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P29120

- NEC1_HUMAN

UniProt

P29120 - NEC1_HUMAN

Protein

Neuroendocrine convertase 1

Gene

PCSK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin and insulin.

    Catalytic activityi

    Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.

    Cofactori

    Calcium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei167 – 1671Charge relay systemBy similarity
    Active sitei208 – 2081Charge relay systemBy similarity
    Active sitei382 – 3821Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: BHF-UCL

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. metabolic process Source: ProtInc
    4. peptide biosynthetic process Source: BHF-UCL
    5. peptide hormone processing Source: Reactome
    6. proteolysis Source: ProtInc
    7. regulation of insulin secretion Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_15452. Peptide hormone biosynthesis.
    REACT_15550. Insulin processing.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    REACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
    SignaLinkiP29120.

    Protein family/group databases

    MEROPSiS08.072.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuroendocrine convertase 1 (EC:3.4.21.93)
    Short name:
    NEC 1
    Alternative name(s):
    Prohormone convertase 1
    Proprotein convertase 1
    Short name:
    PC1
    Gene namesi
    Name:PCSK1
    Synonyms:NEC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:8743. PCSK1.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle
    Note: Localized in the secretion granules.

    GO - Cellular componenti

    1. extracellular space Source: BHF-UCL
    2. Golgi apparatus Source: RefGenome
    3. secretory granule lumen Source: Reactome
    4. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle

    Pathology & Biotechi

    Involvement in diseasei

    Proprotein convertase 1 deficiency (PC1 deficiency) [MIM:600955]: Characterized by obesity, hypogonadism, hypoadrenalism, reactive hypoglycemia as well as marked small-intestinal absorptive dysfunction It is due to impaired processing of prohormones.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131Missing in PC1 deficiency. 1 Publication
    VAR_022777
    Natural varianti307 – 3071S → L in PC1 deficiency; in vitro the mutation markedly impairs the catalytic activity of the enzyme; however intracellular trafficking of this mutant enzyme appears normal; retains some autocatalytic activity even though it is completely inactive on other substrates. 1 Publication
    VAR_055002
    Natural varianti483 – 4831G → R in PC1 deficiency; prevents processing of pro-PCSK1 and leads to its retention in the endoplasmic reticulum. 1 Publication
    VAR_022778

    Keywords - Diseasei

    Disease mutation, Obesity

    Organism-specific databases

    MIMi600955. phenotype.
    612362. phenotype.
    Orphaneti71528. Obesity due to prohormone convertase I deficiency.
    PharmGKBiPA33089.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Propeptidei28 – 11083Sequence AnalysisPRO_0000027057Add
    BLAST
    Chaini111 – 753643Neuroendocrine convertase 1PRO_0000027058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi225 ↔ 374By similarity
    Disulfide bondi317 ↔ 347By similarity
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi467 ↔ 494By similarity
    Glycosylationi632 – 6321O-linked (GalNAc...)1 Publication

    Post-translational modificationi

    O-glycosylated.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP29120.
    PRIDEiP29120.

    PTM databases

    PhosphoSiteiP29120.

    Miscellaneous databases

    PMAP-CutDBP29120.

    Expressioni

    Gene expression databases

    ArrayExpressiP29120.
    BgeeiP29120.
    CleanExiHS_PCSK1.
    GenevestigatoriP29120.

    Organism-specific databases

    HPAiHPA048564.

    Interactioni

    Protein-protein interaction databases

    BioGridi111151. 4 interactions.
    MINTiMINT-6630348.
    STRINGi9606.ENSP00000308024.

    Structurei

    3D structure databases

    ProteinModelPortaliP29120.
    SMRiP29120. Positions 31-103, 123-597, 711-753.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini162 – 451290Peptidase S8Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S8 family. Furin subfamily.Curated
    Contains 1 peptidase S8 domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4935.
    HOGENOMiHOG000192536.
    HOVERGENiHBG008705.
    InParanoidiP29120.
    KOiK01359.
    OMAiNNPGWKK.
    OrthoDBiEOG7BW0JD.
    PhylomeDBiP29120.
    TreeFamiTF314277.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    3.40.50.200. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023827. Peptidase_S8_Asp-AS.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR022005. Proho_convert.
    IPR009020. Prot_inh_propept.
    IPR002884. PrprotnconvertsP.
    [Graphical view]
    PANTHERiPTHR10795. PTHR10795. 1 hit.
    PfamiPF01483. P_proprotein. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    PF12177. Proho_convert. 1 hit.
    [Graphical view]
    PRINTSiPR00723. SUBTILISIN.
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
    PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 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: P29120-1) [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

    MERRAWSLQC TAFVLFCAWC ALNSAKAKRQ FVNEWAAEIP GGPEAASAIA    50
    EELGYDLLGQ IGSLENHYLF KHKNHPRRSR RSAFHITKRL SDDDRVIWAE 100
    QQYEKERSKR SALRDSALNL FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP 150
    VWQKGITGKG VVITVLDDGL EWNHTDIYAN YDPEASYDFN DNDHDPFPRY 200
    DPTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM LDGIVTDAIE 250
    ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG 300
    SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST 350
    LATSYSSGDY TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP 400
    NLTWRDMQHL VVWTSEYDPL ANNPGWKKNG AGLMVNSRFG FGLLNAKALV 450
    DLADPRTWRS VPEKKECVVK DNDFEPRALK ANGEVIIEIP TRACEGQENA 500
    IKSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE RDTSPNGFKN 550
    WDFMSVHTWG ENPIGTWTLR ITDMSGRIQN EGRIVNWKLI LHGTSSQPEH 600
    MKQPRVYTSY NTVQNDRRGV EKMVDPGEEQ PTQENPKENT LVSKSPSSSS 650
    VGGRRDELEE GAPSQAMLRL LQSAFSKNSP PKQSPKKSPS AKLNIPYENF 700
    YEALEKLNKP SQLKDSEDSL YNDYVDVFYN TKPYKHRDDR LLQALVDILN 750
    EEN 753
    Length:753
    Mass (Da):84,152
    Last modified:October 17, 2006 - v2
    Checksum:iD3CBD1B92093A208
    GO
    Isoform 2 (identifier: P29120-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: MERRAWSLQCTAFVLFCAWCALNSAKAKRQFVNEWAAEIPGGPEAASAIAEELGYDLLG → MGKGSISFLFFS

    Note: No experimental confirmation available.

    Show »
    Length:706
    Mass (Da):79,010
    Checksum:iF082971DADE9EAAC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti357 – 3571S → G in CAA46031. (PubMed:1547893)Curated
    Sequence conflicti370 – 3712LH → VD in BAA11133. (PubMed:8666140)Curated
    Sequence conflicti617 – 6171R → G in BAH14073. (PubMed:14702039)Curated

    Polymorphismi

    Genetic variations in PCSK1 define the body mass index quantitative trait locus 12 (BMIQ12) [MIMi:612362]. Variance in body mass index is a susceptibility factor for obesity.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti80 – 801R → Q.1 Publication
    Corresponds to variant rs1799904 [ dbSNP | Ensembl ].
    VAR_013906
    Natural varianti213 – 2131Missing in PC1 deficiency. 1 Publication
    VAR_022777
    Natural varianti221 – 2211N → D Associated with susceptibility to obesity; induces a 10.4% reduction of activity (P = 0.03) when compared to the wild-type enzyme. 2 Publications
    Corresponds to variant rs6232 [ dbSNP | Ensembl ].
    VAR_013907
    Natural varianti307 – 3071S → L in PC1 deficiency; in vitro the mutation markedly impairs the catalytic activity of the enzyme; however intracellular trafficking of this mutant enzyme appears normal; retains some autocatalytic activity even though it is completely inactive on other substrates. 1 Publication
    VAR_055002
    Natural varianti483 – 4831G → R in PC1 deficiency; prevents processing of pro-PCSK1 and leads to its retention in the endoplasmic reticulum. 1 Publication
    VAR_022778
    Natural varianti665 – 6651Q → E.3 Publications
    Corresponds to variant rs6234 [ dbSNP | Ensembl ].
    VAR_013908
    Natural varianti690 – 6901S → T.2 Publications
    Corresponds to variant rs6235 [ dbSNP | Ensembl ].
    VAR_013909

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5959MERRA…YDLLG → MGKGSISFLFFS in isoform 2. 1 PublicationVSP_046100Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64810 mRNA. Translation: CAA46031.1.
    M90753 mRNA. Translation: AAA59918.1.
    D73407 Genomic DNA. Translation: BAA11133.1.
    AK303888 mRNA. Translation: BAH14073.1.
    AC008951 Genomic DNA. No translation available.
    AC108107 Genomic DNA. No translation available.
    U24128 Genomic DNA. Translation: AAA73788.1.
    CCDSiCCDS4081.1. [P29120-1]
    CCDS54881.1. [P29120-2]
    PIRiS21106. KXHUC1.
    RefSeqiNP_000430.3. NM_000439.4. [P29120-1]
    NP_001171346.1. NM_001177875.1. [P29120-2]
    UniGeneiHs.78977.

    Genome annotation databases

    EnsembliENST00000311106; ENSP00000308024; ENSG00000175426. [P29120-1]
    ENST00000508626; ENSP00000421600; ENSG00000175426. [P29120-2]
    GeneIDi5122.
    KEGGihsa:5122.
    UCSCiuc003kls.2. human. [P29120-1]

    Polymorphism databases

    DMDMi116242674.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64810 mRNA. Translation: CAA46031.1 .
    M90753 mRNA. Translation: AAA59918.1 .
    D73407 Genomic DNA. Translation: BAA11133.1 .
    AK303888 mRNA. Translation: BAH14073.1 .
    AC008951 Genomic DNA. No translation available.
    AC108107 Genomic DNA. No translation available.
    U24128 Genomic DNA. Translation: AAA73788.1 .
    CCDSi CCDS4081.1. [P29120-1 ]
    CCDS54881.1. [P29120-2 ]
    PIRi S21106. KXHUC1.
    RefSeqi NP_000430.3. NM_000439.4. [P29120-1 ]
    NP_001171346.1. NM_001177875.1. [P29120-2 ]
    UniGenei Hs.78977.

    3D structure databases

    ProteinModelPortali P29120.
    SMRi P29120. Positions 31-103, 123-597, 711-753.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111151. 4 interactions.
    MINTi MINT-6630348.
    STRINGi 9606.ENSP00000308024.

    Chemistry

    BindingDBi P29120.
    ChEMBLi CHEMBL3182.
    DrugBanki DB00047. Insulin Glargine recombinant.
    DB00046. Insulin Lyspro recombinant.
    DB00030. Insulin recombinant.
    DB00071. Insulin, porcine.

    Protein family/group databases

    MEROPSi S08.072.

    PTM databases

    PhosphoSitei P29120.

    Polymorphism databases

    DMDMi 116242674.

    Proteomic databases

    PaxDbi P29120.
    PRIDEi P29120.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311106 ; ENSP00000308024 ; ENSG00000175426 . [P29120-1 ]
    ENST00000508626 ; ENSP00000421600 ; ENSG00000175426 . [P29120-2 ]
    GeneIDi 5122.
    KEGGi hsa:5122.
    UCSCi uc003kls.2. human. [P29120-1 ]

    Organism-specific databases

    CTDi 5122.
    GeneCardsi GC05M095751.
    HGNCi HGNC:8743. PCSK1.
    HPAi HPA048564.
    MIMi 162150. gene.
    600955. phenotype.
    612362. phenotype.
    neXtProti NX_P29120.
    Orphaneti 71528. Obesity due to prohormone convertase I deficiency.
    PharmGKBi PA33089.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4935.
    HOGENOMi HOG000192536.
    HOVERGENi HBG008705.
    InParanoidi P29120.
    KOi K01359.
    OMAi NNPGWKK.
    OrthoDBi EOG7BW0JD.
    PhylomeDBi P29120.
    TreeFami TF314277.

    Enzyme and pathway databases

    Reactomei REACT_15452. Peptide hormone biosynthesis.
    REACT_15550. Insulin processing.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    REACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
    SignaLinki P29120.

    Miscellaneous databases

    ChiTaRSi PCSK1. human.
    GeneWikii Proprotein_convertase_1.
    GenomeRNAii 5122.
    NextBioi 19750.
    PMAP-CutDB P29120.
    PROi P29120.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29120.
    Bgeei P29120.
    CleanExi HS_PCSK1.
    Genevestigatori P29120.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    3.40.50.200. 1 hit.
    InterProi IPR008979. Galactose-bd-like.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023827. Peptidase_S8_Asp-AS.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR022005. Proho_convert.
    IPR009020. Prot_inh_propept.
    IPR002884. PrprotnconvertsP.
    [Graphical view ]
    PANTHERi PTHR10795. PTHR10795. 1 hit.
    Pfami PF01483. P_proprotein. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    PF12177. Proho_convert. 1 hit.
    [Graphical view ]
    PRINTSi PR00723. SUBTILISIN.
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEi PS00136. SUBTILASE_ASP. 1 hit.
    PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression in human lung tumor cells of the proprotein processing enzyme PC1/PC3. Cloning and primary sequence of a 5 kb cDNA."
      Creemers J.W.M., Roebroek A.J.M., van de Ven W.J.M.
      FEBS Lett. 300:82-88(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The cDNA sequence of the human pro-hormone and pro-protein convertase PC1."
      Seidah N.G., Hamelin J., Gaspar A.M., Day R., Chretien M.
      DNA Cell Biol. 11:283-289(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Human prohormone convertase 3 gene: exon-intron organization and molecular scanning for mutations in Japanese subjects with NIDDM."
      Ohagi S., Sakaguchi H., Sanke T., Tatsuta H., Hanabusa T., Nanjo K.
      Diabetes 45:897-901(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-80 AND GLU-665.
    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] (ISOFORM 2).
      Tissue: Trachea.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Neuroendocrine-specific expression of the human prohormone convertase 1 gene. Hormonal regulation of transcription through distinct cAMP response elements."
      Jansen E.
      J. Biol. Chem. 270:15391-15397(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
    7. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-632, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Obesity and impaired prohormone processing associated with mutations in the human prohormone convertase 1 gene."
      Jackson R.S., Creemers J.W., Ohagi S., Raffin-Sanson M.-L., Sanders L., Montague C.T., Hutton J.C., O'Rahilly S.
      Nat. Genet. 16:303-306(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PC1 DEFICIENCY ARG-483.
    9. Cited for: VARIANTS ASP-221; GLU-665 AND THR-690.
    10. Cited for: VARIANT PC1 DEFICIENCY ALA-213 DEL.
    11. "Hyperphagia and early-onset obesity due to a novel homozygous missense mutation in prohormone convertase 1/3."
      Farooqi I.S., Volders K., Stanhope R., Heuschkel R., White A., Lank E., Keogh J., O'Rahilly S., Creemers J.W.M.
      J. Clin. Endocrinol. Metab. 92:3369-3373(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PC1 DEFICIENCY LEU-307, CHARACTERIZATION OF VARIANT PC1 DEFICIENCY LEU-307, VARIANTS GLU-665 AND THR-690.
    12. Cited for: VARIANT ASP-221, CHARACTERIZATION OF VARIANT ASP-221, ASSOCIATION WITH SUSCEPTIBILITY TO OBESITY.

    Entry informationi

    Entry nameiNEC1_HUMAN
    AccessioniPrimary (citable) accession number: P29120
    Secondary accession number(s): B7Z8T7
    , E9PHA1, P78478, Q92532
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 148 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, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3