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Protein

Protein phosphatase 1 regulatory subunit 15B

Gene

PPP1R15B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Translation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 15B
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14951. PPP1R15B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33633.

Polymorphism and mutation databases

BioMutaiPPP1R15B.
DMDMi74743925.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Protein phosphatase 1 regulatory subunit 15BPRO_0000320520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei508 – 5081PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5SWA1.
MaxQBiQ5SWA1.
PaxDbiQ5SWA1.
PeptideAtlasiQ5SWA1.
PRIDEiQ5SWA1.

PTM databases

iPTMnetiQ5SWA1.
PhosphoSiteiQ5SWA1.

Expressioni

Gene expression databases

BgeeiQ5SWA1.
CleanExiHS_PPP1R15B.
GenevisibleiQ5SWA1. HS.

Organism-specific databases

HPAiHPA028352.
HPA061088.

Interactioni

Subunit structurei

Part of a complex containing PPP1R15B, PP1 and NCK1/2 (By similarity). Interacts with PP1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1CAP621363EBI-2815482,EBI-357253

Protein-protein interaction databases

IntActiQ5SWA1. 5 interactions.
MINTiMINT-1190309.
STRINGi9606.ENSP00000356156.

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi648 – 6525Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V0UX-ray7.88E/G/I/K/O631-701[»]
4V0VX-ray1.61B/D631-660[»]
4V0WX-ray1.55B/D631-669[»]
4V0XX-ray1.85B631-684[»]
ProteinModelPortaliQ5SWA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP1R15 family.Curated

Phylogenomic databases

eggNOGiENOG410IJ9C. Eukaryota.
ENOG4111TVA. LUCA.
HOGENOMiHOG000115677.
HOVERGENiHBG103996.
InParanoidiQ5SWA1.
OrthoDBiEOG77DJ5H.
PhylomeDBiQ5SWA1.
TreeFamiTF105548.

Family and domain databases

InterProiIPR019523. Prot_Pase1_reg-su15A/B_C.
IPR019512. Prot_Pase1_reg-su15B_N.
[Graphical view]
PfamiPF10472. CReP_N. 1 hit.
PF10488. PP1c_bdg. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SWA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPGTGGSRK RLGPRAGFRF WPPFFPRRSQ AGSSKFPTPL GPENSGNPTL
60 70 80 90 100
LSSAQPETRV SYWTKLLSQL LAPLPGLLQK VLIWSQLFGG MFPTRWLDFA
110 120 130 140 150
GVYSALRALK GREKPAAPTA QKSLSSLQLD SSDPSVTSPL DWLEEGIHWQ
160 170 180 190 200
YSPPDLKLEL KAKGSALDPA AQAFLLEQQL WGVELLPSSL QSRLYSNREL
210 220 230 240 250
GSSPSGPLNI QRIDNFSVVS YLLNPSYLDC FPRLEVSYQN SDGNSEVVGF
260 270 280 290 300
QTLTPESSCL REDHCHPQPL SAELIPASWQ GCPPLSTEGL PEIHHLRMKR
310 320 330 340 350
LEFLQQANKG QDLPTPDQDN GYHSLEEEHS LLRMDPKHCR DNPTQFVPAA
360 370 380 390 400
GDIPGNTQES TEEKIELLTT EVPLALEEES PSEGCPSSEI PMEKEPGEGR
410 420 430 440 450
ISVVDYSYLE GDLPISARPA CSNKLIDYIL GGASSDLETS SDPEGEDWDE
460 470 480 490 500
EAEDDGFDSD SSLSDSDLEQ DPEGLHLWNS FCSVDPYNPQ NFTATIQTAA
510 520 530 540 550
RIVPEEPSDS EKDLSGKSDL ENSSQSGSLP ETPEHSSGEE DDWESSADEA
560 570 580 590 600
ESLKLWNSFC NSDDPYNPLN FKAPFQTSGE NEKGCRDSKT PSESIVAISE
610 620 630 640 650
CHTLLSCKVQ LLGSQESECP DSVQRDVLSG GRHTHVKRKK VTFLEEVTEY
660 670 680 690 700
YISGDEDRKG PWEEFARDGC RFQKRIQETE DAIGYCLTFE HRERMFNRLQ
710
GTCFKGLNVL KQC
Length:713
Mass (Da):79,152
Last modified:December 21, 2004 - v1
Checksum:i193679F622E34257
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281R → Q in BAD96597 (Ref. 2) Curated
Sequence conflicti215 – 2151N → D in BAB55266 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261P → S.
Corresponds to variant rs12094135 [ dbSNP | Ensembl ].
VAR_039196
Natural varianti144 – 1441E → K.
Corresponds to variant rs4492688 [ dbSNP | Ensembl ].
VAR_039197
Natural varianti308 – 3081N → S.4 Publications
Corresponds to variant rs3014626 [ dbSNP | Ensembl ].
VAR_039198
Natural varianti363 – 3631E → G.
Corresponds to variant rs2089891 [ dbSNP | Ensembl ].
VAR_039199
Natural varianti589 – 5891K → E.1 Publication
Corresponds to variant rs17855962 [ dbSNP | Ensembl ].
VAR_039200
Natural varianti658 – 6581R → C Found in two patients with young-onset diabetes, microcephaly and short stature; unknown pathological significance; reduced binding to PP1; results in decreased down-regulation of EIF2S1 phosphorylation. 1 Publication
VAR_074072

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027650 mRNA. Translation: BAB55266.1.
AK222877 mRNA. Translation: BAD96597.1.
AL606489 Genomic DNA. Translation: CAI16570.1.
BC065280 mRNA. Translation: AAH65280.1.
AL833746 mRNA. Translation: CAH56240.1.
CCDSiCCDS1445.1.
UniGeneiHs.304376.

Genome annotation databases

EnsembliENST00000367188; ENSP00000356156; ENSG00000158615.
UCSCiuc001hav.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027650 mRNA. Translation: BAB55266.1.
AK222877 mRNA. Translation: BAD96597.1.
AL606489 Genomic DNA. Translation: CAI16570.1.
BC065280 mRNA. Translation: AAH65280.1.
AL833746 mRNA. Translation: CAH56240.1.
CCDSiCCDS1445.1.
UniGeneiHs.304376.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V0UX-ray7.88E/G/I/K/O631-701[»]
4V0VX-ray1.61B/D631-660[»]
4V0WX-ray1.55B/D631-669[»]
4V0XX-ray1.85B631-684[»]
ProteinModelPortaliQ5SWA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5SWA1. 5 interactions.
MINTiMINT-1190309.
STRINGi9606.ENSP00000356156.

PTM databases

iPTMnetiQ5SWA1.
PhosphoSiteiQ5SWA1.

Polymorphism and mutation databases

BioMutaiPPP1R15B.
DMDMi74743925.

Proteomic databases

EPDiQ5SWA1.
MaxQBiQ5SWA1.
PaxDbiQ5SWA1.
PeptideAtlasiQ5SWA1.
PRIDEiQ5SWA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367188; ENSP00000356156; ENSG00000158615.
UCSCiuc001hav.5. human.

Organism-specific databases

GeneCardsiPPP1R15B.
H-InvDBHIX0021246.
HGNCiHGNC:14951. PPP1R15B.
HPAiHPA028352.
HPA061088.
MIMi613257. gene.
neXtProtiNX_Q5SWA1.
PharmGKBiPA33633.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ9C. Eukaryota.
ENOG4111TVA. LUCA.
HOGENOMiHOG000115677.
HOVERGENiHBG103996.
InParanoidiQ5SWA1.
OrthoDBiEOG77DJ5H.
PhylomeDBiQ5SWA1.
TreeFamiTF105548.

Miscellaneous databases

ChiTaRSiPPP1R15B. human.
PROiQ5SWA1.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SWA1.
CleanExiHS_PPP1R15B.
GenevisibleiQ5SWA1. HS.

Family and domain databases

InterProiIPR019523. Prot_Pase1_reg-su15A/B_C.
IPR019512. Prot_Pase1_reg-su15B_N.
[Graphical view]
PfamiPF10472. CReP_N. 1 hit.
PF10488. PP1c_bdg. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANT SER-308.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-308.
    Tissue: Liver.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS SER-308 AND GLU-589.
    Tissue: Eye.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-713, VARIANT SER-308.
    Tissue: Stomach.
  6. "A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress."
    Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.
    Science 307:935-939(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PP1.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-203; SER-205 AND SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  9. Cited for: VARIANT CYS-658, CHARACTERIZATION OF VARIANT CYS-658.

Entry informationi

Entry nameiPR15B_HUMAN
AccessioniPrimary (citable) accession number: Q5SWA1
Secondary accession number(s): Q53GQ4
, Q658M2, Q6P156, Q96SN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: July 6, 2016
This is version 88 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

Miscellaneous

The phosphatase activity of the PPP1R15B-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.