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Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform

Gene

PPP2R5E

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

Functioni

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.

GO - Molecular functioni

  • protein phosphatase type 2A regulator activity Source: ProtInc

GO - Biological processi

  • regulation of protein phosphatase type 2A activity Source: GOC
  • signal transduction Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23879. Platelet sensitization by LDL.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.
SignaLinkiQ16537.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
Alternative name(s):
PP2A B subunit isoform B'-epsilon
PP2A B subunit isoform B56-epsilon
PP2A B subunit isoform PR61-epsilon
PP2A B subunit isoform R5-epsilon
Gene namesi
Name:PPP2R5E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9313. PPP2R5E.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33677.

Polymorphism and mutation databases

DMDMi7387498.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 467466Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoformPRO_0000071454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei30 – 301Phosphoserine1 Publication
Modified residuei32 – 321Phosphoserine1 Publication
Modified residuei34 – 341Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine residues.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16537.
PaxDbiQ16537.
PRIDEiQ16537.

PTM databases

PhosphoSiteiQ16537.

Expressioni

Gene expression databases

BgeeiQ16537.
CleanExiHS_PPP2R5E.
GenevisibleiQ16537. HS.

Organism-specific databases

HPAiHPA006034.

Interactioni

Subunit structurei

Found in a complex with at least ARL2, PPP2CB; PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGOL1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK2O960173EBI-968374,EBI-1180783
DZIP1Q86YF93EBI-968374,EBI-998108
PPP2R1AP301533EBI-968374,EBI-302388
PPP2R1BP301543EBI-968374,EBI-357094
RACGAP1Q9H0H55EBI-968374,EBI-717233
ZDHHC17Q8IUH52EBI-968374,EBI-524753

Protein-protein interaction databases

BioGridi111521. 38 interactions.
IntActiQ16537. 32 interactions.
MINTiMINT-1198703.
STRINGi9606.ENSP00000337641.

Structurei

3D structure databases

ProteinModelPortaliQ16537.
SMRiQ16537. Positions 51-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG264925.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ16537.
KOiK11584.
OMAiCTVFDFM.
OrthoDBiEOG7C2R2S.
PhylomeDBiQ16537.
TreeFamiTF105556.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16537-1) [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
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL
60 70 80 90 100
LKDVPSSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI
110 120 130 140 150
TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH
160 170 180 190 200
LQLVYEFFIR FLESQEFQPS IAKKYIDQKF VLQLLELFDS EDPRERDYLK
210 220 230 240 250
TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE LLEILGSIIN
260 270 280 290 300
GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE
310 320 330 340 350
PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK
360 370 380 390 400
CVSSPHFQVA ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN
410 420 430 440 450
PAIVALVYNV LKAFMEMNST MFDELTATYK SDRQREKKKE KEREELWKKL
460
EDLELKRGLR RDGIIPT
Length:467
Mass (Da):54,699
Last modified:November 1, 1996 - v1
Checksum:iDD9CE11433F499CF
GO
Isoform 2 (identifier: Q16537-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     430-435: KSDRQR → N

Note: No experimental confirmation available.
Show »
Length:462
Mass (Da):54,043
Checksum:iC37302CC366D270C
GO
Isoform 3 (identifier: Q16537-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.

Note: No experimental confirmation available.
Show »
Length:391
Mass (Da):46,180
Checksum:i076E305A94E9F54B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti194 – 1941R → W in BAH14801 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7676Missing in isoform 3. 1 PublicationVSP_055163Add
BLAST
Alternative sequencei430 – 4356KSDRQR → N in isoform 2. 1 PublicationVSP_054588

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69029 mRNA. Translation: CAA93153.1.
L76703 mRNA. Translation: AAB69752.1.
AK316430 mRNA. Translation: BAH14801.1.
AL118555 Genomic DNA. No translation available.
AL132992 Genomic DNA. No translation available.
AL136038 Genomic DNA. No translation available.
BC093766 mRNA. Translation: AAH93766.1.
BC101479 mRNA. Translation: AAI01480.1.
BC143231 mRNA. Translation: AAI43232.1.
BC143234 mRNA. Translation: AAI43235.1.
CCDSiCCDS61467.1. [Q16537-3]
CCDS61468.1. [Q16537-2]
CCDS9758.1. [Q16537-1]
RefSeqiNP_001269108.1. NM_001282179.1. [Q16537-1]
NP_001269109.1. NM_001282180.1. [Q16537-2]
NP_001269110.1. NM_001282181.1. [Q16537-3]
NP_001269111.1. NM_001282182.1. [Q16537-3]
NP_006237.1. NM_006246.3. [Q16537-1]
XP_011535224.1. XM_011536922.1. [Q16537-1]
UniGeneiHs.334868.
Hs.594347.

Genome annotation databases

EnsembliENST00000337537; ENSP00000337641; ENSG00000154001.
ENST00000422769; ENSP00000404632; ENSG00000154001. [Q16537-3]
ENST00000555899; ENSP00000452396; ENSG00000154001. [Q16537-2]
GeneIDi5529.
KEGGihsa:5529.
UCSCiuc001xgd.1. human. [Q16537-1]
uc010tsh.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69029 mRNA. Translation: CAA93153.1.
L76703 mRNA. Translation: AAB69752.1.
AK316430 mRNA. Translation: BAH14801.1.
AL118555 Genomic DNA. No translation available.
AL132992 Genomic DNA. No translation available.
AL136038 Genomic DNA. No translation available.
BC093766 mRNA. Translation: AAH93766.1.
BC101479 mRNA. Translation: AAI01480.1.
BC143231 mRNA. Translation: AAI43232.1.
BC143234 mRNA. Translation: AAI43235.1.
CCDSiCCDS61467.1. [Q16537-3]
CCDS61468.1. [Q16537-2]
CCDS9758.1. [Q16537-1]
RefSeqiNP_001269108.1. NM_001282179.1. [Q16537-1]
NP_001269109.1. NM_001282180.1. [Q16537-2]
NP_001269110.1. NM_001282181.1. [Q16537-3]
NP_001269111.1. NM_001282182.1. [Q16537-3]
NP_006237.1. NM_006246.3. [Q16537-1]
XP_011535224.1. XM_011536922.1. [Q16537-1]
UniGeneiHs.334868.
Hs.594347.

3D structure databases

ProteinModelPortaliQ16537.
SMRiQ16537. Positions 51-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111521. 38 interactions.
IntActiQ16537. 32 interactions.
MINTiMINT-1198703.
STRINGi9606.ENSP00000337641.

PTM databases

PhosphoSiteiQ16537.

Polymorphism and mutation databases

DMDMi7387498.

Proteomic databases

MaxQBiQ16537.
PaxDbiQ16537.
PRIDEiQ16537.

Protocols and materials databases

DNASUi5529.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337537; ENSP00000337641; ENSG00000154001.
ENST00000422769; ENSP00000404632; ENSG00000154001. [Q16537-3]
ENST00000555899; ENSP00000452396; ENSG00000154001. [Q16537-2]
GeneIDi5529.
KEGGihsa:5529.
UCSCiuc001xgd.1. human. [Q16537-1]
uc010tsh.1. human.

Organism-specific databases

CTDi5529.
GeneCardsiGC14M063838.
HGNCiHGNC:9313. PPP2R5E.
HPAiHPA006034.
MIMi601647. gene.
neXtProtiNX_Q16537.
PharmGKBiPA33677.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264925.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ16537.
KOiK11584.
OMAiCTVFDFM.
OrthoDBiEOG7C2R2S.
PhylomeDBiQ16537.
TreeFamiTF105556.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23879. Platelet sensitization by LDL.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.
SignaLinkiQ16537.

Miscellaneous databases

ChiTaRSiPPP2R5E. human.
GeneWikiiPPP2R5E.
GenomeRNAii5529.
NextBioi21418.
PROiQ16537.
SOURCEiSearch...

Gene expression databases

BgeeiQ16537.
CleanExiHS_PPP2R5E.
GenevisibleiQ16537. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
    Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
    Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 449-455.
    Tissue: Fetal retina.
  2. "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
    McCright B., Rivers A.M., Audlin S., Virshup D.M.
    J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  3. "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] (ISOFORM 3).
    Tissue: Testis.
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1 AND 2).
    Tissue: Brain.
  6. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
    Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
    Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGOL1.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-30; SER-32 AND SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry namei2A5E_HUMAN
AccessioniPrimary (citable) accession number: Q16537
Secondary accession number(s): A4FU37
, B7ZAW5, B7ZKK8, B7ZKK9, J3KQN6, Q52LW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 130 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

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 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.