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P10645

- CMGA_HUMAN

UniProt

P10645 - CMGA_HUMAN

Protein

Chromogranin-A

Gene

CHGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 7 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Pancreastatin strongly inhibits glucose induced insulin release from the pancreas.

    GO - Biological processi

    1. regulation of blood pressure Source: ProtInc

    Keywords - Ligandi

    Calcium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromogranin-A
    Short name:
    CgA
    Alternative name(s):
    Pituitary secretory protein I
    Short name:
    SP-I
    Cleaved into the following 13 chains:
    Alternative name(s):
    Vasostatin I
    Alternative name(s):
    Vasostatin II
    Gene namesi
    Name:CHGA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:1929. CHGA.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle lumen By similarity. Cytoplasmic vesiclesecretory vesicle membrane By similarity. Secreted
    Note: Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions.By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. perinuclear region of cytoplasm Source: UniProt
    3. secretory granule Source: InterPro
    4. transport vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26461.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 457439Chromogranin-APRO_0000005408Add
    BLAST
    Peptidei19 – 131113Vasostatin-21 PublicationPRO_0000005409Add
    BLAST
    Peptidei19 – 9476Vasostatin-11 PublicationPRO_0000005410Add
    BLAST
    Peptidei134 – 22592EA-921 PublicationPRO_0000005411Add
    BLAST
    Peptidei228 – 26033ES-431 PublicationPRO_0000005412Add
    BLAST
    Peptidei272 – 31948Pancreastatin1 PublicationPRO_0000005413Add
    BLAST
    Peptidei322 – 33918SS-181 PublicationPRO_0000005414Add
    BLAST
    Peptidei342 – 35514WE-141 PublicationPRO_0000005415Add
    BLAST
    Peptidei342 – 3498WA-81 PublicationPRO_0000005416
    Peptidei358 – 37619LF-191 PublicationPRO_0000005417Add
    BLAST
    Peptidei380 – 39011AL-111 PublicationPRO_0000005418Add
    BLAST
    Peptidei393 – 41119GV-191 PublicationPRO_0000005419Add
    BLAST
    Peptidei413 – 45644GR-441 PublicationPRO_0000005420Add
    BLAST
    Peptidei420 – 45637ER-371 PublicationPRO_0000005421Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 561 Publication
    Modified residuei142 – 1421PhosphoserineBy similarity
    Glycosylationi181 – 1811O-linked (GalNAc...)1 PublicationCAR_000116
    Glycosylationi183 – 1831O-linked (GalNAc...)1 PublicationCAR_000117
    Modified residuei194 – 1941PhosphotyrosineBy similarity
    Modified residuei203 – 2031Phosphoserine1 Publication
    Modified residuei218 – 2181Phosphoserine1 Publication
    Glycosylationi251 – 2511O-linked (GalNAc...)1 PublicationCAR_000118
    Modified residuei270 – 2701Phosphoserine1 Publication
    Modified residuei300 – 3001Phosphoserine1 Publication
    Modified residuei319 – 3191Glycine amide2 Publications
    Modified residuei322 – 3221Phosphoserine2 Publications
    Modified residuei333 – 3331Phosphoserine1 Publication
    Modified residuei398 – 3981PhosphoserineBy similarity
    Modified residuei402 – 4021Phosphoserine1 Publication
    Modified residuei456 – 4561Arginine amide1 Publication

    Post-translational modificationi

    Sulfated on tyrosine residues and/or contains sulfated glycans.
    O-glycosylated with core 1 or possibly core 8 glycans.3 Publications

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP10645.
    PRIDEiP10645.

    PTM databases

    PhosphoSiteiP10645.
    UniCarbKBiP10645.

    Miscellaneous databases

    PMAP-CutDBQ6NR84.

    Expressioni

    Gene expression databases

    ArrayExpressiP10645.
    BgeeiP10645.
    CleanExiHS_CHGA.
    GenevestigatoriP10645.

    Organism-specific databases

    HPAiCAB000023.
    CAB040544.
    CAB055506.
    CAB058688.
    HPA017369.

    Interactioni

    Subunit structurei

    Interacts with SCG3.By similarity

    Protein-protein interaction databases

    BioGridi107538. 6 interactions.
    IntActiP10645. 3 interactions.
    MINTiMINT-4846180.
    STRINGi9606.ENSP00000216492.

    Structurei

    Secondary structure

    1
    457
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi380 – 3834
    Beta strandi385 – 3873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LV4NMR-A370-390[»]
    ProteinModelPortaliP10645.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10645.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 5919O-glycosylated at one site only in cerebrospinal fluidAdd
    BLAST
    Regioni181 – 19111O-glycosylated at one site only in cerebrospinal fluidAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG41926.
    HOVERGENiHBG001272.
    InParanoidiP10645.
    OMAiVNSPMNK.
    OrthoDBiEOG7V766Z.
    PhylomeDBiP10645.
    TreeFamiTF336596.

    Family and domain databases

    InterProiIPR001819. Chromogranin_AB.
    IPR018054. Chromogranin_CS.
    IPR001990. Granin.
    [Graphical view]
    PANTHERiPTHR10583. PTHR10583. 1 hit.
    PfamiPF01271. Granin. 2 hits.
    [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.

    P10645-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSAAVLALL LCAGQVTALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM    50
    PVSQECFETL RGDERILSIL RHQNLLKELQ DLALQGAKER AHQQKKHSGF 100
    EDELSEVLEN QSSQAELKEA VEEPSSKDVM EKREDSKEAE KSGEATDGAR 150
    PQALPEPMQE SKAEGNNQAP GEEEEEEEEA TNTHPPASLP SQKYPGPQAE 200
    GDSEGLSQGL VDREKGLSAE PGWQAKREEE EEEEEEAEAG EEAVPEEEGP 250
    TVVLNPHPSL GYKEIRKGES RSEALAVDGA GKPGAEEAQD PEGKGEQEHS 300
    QQKEEEEEMA VVPQGLFRGG KSGELEQEEE RLSKEWEDSK RWSKMDQLAK 350
    ELTAEKRLEG QEEEEDNRDS SMKLSFRARA YGFRGPGPQL RRGWRPSSRE 400
    DSLEAGLPLQ VRGYPEEKKE EEGSANRRPE DQELESLSAI EAELEKVAHQ 450
    LQALRRG 457
    Length:457
    Mass (Da):50,688
    Last modified:November 25, 2008 - v7
    Checksum:i2F634E1A83FF0BB1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411S → Y in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti54 – 541Q → K in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti87 – 871A → R in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti119 – 1191E → Q in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti167 – 1671N → K in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti200 – 2001E → K in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti219 – 2191A → V in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti339 – 3402SK → TN in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti370 – 3701S → R in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti373 – 3731K → R in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti380 – 3801A → G in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti394 – 3941W → S in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti397 – 3971S → N in AAA52018. (PubMed:2445752)Curated
    Sequence conflicti416 – 4161E → Q in AAA52018. (PubMed:2445752)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611R → Q.
    Corresponds to variant rs3742712 [ dbSNP | Ensembl ].
    VAR_047417
    Natural varianti176 – 1761E → K.
    Corresponds to variant rs9658654 [ dbSNP | Ensembl ].
    VAR_025636
    Natural varianti264 – 2641E → D.1 Publication
    Corresponds to variant rs9658655 [ dbSNP | Ensembl ].
    VAR_025637
    Natural varianti271 – 2711R → W.
    Corresponds to variant rs9658662 [ dbSNP | Ensembl ].
    VAR_025638
    Natural varianti274 – 2741A → G.
    Corresponds to variant rs9658663 [ dbSNP | Ensembl ].
    VAR_025639
    Natural varianti315 – 3151G → S.
    Corresponds to variant rs9658664 [ dbSNP | Ensembl ].
    VAR_025640
    Natural varianti332 – 3321L → P.
    Corresponds to variant rs9658665 [ dbSNP | Ensembl ].
    VAR_025641
    Natural varianti369 – 3691D → N.
    Corresponds to variant rs2228575 [ dbSNP | Ensembl ].
    VAR_025642
    Natural varianti382 – 3821G → S Reduces activity 4.7 fold. 1 Publication
    Corresponds to variant rs9658667 [ dbSNP | Ensembl ].
    VAR_025643
    Natural varianti388 – 3881P → L Increases activity 2.3 fold. 1 Publication
    Corresponds to variant rs9658668 [ dbSNP | Ensembl ].
    VAR_025644
    Natural varianti399 – 3991R → W.3 Publications
    Corresponds to variant rs729940 [ dbSNP | Ensembl ].
    VAR_025645

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03483 mRNA. Translation: AAA52017.1.
    J03915 mRNA. Translation: AAA52018.1.
    U03749
    , U03742, U03743, U03744, U03748, U03745, U03746, U03747 Genomic DNA. Translation: AAB53685.1.
    BT006869 mRNA. Translation: AAP35515.1.
    AK223381 mRNA. Translation: BAD97101.1.
    AL117192 Genomic DNA. No translation available.
    AK313757 mRNA. Translation: BAG36496.1.
    CH471061 Genomic DNA. Translation: EAW81505.1.
    BC001059 mRNA. Translation: AAH01059.1.
    BC006459 mRNA. Translation: AAH06459.1.
    BC009384 mRNA. Translation: AAH09384.2.
    BC012755 mRNA. Translation: AAH12755.2.
    CCDSiCCDS9906.1.
    PIRiA54376. A28468.
    RefSeqiNP_001266.1. NM_001275.3.
    UniGeneiHs.150793.

    Genome annotation databases

    EnsembliENST00000216492; ENSP00000216492; ENSG00000100604.
    GeneIDi1113.
    KEGGihsa:1113.
    UCSCiuc001ybc.4. human.

    Polymorphism databases

    DMDMi215274270.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03483 mRNA. Translation: AAA52017.1 .
    J03915 mRNA. Translation: AAA52018.1 .
    U03749
    , U03742 , U03743 , U03744 , U03748 , U03745 , U03746 , U03747 Genomic DNA. Translation: AAB53685.1 .
    BT006869 mRNA. Translation: AAP35515.1 .
    AK223381 mRNA. Translation: BAD97101.1 .
    AL117192 Genomic DNA. No translation available.
    AK313757 mRNA. Translation: BAG36496.1 .
    CH471061 Genomic DNA. Translation: EAW81505.1 .
    BC001059 mRNA. Translation: AAH01059.1 .
    BC006459 mRNA. Translation: AAH06459.1 .
    BC009384 mRNA. Translation: AAH09384.2 .
    BC012755 mRNA. Translation: AAH12755.2 .
    CCDSi CCDS9906.1.
    PIRi A54376. A28468.
    RefSeqi NP_001266.1. NM_001275.3.
    UniGenei Hs.150793.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LV4 NMR - A 370-390 [» ]
    ProteinModelPortali P10645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107538. 6 interactions.
    IntActi P10645. 3 interactions.
    MINTi MINT-4846180.
    STRINGi 9606.ENSP00000216492.

    PTM databases

    PhosphoSitei P10645.
    UniCarbKBi P10645.

    Polymorphism databases

    DMDMi 215274270.

    Proteomic databases

    PaxDbi P10645.
    PRIDEi P10645.

    Protocols and materials databases

    DNASUi 1113.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216492 ; ENSP00000216492 ; ENSG00000100604 .
    GeneIDi 1113.
    KEGGi hsa:1113.
    UCSCi uc001ybc.4. human.

    Organism-specific databases

    CTDi 1113.
    GeneCardsi GC14P093389.
    HGNCi HGNC:1929. CHGA.
    HPAi CAB000023.
    CAB040544.
    CAB055506.
    CAB058688.
    HPA017369.
    MIMi 118910. gene.
    neXtProti NX_P10645.
    PharmGKBi PA26461.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41926.
    HOVERGENi HBG001272.
    InParanoidi P10645.
    OMAi VNSPMNK.
    OrthoDBi EOG7V766Z.
    PhylomeDBi P10645.
    TreeFami TF336596.

    Miscellaneous databases

    ChiTaRSi CHGA. human.
    EvolutionaryTracei P10645.
    GeneWikii Chromogranin_A.
    GenomeRNAii 1113.
    NextBioi 4618.
    PMAP-CutDB Q6NR84.
    PROi P10645.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10645.
    Bgeei P10645.
    CleanExi HS_CHGA.
    Genevestigatori P10645.

    Family and domain databases

    InterProi IPR001819. Chromogranin_AB.
    IPR018054. Chromogranin_CS.
    IPR001990. Granin.
    [Graphical view ]
    PANTHERi PTHR10583. PTHR10583. 1 hit.
    Pfami PF01271. Granin. 2 hits.
    [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 chromogranin A and pancreastatin."
      Konecki D.S., Benedum U.M., Gerdes H.-H., Huttner W.B.
      J. Biol. Chem. 262:17026-17030(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISULFIDE BOND, VARIANT TRP-399.
    2. "Molecular cloning and primary structure of human chromogranin A (secretory protein I) cDNA."
      Helman L.J., Ahn T.G., Levine M.A., Allison A., Cohen P.S., Cooper M.J., Cohn D.V., Israel M.A.
      J. Biol. Chem. 263:11559-11563(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Human chromogranin A gene. Molecular cloning, structural analysis, and neuroendocrine cell-specific expression."
      Mouland A.J., Bevan S., White J.H., Hendy G.N.
      J. Biol. Chem. 269:6918-6926(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-399.
      Tissue: Liver.
    4. Mouland A.J., Bevan S., White J.H., Hendy G.N.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 384-397.
    5. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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], VARIANT TRP-399.
      Tissue: Stomach.
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-264.
      Tissue: Gastric mucosa.
    8. "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].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
      Tissue: Brain.
    11. "Chromogranin from normal human adrenal glands: purification by monoclonal antibody affinity chromatography and partial N-terminal amino acid sequence."
      Wilson B.S., Phan S.H., Lloyd R.V.
      Regul. Pept. 13:207-223(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-46.
      Tissue: Adrenal gland.
    12. "Isolation and characterization of a tumor-derived human protein related to chromogranin A and its in vitro conversion to human pancreastatin-48."
      Tamamura H., Ohta M., Yoshizawa K., Ono Y., Funakoshi A., Miyasaka K., Tateishi K., Jimi A., Yajima H., Fujii N., Funakoshi S.
      Eur. J. Biochem. 191:33-39(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 134-319, AMIDATION AT GLY-319.
      Tissue: Pancreas.
    13. "Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma."
      Sekiya K., Ghatei M.A., Minamino N., Bretherton-Watt D., Matsuo H., Bloom S.R.
      FEBS Lett. 228:153-156(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 291-319, AMIDATION AT GLY-319.
      Tissue: Pancreas.
    14. "Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour."
      Curry W.J., Shaw C., Johnston C.F., Thim L., Buchanan K.D.
      FEBS Lett. 301:319-321(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 342-355.
    15. "The spectrum of endogenous human chromogranin A-derived peptides identified using a modified proteomic strategy."
      Orr D.F., Chen T., Johnsen A.H., Chalk R., Buchanan K.D., Sloan J.M., Rao P., Shaw C.
      Proteomics 2:1586-1600(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF DERIVED PEPTIDES, AMIDATION AT ARG-456 (PEPTIDE GR-44 AND PEPTIDE ER-37).
    16. "Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors."
      Gadroy P., Stridsberg M., Capon C., Michalski J.-C., Strub J.-M., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.
      J. Biol. Chem. 273:34087-34097(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-181; THR-183 AND THR-251, PHOSPHORYLATION AT SER-218; SER-270 AND SER-333.
    17. "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-322.
      Tissue: Pituitary.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-300; SER-322 AND SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    19. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    20. "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.
    21. "Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A."
      Preece N.E., Nguyen M., Mahata M., Mahata S.K., Mahapatra N.R., Tsigelny I., O'Connor D.T.
      Regul. Pept. 118:75-87(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 370-390.
    22. "Both rare and common polymorphisms contribute functional variation at CHGA, a regulator of catecholamine physiology."
      Wen G., Mahata S.K., Cadman P., Mahata M., Ghosh S., Mahapatra N.R., Rao F., Stridsberg M., Smith D.W., Mahboubi P., Schork N.J., O'Connor D.T., Hamilton B.A.
      Am. J. Hum. Genet. 74:197-207(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SER-382 AND LEU-388.

    Entry informationi

    Entry nameiCMGA_HUMAN
    AccessioniPrimary (citable) accession number: P10645
    Secondary accession number(s): B2R9E9
    , Q53FA8, Q6NR84, Q96E84, Q96GL7, Q9BQB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 159 of the entry and version 7 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

    Miscellaneous

    Binds calcium with a low-affinity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3