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P14314

- GLU2B_HUMAN

UniProt

P14314 - GLU2B_HUMAN

Protein

Glucosidase 2 subunit beta

Gene

PRKCSH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Regulatory subunit of glucosidase II.1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi213 – 236241PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. ion channel binding Source: UniProt
    3. phosphoprotein binding Source: UniProt
    4. protein kinase C binding Source: UniProtKB
    5. RNA binding Source: Ensembl

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. innate immune response Source: Reactome
    3. intracellular signal transduction Source: UniProtKB
    4. in utero embryonic development Source: Ensembl
    5. liver development Source: Ensembl
    6. negative regulation of neuron projection development Source: Ensembl
    7. N-glycan processing Source: InterPro
    8. nitrogen compound metabolic process Source: Ensembl
    9. post-translational protein modification Source: Reactome
    10. protein folding Source: Reactome
    11. protein heterooligomerization Source: Ensembl
    12. protein N-linked glycosylation via asparagine Source: Reactome
    13. renal system development Source: Ensembl

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.2.1.84. 2681.
    ReactomeiREACT_23810. Calnexin/calreticulin cycle.
    REACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.
    SignaLinkiP14314.
    UniPathwayiUPA00957.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucosidase 2 subunit beta
    Alternative name(s):
    80K-H protein
    Glucosidase II subunit beta
    Protein kinase C substrate 60.1 kDa protein heavy chain
    Short name:
    PKCSH
    Gene namesi
    Name:PRKCSH
    Synonyms:G19P1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9411. PRKCSH.

    Subcellular locationi

    Endoplasmic reticulum PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProt
    2. endoplasmic reticulum lumen Source: Reactome
    3. intracellular Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Polycystic liver disease (PCLD) [MIM:174050]: A hepatobiliary disease characterized by overgrowth of biliary epithelium and supportive connective tissue, resulting in multiple liver cysts.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi174050. phenotype.
    Orphaneti2924. Isolated polycystic liver disease.
    PharmGKBiPA33774.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 14141 PublicationAdd
    BLAST
    Chaini15 – 528514Glucosidase 2 subunit betaPRO_0000004143Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Modified residuei89 – 891Phosphoserine; by PKCSequence Analysis
    Modified residuei166 – 1661N6-succinyllysineBy similarity
    Modified residuei383 – 3831Phosphoserine; by PKCSequence Analysis
    Modified residuei390 – 3901Phosphoserine; by PKCSequence Analysis
    Modified residuei434 – 4341Phosphoserine; by PKCSequence Analysis
    Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP14314.
    PaxDbiP14314.
    PRIDEiP14314.

    PTM databases

    PhosphoSiteiP14314.

    Miscellaneous databases

    PMAP-CutDBP14314.

    Expressioni

    Gene expression databases

    ArrayExpressiP14314.
    BgeeiP14314.
    CleanExiHS_PRKCSH.
    GenevestigatoriP14314.

    Organism-specific databases

    HPAiCAB004465.
    HPA041940.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH). Binds glycosylated PTPRC By similarity.By similarity

    Protein-protein interaction databases

    BioGridi111575. 28 interactions.
    IntActiP14314. 13 interactions.
    MINTiMINT-1380114.
    STRINGi9606.ENSP00000252455.

    Structurei

    3D structure databases

    ProteinModelPortaliP14314.
    SMRiP14314. Positions 423-512.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini209 – 24436EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini245 – 29046EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini413 – 46856PRKCSHAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi525 – 5284Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi313 – 33624Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 1 PRKCSH domain.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG289998.
    HOGENOMiHOG000007805.
    HOVERGENiHBG051738.
    InParanoidiP14314.
    KOiK08288.
    OrthoDBiEOG7DZ8JX.
    PhylomeDBiP14314.
    TreeFamiTF329550.

    Family and domain databases

    Gene3Di2.70.130.10. 1 hit.
    4.10.400.10. 2 hits.
    InterProiIPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR026874. Glucosidase_2_bsu.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR009011. Man6P_isomerase_rcpt-bd_dom.
    IPR028146. PRKCSH_N.
    [Graphical view]
    PANTHERiPTHR12630:SF1. PTHR12630:SF1. 1 hit.
    PfamiPF13202. EF-hand_5. 2 hits.
    PF12999. PRKCSH-like. 1 hit.
    [Graphical view]
    SMARTiSM00192. LDLa. 1 hit.
    [Graphical view]
    SUPFAMiSSF50911. SSF50911. 1 hit.
    SSF57424. SSF57424. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P14314-1) [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

    MLLPLLLLLP MCWAVEVKRP RGVSLTNHHF YDESKPFTCL DGSATIPFDQ    50
    VNDDYCDCKD GSDEPGTAAC PNGSFHCTNT GYKPLYIPSN RVNDGVCDCC 100
    DGTDEYNSGV ICENTCKEKG RKERESLQQM AEVTREGFRL KKILIEDWKK 150
    AREEKQKKLI ELQAGKKSLE DQVEMLRTVK EEAEKPEREA KEQHQKLWEE 200
    QLAAAKAQQE QELAADAFKE LDDDMDGTVS VTELQTHPEL DTDGDGALSE 250
    AEAQALLSGD TQTDATSFYD RVWAAIRDKY RSEALPTDLP APSAPDLTEP 300
    KEEQPPVPSS PTEEEEEEEE EEEEEAEEEE EEEDSEEAPP PLSPPQPASP 350
    AEEDKMPPYD EQTQAFIDAA QEARNKFEEA ERSLKDMEES IRNLEQEISF 400
    DFGPNGEFAY LYSQCYELTT NEYVYRLCPF KLVSQKPKLG GSPTSLGTWG 450
    SWIGPDHDKF SAMKYEQGTG CWQGPNRSTT VRLLCGKETM VTSTTEPSRC 500
    EYLMELMTPA ACPEPPPEAP TEDDHDEL 528
    Length:528
    Mass (Da):59,425
    Last modified:October 17, 2006 - v2
    Checksum:i8DAD9776037E878E
    GO
    Isoform 2 (identifier: P14314-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         337-346: EAPPPLSPPQ → VQGEQPK

    Show »
    Length:525
    Mass (Da):59,178
    Checksum:iABACF156C534F30E
    GO

    Sequence cautioni

    The sequence AAH15154.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti325 – 3251Missing in AAA52493. (PubMed:2793184)Curated
    Sequence conflicti325 – 3251Missing in AAA98668. (PubMed:9043864)Curated
    Sequence conflicti325 – 3251Missing in AAP88860. 1 PublicationCurated
    Sequence conflicti325 – 3251Missing in AAH13586. (PubMed:15057824)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti74 – 741S → N.
    Corresponds to variant rs10406672 [ dbSNP | Ensembl ].
    VAR_028761
    Natural varianti291 – 2911A → T.2 Publications
    Corresponds to variant rs11557488 [ dbSNP | Ensembl ].
    VAR_028762
    Natural varianti338 – 3381A → G.
    Corresponds to variant rs35847588 [ dbSNP | Ensembl ].
    VAR_048658

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei337 – 34610EAPPPLSPPQ → VQGEQPK in isoform 2. 2 PublicationsVSP_043749

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03075 mRNA. Translation: AAA52493.1.
    U50326
    , U50317, U50318, U50319, U50320, U50321, U50322, U50323, U50324, U50325 Genomic DNA. Translation: AAA98668.1.
    AF144075 mRNA. Translation: AAF66686.1.
    BT009858 mRNA. Translation: AAP88860.1.
    AK290433 mRNA. Translation: BAF83122.1.
    AC008481 Genomic DNA. No translation available.
    AC024575 Genomic DNA. No translation available.
    BC013586 mRNA. Translation: AAH13586.2.
    BC015154 mRNA. Translation: AAH15154.1. Different initiation.
    CCDSiCCDS32911.1. [P14314-1]
    CCDS45977.1. [P14314-2]
    PIRiA32469.
    RefSeqiNP_001001329.1. NM_001001329.2. [P14314-2]
    NP_001276031.1. NM_001289102.1. [P14314-2]
    NP_002734.2. NM_002743.3. [P14314-1]
    UniGeneiHs.610830.

    Genome annotation databases

    EnsembliENST00000586486; ENSP00000465948; ENSG00000130175.
    ENST00000587327; ENSP00000466012; ENSG00000130175. [P14314-2]
    ENST00000589838; ENSP00000465461; ENSG00000130175. [P14314-1]
    ENST00000591462; ENSP00000465489; ENSG00000130175. [P14314-2]
    GeneIDi5589.
    KEGGihsa:5589.
    UCSCiuc002mrt.3. human. [P14314-1]
    uc002mru.3. human. [P14314-2]

    Polymorphism databases

    DMDMi116242499.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03075 mRNA. Translation: AAA52493.1 .
    U50326
    , U50317 , U50318 , U50319 , U50320 , U50321 , U50322 , U50323 , U50324 , U50325 Genomic DNA. Translation: AAA98668.1 .
    AF144075 mRNA. Translation: AAF66686.1 .
    BT009858 mRNA. Translation: AAP88860.1 .
    AK290433 mRNA. Translation: BAF83122.1 .
    AC008481 Genomic DNA. No translation available.
    AC024575 Genomic DNA. No translation available.
    BC013586 mRNA. Translation: AAH13586.2 .
    BC015154 mRNA. Translation: AAH15154.1 . Different initiation.
    CCDSi CCDS32911.1. [P14314-1 ]
    CCDS45977.1. [P14314-2 ]
    PIRi A32469.
    RefSeqi NP_001001329.1. NM_001001329.2. [P14314-2 ]
    NP_001276031.1. NM_001289102.1. [P14314-2 ]
    NP_002734.2. NM_002743.3. [P14314-1 ]
    UniGenei Hs.610830.

    3D structure databases

    ProteinModelPortali P14314.
    SMRi P14314. Positions 423-512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111575. 28 interactions.
    IntActi P14314. 13 interactions.
    MINTi MINT-1380114.
    STRINGi 9606.ENSP00000252455.

    PTM databases

    PhosphoSitei P14314.

    Polymorphism databases

    DMDMi 116242499.

    Proteomic databases

    MaxQBi P14314.
    PaxDbi P14314.
    PRIDEi P14314.

    Protocols and materials databases

    DNASUi 5589.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000586486 ; ENSP00000465948 ; ENSG00000130175 .
    ENST00000587327 ; ENSP00000466012 ; ENSG00000130175 . [P14314-2 ]
    ENST00000589838 ; ENSP00000465461 ; ENSG00000130175 . [P14314-1 ]
    ENST00000591462 ; ENSP00000465489 ; ENSG00000130175 . [P14314-2 ]
    GeneIDi 5589.
    KEGGi hsa:5589.
    UCSCi uc002mrt.3. human. [P14314-1 ]
    uc002mru.3. human. [P14314-2 ]

    Organism-specific databases

    CTDi 5589.
    GeneCardsi GC19P011546.
    HGNCi HGNC:9411. PRKCSH.
    HPAi CAB004465.
    HPA041940.
    MIMi 174050. phenotype.
    177060. gene.
    neXtProti NX_P14314.
    Orphaneti 2924. Isolated polycystic liver disease.
    PharmGKBi PA33774.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289998.
    HOGENOMi HOG000007805.
    HOVERGENi HBG051738.
    InParanoidi P14314.
    KOi K08288.
    OrthoDBi EOG7DZ8JX.
    PhylomeDBi P14314.
    TreeFami TF329550.

    Enzyme and pathway databases

    UniPathwayi UPA00957 .
    BRENDAi 3.2.1.84. 2681.
    Reactomei REACT_23810. Calnexin/calreticulin cycle.
    REACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.
    SignaLinki P14314.

    Miscellaneous databases

    ChiTaRSi PRKCSH. human.
    GeneWikii PRKCSH.
    GenomeRNAii 5589.
    NextBioi 21678.
    PMAP-CutDB P14314.
    PROi P14314.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14314.
    Bgeei P14314.
    CleanExi HS_PRKCSH.
    Genevestigatori P14314.

    Family and domain databases

    Gene3Di 2.70.130.10. 1 hit.
    4.10.400.10. 2 hits.
    InterProi IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR026874. Glucosidase_2_bsu.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR009011. Man6P_isomerase_rcpt-bd_dom.
    IPR028146. PRKCSH_N.
    [Graphical view ]
    PANTHERi PTHR12630:SF1. PTHR12630:SF1. 1 hit.
    Pfami PF13202. EF-hand_5. 2 hits.
    PF12999. PRKCSH-like. 1 hit.
    [Graphical view ]
    SMARTi SM00192. LDLa. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50911. SSF50911. 1 hit.
    SSF57424. SSF57424. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80K protein."
      Sakai K., Masamichi H., Minoshima S., Kudoh J., Fukuyama R., Shimizu N.
      Genomics 5:309-315(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "A 3-Mb region for the familial hemiplegic migraine locus on 19p13.1-p13.2: exclusion of PRKCSH as a candidate gene."
      Ophoff R.A., Terwindt G.M., Vergouwe M.N., van Eijk R., Mohrenweiser H., Litt M., Hofker M.H., Haan J., Ferrari M.D., Frants R.R.
      Eur. J. Hum. Genet. 4:321-328(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo."
      Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C., Chevet E., Menard R., Bergeron J.J.M., Thomas D.Y.
      Glycobiology 10:815-827(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GANAB, SUBCELLULAR LOCATION.
      Tissue: Lymphocyte.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-528 (ISOFORM 1), VARIANT THR-291.
    5. "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 2).
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [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] OF 22-528 (ISOFORM 2), VARIANT THR-291.
      Tissue: Lung.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 15-21.
      Tissue: Platelet.
    9. "Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease."
      Li A., Davila S., Furu L., Qian Q., Tian X., Kamath P.S., King B.F., Torres V.E., Somlo S.
      Am. J. Hum. Genet. 72:691-703(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PCLD.
    10. "Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease."
      Drenth J.P.H., te Morsche R.H.M., Smink R., Bonifacino J.S., Jansen J.B.M.J.
      Nat. Genet. 33:345-347(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PCLD.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGLU2B_HUMAN
    AccessioniPrimary (citable) accession number: P14314
    Secondary accession number(s): A8K318
    , Q96BU9, Q96D06, Q9P0W9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 161 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3