: Q8NEY8-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     342-367: ESAGQTWQQVPPVRNTEMDHDGTPEN → GERCVEELKHFIAEYDTSTQDFGEPF
     368-458: Missing.

Note: No experimental confirmation available.
Show »
Length:367
Mass (Da):42,475
Checksum:iD6CA75F0569FBCE7
GO
Isoform 9 (identifier: Q8NEY8-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-190: RKSVRPGASYKRQNEGNPERD → RN
     342-367: ESAGQTWQQVPPVRNTEMDHDGTPEN → GERCVEELKHFIAEYDTSTQDFGEPF
     368-458: Missing.

Note: No experimental confirmation available.
Show »
Length:348
Mass (Da):40,319
Checksum:i1730F2459FE4A5BE
GO

Sequence cautioni

Isoform 6 : The sequence AAF36126.1 differs from that shown. Reason: Frameshift at positions 171, 193, 216, 243 and 257. Curated
Isoform 6 : The sequence AAF36152.1 differs from that shown. Reason: Frameshift at positions 191, 199 and 451. Curated
The sequence AAH25306.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971P → L in AAF36126 (PubMed:11042152).Curated
Sequence conflicti178 – 1781S → F in AAO16497 (PubMed:12853457).Curated
Sequence conflicti253 – 2531S → P in AAF36126 (PubMed:11042152).Curated
Sequence conflicti283 – 2831E → K in AAF36126 (PubMed:11042152).Curated
Isoform 3 (identifier: Q8NEY8-3)
Sequence conflicti341 – 3411Q → P in AAH25306 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731V → M in a breast cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs140585847 [ dbSNP | Ensembl ].
VAR_036233

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 184184Missing in isoform 7. 1 PublicationVSP_009898Add
BLAST
Alternative sequencei1 – 11M → MAYRRDEM in isoform 2, isoform 5 and isoform 6. 3 PublicationsVSP_009899
Alternative sequencei25 – 7955Missing in isoform 3, isoform 5 and isoform 6. 2 PublicationsVSP_009900Add
BLAST
Alternative sequencei170 – 19021RKSVR…NPERD → RN in isoform 9. 1 PublicationVSP_054078Add
BLAST
Alternative sequencei185 – 1895GNPER → MFSYI in isoform 7. 1 PublicationVSP_009902
Alternative sequencei305 – 3062YR → RV in isoform 5 and isoform 7. 2 PublicationsVSP_009903
Alternative sequencei307 – 458152Missing in isoform 5 and isoform 7. 2 PublicationsVSP_009904Add
BLAST
Alternative sequencei342 – 36726ESAGQ…GTPEN → GERCVEELKHFIAEYDTSTQ DFGEPF in isoform 2, isoform 6, isoform 8 and isoform 9. 4 PublicationsVSP_009905Add
BLAST
Alternative sequencei368 – 45891Missing in isoform 2, isoform 6, isoform 8 and isoform 9. 4 PublicationsVSP_009906Add
BLAST
Alternative sequencei376 – 3761A → ALFGFQHDASNHTIVGLGPN QVPEMKETTLQA in isoform 3. 1 PublicationVSP_009907

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY039238 mRNA. Translation: AAK68657.1.
AY157850 mRNA. Translation: AAO16497.1.
AF151040 mRNA. Translation: AAF36126.1. Frameshift.
AF151066 mRNA. Translation: AAF36152.1. Frameshift.
AK055690 mRNA. Translation: BAB70985.1.
AK000186 mRNA. Translation: BAA90996.1.
CR621833 mRNA. No translation available.
AC020629 Genomic DNA. No translation available.
AC079601 Genomic DNA. No translation available.
AC079684 Genomic DNA. No translation available.
BC025306 mRNA. Translation: AAH25306.1. Different initiation.
BC039832 mRNA. Translation: AAH39832.1.
CCDSiCCDS31777.1. [Q8NEY8-1]
CCDS41773.1. [Q8NEY8-2]
CCDS44860.1. [Q8NEY8-3]
CCDS44861.1. [Q8NEY8-9]
CCDS55817.1. [Q8NEY8-6]
CCDS8741.1. [Q8NEY8-8]
RefSeqiNP_001137259.1. NM_001143787.1. [Q8NEY8-3]
NP_001137260.1. NM_001143788.1. [Q8NEY8-9]
NP_057572.5. NM_016488.6. [Q8NEY8-1]
NP_958846.1. NM_201438.1. [Q8NEY8-5]
NP_958847.1. NM_201439.1. [Q8NEY8-8]
NP_958848.1. NM_201440.1. [Q8NEY8-6]
NP_958923.1. NM_201515.1. [Q8NEY8-2]
UniGeneiHs.444157.

Genome annotation databases

EnsembliENST00000358314; ENSP00000351066; ENSG00000134283. [Q8NEY8-8]
ENST00000395568; ENSP00000378935; ENSG00000134283. [Q8NEY8-1]
ENST00000395580; ENSP00000378947; ENSG00000134283. [Q8NEY8-2]
ENST00000432191; ENSP00000393965; ENSG00000134283. [Q8NEY8-3]
ENST00000449194; ENSP00000390681; ENSG00000134283. [Q8NEY8-9]
ENST00000552761; ENSP00000449331; ENSG00000134283. [Q8NEY8-6]
ENST00000610488; ENSP00000479913; ENSG00000134283. [Q8NEY8-1]
ENST00000613154; ENSP00000478872; ENSG00000134283. [Q8NEY8-9]
ENST00000619544; ENSP00000477681; ENSG00000134283. [Q8NEY8-3]
GeneIDi51535.
KEGGihsa:51535.
UCSCiuc001rnb.4. human. [Q8NEY8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY039238 mRNA. Translation: AAK68657.1.
AY157850 mRNA. Translation: AAO16497.1.
AF151040 mRNA. Translation: AAF36126.1. Frameshift.
AF151066 mRNA. Translation: AAF36152.1. Frameshift.
AK055690 mRNA. Translation: BAB70985.1.
AK000186 mRNA. Translation: BAA90996.1.
CR621833 mRNA. No translation available.
AC020629 Genomic DNA. No translation available.
AC079601 Genomic DNA. No translation available.
AC079684 Genomic DNA. No translation available.
BC025306 mRNA. Translation: AAH25306.1. Different initiation.
BC039832 mRNA. Translation: AAH39832.1.
CCDSiCCDS31777.1. [Q8NEY8-1]
CCDS41773.1. [Q8NEY8-2]
CCDS44860.1. [Q8NEY8-3]
CCDS44861.1. [Q8NEY8-9]
CCDS55817.1. [Q8NEY8-6]
CCDS8741.1. [Q8NEY8-8]
RefSeqiNP_001137259.1. NM_001143787.1. [Q8NEY8-3]
NP_001137260.1. NM_001143788.1. [Q8NEY8-9]
NP_057572.5. NM_016488.6. [Q8NEY8-1]
NP_958846.1. NM_201438.1. [Q8NEY8-5]
NP_958847.1. NM_201439.1. [Q8NEY8-8]
NP_958848.1. NM_201440.1. [Q8NEY8-6]
NP_958923.1. NM_201515.1. [Q8NEY8-2]
UniGeneiHs.444157.

3D structure databases

ProteinModelPortaliQ8NEY8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119596. 59 interactions.
DIPiDIP-49051N.
IntActiQ8NEY8. 35 interactions.
MINTiMINT-1431126.
STRINGi9606.ENSP00000378935.

PTM databases

iPTMnetiQ8NEY8.
PhosphoSiteiQ8NEY8.

Polymorphism and mutation databases

BioMutaiPPHLN1.
DMDMi46396942.

Proteomic databases

EPDiQ8NEY8.
MaxQBiQ8NEY8.
PaxDbiQ8NEY8.
PeptideAtlasiQ8NEY8.
PRIDEiQ8NEY8.

Protocols and materials databases

DNASUi51535.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358314; ENSP00000351066; ENSG00000134283. [Q8NEY8-8]
ENST00000395568; ENSP00000378935; ENSG00000134283. [Q8NEY8-1]
ENST00000395580; ENSP00000378947; ENSG00000134283. [Q8NEY8-2]
ENST00000432191; ENSP00000393965; ENSG00000134283. [Q8NEY8-3]
ENST00000449194; ENSP00000390681; ENSG00000134283. [Q8NEY8-9]
ENST00000552761; ENSP00000449331; ENSG00000134283. [Q8NEY8-6]
ENST00000610488; ENSP00000479913; ENSG00000134283. [Q8NEY8-1]
ENST00000613154; ENSP00000478872; ENSG00000134283. [Q8NEY8-9]
ENST00000619544; ENSP00000477681; ENSG00000134283. [Q8NEY8-3]
GeneIDi51535.
KEGGihsa:51535.
UCSCiuc001rnb.4. human. [Q8NEY8-1]

Organism-specific databases

CTDi51535.
GeneCardsiPPHLN1.
HGNCiHGNC:19369. PPHLN1.
HPAiHPA038902.
HPA038903.
MIMi608150. gene.
neXtProtiNX_Q8NEY8.
PharmGKBiPA134881011.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFSB. Eukaryota.
ENOG4111JYA. LUCA.
GeneTreeiENSGT00390000016228.
HOVERGENiHBG053653.
InParanoidiQ8NEY8.
PhylomeDBiQ8NEY8.
TreeFamiTF335813.

Miscellaneous databases

ChiTaRSiPPHLN1. human.
GeneWikiiPPHLN1.
GenomeRNAii51535.
PROiQ8NEY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NEY8.
CleanExiHS_PPHLN1.
ExpressionAtlasiQ8NEY8. baseline and differential.
GenevisibleiQ8NEY8. HS.

Family and domain databases

InterProiIPR028851. Pphln1.
[Graphical view]
PANTHERiPTHR15836:SF2. PTHR15836:SF2. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Serological identification and expression analysis of gastric cancer-associated genes."
    Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.
    Br. J. Cancer 86:1824-1830(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Gastric adenocarcinoma.
  2. "Characterization of periphilin, a widespread, highly insoluble nuclear protein and potential constituent of the keratinocyte cornified envelope."
    Kazerounian S., Aho S.
    J. Biol. Chem. 278:36707-36717(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, HOMODIMERIZATION, INTERACTION WITH PPL, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Keratinocyte.
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Umbilical cord blood.
  4. "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.
    , 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] (ISOFORMS 7 AND 8).
    Tissue: Colon.
  5. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
    Tissue: Placenta.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 3 AND 5).
    Tissue: Brain and Skin.
  8. "Overexpression of CR/periphilin downregulates Cdc7 expression and induces S-phase arrest."
    Kurita M., Suzuki H., Masai H., Mizumoto K., Ogata E., Nishimoto I., Aiso S., Matsuoka M.
    Biochem. Biophys. Res. Commun. 324:554-561(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "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-133 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "CR/periphilin is a transcriptional co-repressor involved in cell cycle progression."
    Kurita M., Suzuki H., Kawano Y., Aiso S., Matsuoka M.
    Biochem. Biophys. Res. Commun. 364:930-936(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SIN3A AND HDAC1.
  12. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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].
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235 AND LYS-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-110; SER-133; SER-161; SER-167 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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-133 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-114; SER-133; SER-197; SER-201 AND SER-325, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240 AND LYS-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Epigenetic silencing by the HUSH complex mediates position-effect variegation in human cells."
    Tchasovnikarova I.A., Timms R.T., Matheson N.J., Wals K., Antrobus R., Goettgens B., Dougan G., Dawson M.A., Lehner P.J.
    Science 348:1481-1485(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE HUSH COMPLEX.
  24. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-173.

Entry informationi

Entry nameiPPHLN_HUMAN
AccessioniPrimary (citable) accession number: Q8NEY8
Secondary accession number(s): E9PAX8
, Q86YT2, Q8IXN3, Q8TB09, Q96NB9, Q9NXL4, Q9P0P6, Q9P0R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 6, 2016
This is version 124 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.