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Protein

Phostensin

Gene

PPP1R18

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

Functioni

Isoform 1: May target protein phosphatase 1 to F-actin cytoskeleton.1 Publication
Isoform 4: May target protein phosphatase 1 to F-actin cytoskeleton.1 Publication

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phostensin
Alternative name(s):
Protein phosphatase 1 F-actin cytoskeleton-targeting subunit
Protein phosphatase 1 regulatory subunit 18
Gene namesi
Name:PPP1R18
Synonyms:HKMT1098, KIAA1949
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:29413. PPP1R18.

Subcellular locationi

Isoform 1 :
Isoform 4 :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi540 – 5401I → G: Decrease binding to PP1. Complete inhibition of PP1 binding; when associated with G-542. 1 Publication
Mutagenesisi542 – 5421F → G: Decrease binding to PP1. Decrease binding to PP1. Complete inhibition of PP1 binding; when associated with G-540. 1 Publication

Organism-specific databases

PharmGKBiPA134918172.

Polymorphism and mutation databases

BioMutaiPPP1R18.
DMDMi68052323.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 613613PhostensinPRO_0000050807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei175 – 1751PhosphoserineCombined sources
Modified residuei195 – 1951PhosphoserineCombined sources
Modified residuei199 – 1991PhosphothreonineCombined sources
Modified residuei224 – 2241PhosphoserineCombined sources
Modified residuei368 – 3681PhosphoserineCombined sources
Modified residuei432 – 4321PhosphoserineBy similarity
Modified residuei457 – 4571N6-acetyllysineBy similarity
Modified residuei530 – 5301PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6NYC8.
MaxQBiQ6NYC8.
PaxDbiQ6NYC8.
PRIDEiQ6NYC8.

PTM databases

iPTMnetiQ6NYC8.
PhosphoSiteiQ6NYC8.

Expressioni

Tissue specificityi

Isoform 4 is predominantly expressed in leukocytes and spleen.1 Publication

Gene expression databases

BgeeiQ6NYC8.
ExpressionAtlasiQ6NYC8. baseline and differential.
GenevisibleiQ6NYC8. HS.

Organism-specific databases

HPAiHPA044745.
HPA051000.

Interactioni

Subunit structurei

Interacts with Protein phosphatase 1 (PP1).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCOCO2Q131373EBI-2557469,EBI-739580
CARD9Q9H2573EBI-2557469,EBI-751319
CCDC102BA1A4H13EBI-2557469,EBI-10171570
CCDC136Q96JN2-23EBI-2557469,EBI-10171416
CCDC155Q8N6L03EBI-2557469,EBI-749265
CCDC57Q2TAC23EBI-2557469,EBI-2808286
DESP176613EBI-2557469,EBI-1055572
FAM9BQ8IZU03EBI-2557469,EBI-10175124
FSD2A1L4K13EBI-2557469,EBI-5661036
GOLGA2Q083793EBI-2557469,EBI-618309
HOMER3B2RA103EBI-2557469,EBI-10175777
KCTD9Q7L2733EBI-2557469,EBI-4397613
KRT13A1A4E93EBI-2557469,EBI-10171552
KRT15P190123EBI-2557469,EBI-739566
KRT19P087273EBI-2557469,EBI-742756
KRT31Q153233EBI-2557469,EBI-948001
KRT40Q6A1623EBI-2557469,EBI-10171697
LZTS2Q9BRK43EBI-2557469,EBI-741037
MID2Q9UJV3-23EBI-2557469,EBI-10172526
MTUS2Q5JR593EBI-2557469,EBI-742948
NEFLI6L9F63EBI-2557469,EBI-10178578
NEFLP071963EBI-2557469,EBI-475646
PDE4DIPQ5VU433EBI-2557469,EBI-1105124
SPDL1Q96EA43EBI-2557469,EBI-715381
SPERTQ8NA613EBI-2557469,EBI-741724
STX11O755583EBI-2557469,EBI-714135
TCF4P158843EBI-2557469,EBI-533224
TEX11Q8IYF33EBI-2557469,EBI-742397
TFIP11Q9UBB93EBI-2557469,EBI-1105213
TRAF2Q129333EBI-2557469,EBI-355744
TRIM23P364063EBI-2557469,EBI-740098
TRIM27P143734EBI-2557469,EBI-719493
TRIM54Q9BYV23EBI-2557469,EBI-2130429
TRIM69Q86WT63EBI-2557469,EBI-749955
TSGA10Q9BZW73EBI-2557469,EBI-744794
VPS52Q8N1B43EBI-2557469,EBI-2799833

Protein-protein interaction databases

BioGridi128092. 66 interactions.
IntActiQ6NYC8. 58 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ6NYC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 1038Poly-Gln

Phylogenomic databases

eggNOGiENOG410IJQY. Eukaryota.
ENOG410ZUB8. LUCA.
GeneTreeiENSGT00530000064035.
HOVERGENiHBG080180.
InParanoidiQ6NYC8.
KOiK17559.
OMAiWTPRDTE.
OrthoDBiEOG7Z3F49.
PhylomeDBiQ6NYC8.
TreeFamiTF337604.

Family and domain databases

InterProiIPR025903. Phostensin/Taperin_N_dom.
IPR025907. Phostensin/Taperin_PP1-bd_dom.
IPR026671. PPP1R18/Tprn.
[Graphical view]
PANTHERiPTHR21685. PTHR21685. 1 hit.
PfamiPF13914. Phostensin. 1 hit.
PF13916. Phostensin_N. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6NYC8-1) [UniParc]FASTAAdd to basket

Also known as: 110 kDa, phostensin-beta

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
MATIPDWKLQ LLARRRQEEA SVRGREKAER ERLSQMPAWK RGLLERRRAK
60 70 80 90 100
LGLSPGEPSP VLGTVEAGPP DPDESAVLLE AIGPVHQNRF IRQERQQQQQ
110 120 130 140 150
QQQRSEELLA ERKPGPLEAR ERRPSPGEMR DQSPKGRESR EERLSPRETR
160 170 180 190 200
ERRLGIGGAQ ELSLRPLEAR DWRQSPGEVG DRSSRLSEAW KWRLSPGETP
210 220 230 240 250
ERSLRLAESR EQSPRRKEVE SRLSPGESAY QKLGLTEAHK WRPDSRESQE
260 270 280 290 300
QSLVQLEATE WRLRSGEERQ DYSEECGRKE EWPVPGVAPK ETAELSETLT
310 320 330 340 350
REAQGNSSAG VEAAEQRPVE DGERGMKPTE GWKWTLNSGK AREWTPRDIE
360 370 380 390 400
AQTQKPEPPE SAEKLLESPG VEAGEGEAEK EEAGAQGRPL RALQNCCSVP
410 420 430 440 450
SPLPPEDAGT GGLRQQEEEA VELQPPPPAP LSPPPPAPTA PQPPGDPLMS
460 470 480 490 500
RLFYGVKAGP GVGAPRRSGH TFTVNPRRSV PPATPATPTS PATVDAAVPG
510 520 530 540 550
AGKKRYPTAE EILVLGGYLR LSRSCLAKGS PERHHKQLKI SFSETALETT
560 570 580 590 600
YQYPSESSVL EELGPEPEVP SAPNPPAAQP DDEEDEEELL LLQPELQGGL
610
RTKALIVDES CRR
Length:613
Mass (Da):67,943
Last modified:July 5, 2004 - v1
Checksum:iAB1F7C82DD50BB66
GO
Isoform 2 (identifier: Q6NYC8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     337-377: NSGKAREWTP...SPGVEAGEGE → IMSLAGKGNQ...LIQSPWCGWG
     378-613: Missing.

Show »
Length:377
Mass (Da):42,833
Checksum:i604591F8FB80F24D
GO
Isoform 3 (identifier: Q6NYC8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-325: Missing.
     562-582: ELGPEPEVPSAPNPPAAQPDD → RRRAKLGLSP...DQSPKGRESR

Note: No experimental confirmation available.
Show »
Length:362
Mass (Da):39,373
Checksum:iB48C33E8148B37BB
GO
Isoform 4 (identifier: Q6NYC8-4) [UniParc]FASTAAdd to basket

Also known as: 26kDa, phostensin-alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1-448: Missing.

Show »
Length:165
Mass (Da):17,771
Checksum:iB207EF0F57B36324
GO

Sequence cautioni

The sequence BAB85535.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811A → T in BAC86229 (PubMed:14702039).Curated
Sequence conflicti237 – 2371E → G in BAC86229 (PubMed:14702039).Curated
Sequence conflicti307 – 3071S → G in BAD38640 (PubMed:15221005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti222 – 2221R → G.1 Publication
Corresponds to variant rs9262144 [ dbSNP | Ensembl ].
VAR_046132
Natural varianti339 – 3391G → R.2 Publications
Corresponds to variant rs9262143 [ dbSNP | Ensembl ].
VAR_046133
Natural varianti356 – 3561P → L.
Corresponds to variant rs2213944 [ dbSNP | Ensembl ].
VAR_034045

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 448448Missing in isoform 4. VSP_057117Add
BLAST
Alternative sequencei1 – 325325Missing in isoform 3. VSP_057118Add
BLAST
Alternative sequencei337 – 37741NSGKA…AGEGE → IMSLAGKGNQHLVTCFPHPV SGGRANCPISTLIQSPWCGW G in isoform 2. 1 PublicationVSP_014258Add
BLAST
Alternative sequencei378 – 613236Missing in isoform 2. 1 PublicationVSP_014259Add
BLAST
Alternative sequencei562 – 58221ELGPE…AQPDD → RRRAKLGLSPGEPSPVLGTV EAGPPDPDESAVLLEAIGPV HQNRFIRQERQQQQQQQQRS EELLAERKPGPLEARERRPS PGEMRDQSPKGRESR in isoform 3. VSP_057119Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ988947 mRNA. Translation: ABL61261.1.
AB075829 mRNA. Translation: BAB85535.1. Different initiation.
AB073600 mRNA. Translation: BAD38640.1.
AK124880 mRNA. Translation: BAG54110.1.
AK125639 mRNA. Translation: BAC86229.1.
AK126182 mRNA. Translation: BAC86478.1.
AL832318 mRNA. Translation: CAD38613.1.
BX647622 mRNA. Translation: CAI46080.1.
AL845353 Genomic DNA. Translation: CAX11917.1.
AL732442 Genomic DNA. Translation: CAM25008.1.
AL662797, AL662798 Genomic DNA. Translation: CAM25509.1.
AL662798, AL662797 Genomic DNA. Translation: CAM25551.1.
CR936878, CR753328 Genomic DNA. Translation: CAQ06808.1.
BX908728 Genomic DNA. Translation: CAQ07426.1.
CR788240 Genomic DNA. Translation: CAQ07566.1.
CR753328, CR936878 Genomic DNA. Translation: CAQ07800.1.
CR759873 Genomic DNA. Translation: CAQ08685.1.
CH471081 Genomic DNA. Translation: EAX03318.1.
BC006176 mRNA. Translation: AAH06176.1.
BC066644 mRNA. Translation: AAH66644.1.
CCDSiCCDS43444.1. [Q6NYC8-1]
RefSeqiNP_001128342.1. NM_001134870.1. [Q6NYC8-1]
NP_597728.1. NM_133471.3. [Q6NYC8-1]
UniGeneiHs.101150.

Genome annotation databases

EnsembliENST00000274853; ENSP00000274853; ENSG00000146112. [Q6NYC8-1]
ENST00000383573; ENSP00000373067; ENSG00000206485.
ENST00000399199; ENSP00000382150; ENSG00000146112. [Q6NYC8-1]
ENST00000400554; ENSP00000383400; ENSG00000206485.
ENST00000437121; ENSP00000405234; ENSG00000225060. [Q6NYC8-1]
ENST00000438815; ENSP00000413596; ENSG00000230341. [Q6NYC8-1]
ENST00000438945; ENSP00000400990; ENSG00000234000. [Q6NYC8-1]
ENST00000443517; ENSP00000404066; ENSG00000229998. [Q6NYC8-1]
ENST00000444206; ENSP00000416648; ENSG00000230341. [Q6NYC8-1]
ENST00000449705; ENSP00000388790; ENSG00000229998. [Q6NYC8-1]
ENST00000451544; ENSP00000400129; ENSG00000225060. [Q6NYC8-1]
ENST00000455935; ENSP00000412456; ENSG00000234000. [Q6NYC8-1]
ENST00000548255; ENSP00000446851; ENSG00000231247.
ENST00000615527; ENSP00000480270; ENSG00000146112. [Q6NYC8-1]
ENST00000615892; ENSP00000482578; ENSG00000146112. [Q6NYC8-4]
GeneIDi170954.
KEGGihsa:170954.
UCSCiuc003nra.4. human. [Q6NYC8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ988947 mRNA. Translation: ABL61261.1.
AB075829 mRNA. Translation: BAB85535.1. Different initiation.
AB073600 mRNA. Translation: BAD38640.1.
AK124880 mRNA. Translation: BAG54110.1.
AK125639 mRNA. Translation: BAC86229.1.
AK126182 mRNA. Translation: BAC86478.1.
AL832318 mRNA. Translation: CAD38613.1.
BX647622 mRNA. Translation: CAI46080.1.
AL845353 Genomic DNA. Translation: CAX11917.1.
AL732442 Genomic DNA. Translation: CAM25008.1.
AL662797, AL662798 Genomic DNA. Translation: CAM25509.1.
AL662798, AL662797 Genomic DNA. Translation: CAM25551.1.
CR936878, CR753328 Genomic DNA. Translation: CAQ06808.1.
BX908728 Genomic DNA. Translation: CAQ07426.1.
CR788240 Genomic DNA. Translation: CAQ07566.1.
CR753328, CR936878 Genomic DNA. Translation: CAQ07800.1.
CR759873 Genomic DNA. Translation: CAQ08685.1.
CH471081 Genomic DNA. Translation: EAX03318.1.
BC006176 mRNA. Translation: AAH06176.1.
BC066644 mRNA. Translation: AAH66644.1.
CCDSiCCDS43444.1. [Q6NYC8-1]
RefSeqiNP_001128342.1. NM_001134870.1. [Q6NYC8-1]
NP_597728.1. NM_133471.3. [Q6NYC8-1]
UniGeneiHs.101150.

3D structure databases

ProteinModelPortaliQ6NYC8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128092. 66 interactions.
IntActiQ6NYC8. 58 interactions.

PTM databases

iPTMnetiQ6NYC8.
PhosphoSiteiQ6NYC8.

Polymorphism and mutation databases

BioMutaiPPP1R18.
DMDMi68052323.

Proteomic databases

EPDiQ6NYC8.
MaxQBiQ6NYC8.
PaxDbiQ6NYC8.
PRIDEiQ6NYC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274853; ENSP00000274853; ENSG00000146112. [Q6NYC8-1]
ENST00000383573; ENSP00000373067; ENSG00000206485.
ENST00000399199; ENSP00000382150; ENSG00000146112. [Q6NYC8-1]
ENST00000400554; ENSP00000383400; ENSG00000206485.
ENST00000437121; ENSP00000405234; ENSG00000225060. [Q6NYC8-1]
ENST00000438815; ENSP00000413596; ENSG00000230341. [Q6NYC8-1]
ENST00000438945; ENSP00000400990; ENSG00000234000. [Q6NYC8-1]
ENST00000443517; ENSP00000404066; ENSG00000229998. [Q6NYC8-1]
ENST00000444206; ENSP00000416648; ENSG00000230341. [Q6NYC8-1]
ENST00000449705; ENSP00000388790; ENSG00000229998. [Q6NYC8-1]
ENST00000451544; ENSP00000400129; ENSG00000225060. [Q6NYC8-1]
ENST00000455935; ENSP00000412456; ENSG00000234000. [Q6NYC8-1]
ENST00000548255; ENSP00000446851; ENSG00000231247.
ENST00000615527; ENSP00000480270; ENSG00000146112. [Q6NYC8-1]
ENST00000615892; ENSP00000482578; ENSG00000146112. [Q6NYC8-4]
GeneIDi170954.
KEGGihsa:170954.
UCSCiuc003nra.4. human. [Q6NYC8-1]

Organism-specific databases

CTDi170954.
GeneCardsiPPP1R18.
HGNCiHGNC:29413. PPP1R18.
HPAiHPA044745.
HPA051000.
MIMi610990. gene.
neXtProtiNX_Q6NYC8.
PharmGKBiPA134918172.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJQY. Eukaryota.
ENOG410ZUB8. LUCA.
GeneTreeiENSGT00530000064035.
HOVERGENiHBG080180.
InParanoidiQ6NYC8.
KOiK17559.
OMAiWTPRDTE.
OrthoDBiEOG7Z3F49.
PhylomeDBiQ6NYC8.
TreeFamiTF337604.

Miscellaneous databases

ChiTaRSiPPP1R18. human.
GeneWikiiKIAA1949.
GenomeRNAii170954.
NextBioi89134.
PROiQ6NYC8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NYC8.
ExpressionAtlasiQ6NYC8. baseline and differential.
GenevisibleiQ6NYC8. HS.

Family and domain databases

InterProiIPR025903. Phostensin/Taperin_N_dom.
IPR025907. Phostensin/Taperin_PP1-bd_dom.
IPR026671. PPP1R18/Tprn.
[Graphical view]
PANTHERiPTHR21685. PTHR21685. 1 hit.
PfamiPF13914. Phostensin. 1 hit.
PF13916. Phostensin_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4), INTERACTION WITH PROTEIN PHOSPHATASE 1, MUTAGENESIS OF ILE-540 AND PHE-542, TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
    Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
    Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hepatoblastoma.
  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 2 AND 3), VARIANT ARG-339.
    Tissue: Hippocampus, Synovial cell and Thymus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Cervix.
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLY-222 AND ARG-339.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1).
    Tissue: B-cell and Testis.
  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-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-54; SER-175; SER-195; THR-199; SER-224 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Identification of the high molecular weight isoform of phostensin."
    Lin Y.S., Huang H.L., Liu W.T., Lin T.H., Huang H.B.
    Int. J. Mol. Sci. 15:1068-1079(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), INTERACTION WITH PROTEIN PHOSPHATASE 1, ALTERNATIVE SPLICING (ISOFORMS 1 AND 4).
  17. "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-54 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPPR18_HUMAN
AccessioniPrimary (citable) accession number: Q6NYC8
Secondary accession number(s): A2AB01
, A2AIB8, A4UBI6, A6NCB7, A8MSS7, B7ZCV7, Q68CK8, Q6ZTV1, Q6ZUJ6, Q8NDQ4, Q8TF52, Q9BRL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: July 5, 2004
Last modified: April 13, 2016
This is version 113 of the entry and version 1 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 6
    Human chromosome 6: 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.