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Q16537

- 2A5E_HUMAN

UniProt

Q16537 - 2A5E_HUMAN

Protein

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

Gene

PPP2R5E

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    1. protein binding Source: IntAct
    2. protein phosphatase type 2A regulator activity Source: ProtInc

    GO - Biological processi

    1. regulation of catalytic activity Source: GOC
    2. signal transduction Source: InterPro

    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_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    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: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9313. PPP2R5E.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. protein phosphatase type 2A complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33677.

    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.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ16537.
    PaxDbiQ16537.
    PRIDEiQ16537.

    PTM databases

    PhosphoSiteiQ16537.

    Expressioni

    Gene expression databases

    ArrayExpressiQ16537.
    BgeeiQ16537.
    CleanExiHS_PPP2R5E.
    GenevestigatoriQ16537.

    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. 23 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.
    HOGENOMiHOG000067326.
    HOVERGENiHBG000009.
    InParanoidiQ16537.
    KOiK11584.
    OMAiTEQAYPE.
    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. Align

    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

    MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL    50
    LKDVPSSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI 100
    TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH 150
    LQLVYEFFIR FLESQEFQPS IAKKYIDQKF VLQLLELFDS EDPRERDYLK 200
    TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE LLEILGSIIN 250
    GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE 300
    PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK 350
    CVSSPHFQVA ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN 400
    PAIVALVYNV LKAFMEMNST MFDELTATYK SDRQREKKKE KEREELWKKL 450
    EDLELKRGLR RDGIIPT 467
    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:
    EMBL
    GenBank
    DDBJ
    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.
    NP_001269111.1. NM_001282182.1.
    NP_006237.1. NM_006246.3. [Q16537-1]
    UniGeneiHs.334868.
    Hs.594347.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi7387498.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS61467.1. [Q16537-3 ]
    CCDS61468.1. [Q16537-2 ]
    CCDS9758.1. [Q16537-1 ]
    RefSeqi NP_001269108.1. NM_001282179.1. [Q16537-1 ]
    NP_001269109.1. NM_001282180.1. [Q16537-2 ]
    NP_001269110.1. NM_001282181.1.
    NP_001269111.1. NM_001282182.1.
    NP_006237.1. NM_006246.3. [Q16537-1 ]
    UniGenei Hs.334868.
    Hs.594347.

    3D structure databases

    ProteinModelPortali Q16537.
    SMRi Q16537. Positions 51-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111521. 23 interactions.
    IntActi Q16537. 32 interactions.
    MINTi MINT-1198703.
    STRINGi 9606.ENSP00000337641.

    PTM databases

    PhosphoSitei Q16537.

    Polymorphism databases

    DMDMi 7387498.

    Proteomic databases

    MaxQBi Q16537.
    PaxDbi Q16537.
    PRIDEi Q16537.

    Protocols and materials databases

    DNASUi 5529.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337537 ; ENSP00000337641 ; ENSG00000154001 . [Q16537-1 ]
    ENST00000422769 ; ENSP00000404632 ; ENSG00000154001 . [Q16537-3 ]
    ENST00000555899 ; ENSP00000452396 ; ENSG00000154001 . [Q16537-2 ]
    GeneIDi 5529.
    KEGGi hsa:5529.
    UCSCi uc001xgd.1. human. [Q16537-1 ]

    Organism-specific databases

    CTDi 5529.
    GeneCardsi GC14M063838.
    HGNCi HGNC:9313. PPP2R5E.
    HPAi HPA006034.
    MIMi 601647. gene.
    neXtProti NX_Q16537.
    PharmGKBi PA33677.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264925.
    HOGENOMi HOG000067326.
    HOVERGENi HBG000009.
    InParanoidi Q16537.
    KOi K11584.
    OMAi TEQAYPE.
    OrthoDBi EOG7C2R2S.
    PhylomeDBi Q16537.
    TreeFami TF105556.

    Enzyme and pathway databases

    Reactomei REACT_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_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    REACT_682. Mitotic Prometaphase.
    SignaLinki Q16537.

    Miscellaneous databases

    ChiTaRSi PPP2R5E. human.
    GeneWikii PPP2R5E.
    GenomeRNAii 5529.
    NextBioi 21418.
    PROi Q16537.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16537.
    Bgeei Q16537.
    CleanExi HS_PPP2R5E.
    Genevestigatori Q16537.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR002554. PP2A_B56.
    [Graphical view ]
    PANTHERi PTHR10257. PTHR10257. 1 hit.
    Pfami PF01603. B56. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028043. PP2A_B56. 1 hit.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 121 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