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P05060

- SCG1_HUMAN

UniProt

P05060 - SCG1_HUMAN

Protein

Secretogranin-1

Gene

CHGB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.

    GO - Molecular functioni

    1. hormone activity Source: ProtInc
    2. protein binding Source: IntAct

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Secretogranin-1
    Alternative name(s):
    Chromogranin-B
    Short name:
    CgB
    Secretogranin I
    Short name:
    SgI
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CHGB
    Synonyms:SCG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:1930. CHGB.

    Subcellular locationi

    Secreted
    Note: Neuroendocrine and endocrine secretory granules.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. secretory granule Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26462.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20202 PublicationsAdd
    BLAST
    Chaini21 – 677657Secretogranin-1PRO_0000005438Add
    BLAST
    Peptidei440 – 51374GAWK peptidePRO_0000005439Add
    BLAST
    Peptidei617 – 67357CCB peptidePRO_0000005440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi36 ↔ 57
    Modified residuei79 – 791PhosphothreonineCurated
    Modified residuei99 – 991PhosphoserineSequence Analysis
    Modified residuei100 – 1001PhosphoserineSequence Analysis
    Modified residuei149 – 1491Phosphoserine2 Publications
    Modified residuei183 – 1831PhosphoserineBy similarity
    Modified residuei259 – 2591Phosphoserine1 Publication
    Modified residuei263 – 2631Phosphoserine1 Publication
    Modified residuei293 – 2931PhosphoserineSequence Analysis
    Modified residuei294 – 2941PhosphoserineSequence Analysis
    Modified residuei311 – 3111Phosphoserine1 Publication
    Modified residuei335 – 3351Phosphoserine1 Publication
    Modified residuei341 – 3411SulfotyrosineBy similarity
    Modified residuei377 – 3771PhosphoserineBy similarity
    Modified residuei380 – 3801Phosphoserine
    Modified residuei405 – 4051Phosphoserine2 Publications
    Modified residuei471 – 4711SulfotyrosineSequence Analysis
    Modified residuei474 – 4741SulfotyrosineCurated
    Modified residuei533 – 5331PhosphoserineSequence Analysis
    Modified residuei534 – 5341PhosphoserineSequence Analysis
    Modified residuei566 – 5661SulfotyrosineCurated
    Modified residuei568 – 5681SulfotyrosineSequence Analysis
    Modified residuei617 – 6171Phosphoserine1 Publication
    Modified residuei624 – 6241SulfotyrosineBy similarity
    Modified residuei626 – 6261PhosphoserineBy similarity
    Modified residuei631 – 6311PhosphoserineBy similarity

    Post-translational modificationi

    Extensively processed by limited proteolysis at conserved basic residues. Alternative processing are seen in different tissues By similarity.By similarity
    O-glycosylated.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    PaxDbiP05060.
    PeptideAtlasiP05060.
    PRIDEiP05060.

    PTM databases

    PhosphoSiteiP05060.

    Expressioni

    Tissue specificityi

    Expressed in the adrenal medulla, and in pheochromocytoma. Not expressed in liver.1 Publication

    Gene expression databases

    BgeeiP05060.
    CleanExiHS_CHGB.
    GenevestigatoriP05060.

    Organism-specific databases

    HPAiCAB009403.
    HPA008759.
    HPA012602.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-712619,EBI-5323863
    SMAD2Q157962EBI-712619,EBI-1040141

    Protein-protein interaction databases

    BioGridi107539. 29 interactions.
    IntActiP05060. 33 interactions.
    MINTiMINT-1414600.
    STRINGi9606.ENSP00000368244.

    Structurei

    3D structure databases

    ProteinModelPortaliP05060.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni116 – 1205O-glycosylated at one site

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi163 – 1719Poly-Glu

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG39839.
    HOVERGENiHBG057317.
    InParanoidiP05060.
    OMAiKKSAEFP.
    OrthoDBiEOG74N5GF.
    PhylomeDBiP05060.
    TreeFamiTF336596.

    Family and domain databases

    InterProiIPR001819. Chromogranin_AB.
    IPR018054. Chromogranin_CS.
    IPR001990. Granin.
    [Graphical view]
    PANTHERiPTHR10583. PTHR10583. 1 hit.
    PfamiPF01271. Granin. 1 hit.
    [Graphical view]
    PRINTSiPR00659. CHROMOGRANIN.
    PROSITEiPS00422. GRANINS_1. 1 hit.
    PS00423. GRANINS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P05060-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPTLLLSLL GAVGLAAVNS MPVDNRNHNE GMVTRCIIEV LSNALSKSSA    50
    PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS 100
    RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE 150
    EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN 200
    ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EETGSQENHP 250
    QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP 300
    SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG 350
    VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG 400
    YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE 450
    NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR 500
    FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE 550
    EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ 600
    YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE 650
    DEKKELENLA AMDLELQKIA EKFSQRG 677
    Length:677
    Mass (Da):78,276
    Last modified:November 2, 2010 - v2
    Checksum:iBFDC97F7B21245B3
    GO

    Sequence cautioni

    The sequence BAD92949.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241D → E in BAF82075. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti93 – 931S → T.2 Publications
    Corresponds to variant rs6085324 [ dbSNP | Ensembl ].
    VAR_043578
    Natural varianti117 – 1171K → N.
    Corresponds to variant rs236150 [ dbSNP | Ensembl ].
    VAR_024414
    Natural varianti145 – 1451D → N.
    Corresponds to variant rs6133278 [ dbSNP | Ensembl ].
    VAR_028235
    Natural varianti178 – 1781R → Q.2 Publications
    Corresponds to variant rs910122 [ dbSNP | Ensembl ].
    VAR_020287
    Natural varianti200 – 2001N → H.
    Corresponds to variant rs881118 [ dbSNP | Ensembl ].
    VAR_028236
    Natural varianti232 – 2321R → Q.
    Corresponds to variant rs6139873 [ dbSNP | Ensembl ].
    VAR_028237
    Natural varianti243 – 2431T → A.6 Publications
    Corresponds to variant rs236151 [ dbSNP | Ensembl ].
    VAR_024415
    Natural varianti353 – 3531A → G.2 Publications
    Corresponds to variant rs236152 [ dbSNP | Ensembl ].
    VAR_024416
    Natural varianti413 – 4131P → L.
    Corresponds to variant rs742710 [ dbSNP | Ensembl ].
    VAR_028238
    Natural varianti417 – 4171R → H.2 Publications
    Corresponds to variant rs742711 [ dbSNP | Ensembl ].
    VAR_022012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00064 mRNA. Translation: CAA68271.1.
    AK289386 mRNA. Translation: BAF82075.1.
    CR456726 mRNA. Translation: CAG33007.1.
    AB209712 mRNA. Translation: BAD92949.1. Different initiation.
    AL035461 Genomic DNA. Translation: CAB55272.1.
    AL035461 Genomic DNA. Translation: CAC34360.1.
    CH471133 Genomic DNA. Translation: EAX10410.1.
    BC000375 mRNA. Translation: AAH00375.1.
    CCDSiCCDS13092.1.
    PIRiA29264. CNHUB.
    RefSeqiNP_001810.2. NM_001819.2.
    UniGeneiHs.516874.

    Genome annotation databases

    EnsembliENST00000378961; ENSP00000368244; ENSG00000089199.
    GeneIDi1114.
    KEGGihsa:1114.
    UCSCiuc002wmg.3. human.

    Polymorphism databases

    DMDMi311033509.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00064 mRNA. Translation: CAA68271.1 .
    AK289386 mRNA. Translation: BAF82075.1 .
    CR456726 mRNA. Translation: CAG33007.1 .
    AB209712 mRNA. Translation: BAD92949.1 . Different initiation.
    AL035461 Genomic DNA. Translation: CAB55272.1 .
    AL035461 Genomic DNA. Translation: CAC34360.1 .
    CH471133 Genomic DNA. Translation: EAX10410.1 .
    BC000375 mRNA. Translation: AAH00375.1 .
    CCDSi CCDS13092.1.
    PIRi A29264. CNHUB.
    RefSeqi NP_001810.2. NM_001819.2.
    UniGenei Hs.516874.

    3D structure databases

    ProteinModelPortali P05060.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107539. 29 interactions.
    IntActi P05060. 33 interactions.
    MINTi MINT-1414600.
    STRINGi 9606.ENSP00000368244.

    PTM databases

    PhosphoSitei P05060.

    Polymorphism databases

    DMDMi 311033509.

    Proteomic databases

    PaxDbi P05060.
    PeptideAtlasi P05060.
    PRIDEi P05060.

    Protocols and materials databases

    DNASUi 1114.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378961 ; ENSP00000368244 ; ENSG00000089199 .
    GeneIDi 1114.
    KEGGi hsa:1114.
    UCSCi uc002wmg.3. human.

    Organism-specific databases

    CTDi 1114.
    GeneCardsi GC20P005891.
    H-InvDB HIX0015625.
    HGNCi HGNC:1930. CHGB.
    HPAi CAB009403.
    HPA008759.
    HPA012602.
    MIMi 118920. gene.
    neXtProti NX_P05060.
    PharmGKBi PA26462.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39839.
    HOVERGENi HBG057317.
    InParanoidi P05060.
    OMAi KKSAEFP.
    OrthoDBi EOG74N5GF.
    PhylomeDBi P05060.
    TreeFami TF336596.

    Miscellaneous databases

    ChiTaRSi CHGB. human.
    GeneWikii Secretoneurin.
    GenomeRNAii 1114.
    NextBioi 4622.
    PROi P05060.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05060.
    CleanExi HS_CHGB.
    Genevestigatori P05060.

    Family and domain databases

    InterProi IPR001819. Chromogranin_AB.
    IPR018054. Chromogranin_CS.
    IPR001990. Granin.
    [Graphical view ]
    PANTHERi PTHR10583. PTHR10583. 1 hit.
    Pfami PF01271. Granin. 1 hit.
    [Graphical view ]
    PRINTSi PR00659. CHROMOGRANIN.
    PROSITEi PS00422. GRANINS_1. 1 hit.
    PS00423. GRANINS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region."
      Benedum U.M., Lamouroux A., Konecki D.S., Hille A., Baeuerle P.A., Frank R., Lottspeich F., Mallet J., Huttner W.B.
      EMBO J. 6:1203-1211(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-34; 85-93; 334-340 AND 347-355, TISSUE SPECIFICITY, VARIANT ALA-243.
      Tissue: Adrenal medulla.
    2. "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], VARIANTS THR-93; GLN-178; ALA-243; GLY-353 AND HIS-417.
      Tissue: Adrenal gland.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-243.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-93; GLN-178; ALA-243; GLY-353 AND HIS-417.
      Tissue: Brain.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-243.
    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], VARIANT ALA-243.
      Tissue: Lung.
    8. "Chromogranin B: isolation from pheochromocytoma, N-terminal sequence, tissue distribution and secretory vesicle processing."
      Gill B.M., Barbosa J.A., Dinh T.Q., Garrod S., O'Connor D.T.
      Regul. Pept. 33:223-235(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-48.
    9. "Identification of a new chromogranin B fragment (314-365) in endocrine tumors."
      Woussen-Colle M.-C., Gourlet P., Vandermeers A., Vandermeers-Piret M.-C., D'Haens J., Velkeniers B., Robberecht P.
      Peptides 16:231-236(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 334-385.
    10. "GAWK, a novel human pituitary polypeptide: isolation, immunocytochemical localization and complete amino acid sequence."
      Benjannet S., Leduc R., Lazure C., Seidah N.G., Marcinkiewicz M., Chretien M.
      Biochem. Biophys. Res. Commun. 126:602-609(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 440-513.
      Tissue: Pituitary.
    11. "Chromogranin B (secretogranin I), a putative precursor of two novel pituitary peptides through processing at paired basic residues."
      Benjannet S., Leduc R., Adrouche N., Falgueyret J.P., Marcinkiewicz M., Seidah N.G., Mbikay M., Lazure C., Chretien M.
      FEBS Lett. 224:142-148(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 617-673.
      Tissue: Pituitary.
    12. "Identification and characterization of phosphorylated proteins in the human pituitary."
      Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
      Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-149 AND SER-405.
      Tissue: Pituitary.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-259; SER-263; SER-311; SER-335; SER-405 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    14. "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, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSCG1_HUMAN
    AccessioniPrimary (citable) accession number: P05060
    Secondary accession number(s): A8K021
    , Q59EU9, Q6IBS6, Q9BQV6, Q9UC25, Q9UJA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 152 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 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3