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P10645

- CMGA_HUMAN

UniProt

P10645 - CMGA_HUMAN

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Protein

Chromogranin-A

Gene

CHGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Pancreastatin strongly inhibits glucose induced insulin release from the pancreas.

GO - Biological processi

  1. regulation of blood pressure Source: ProtInc
Complete GO annotation...

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-KW
  2. membrane Source: UniProtKB-KW
  3. perinuclear region of cytoplasm Source: UniProt
  4. secretory granule Source: InterPro
Complete GO annotation...

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

BgeeiP10645.
CleanExiHS_CHGA.
ExpressionAtlasiP10645. baseline and differential.
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.
GeneTreeiENSGT00730000111266.
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

        10         20         30         40         50
MRSAAVLALL LCAGQVTALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM
60 70 80 90 100
PVSQECFETL RGDERILSIL RHQNLLKELQ DLALQGAKER AHQQKKHSGF
110 120 130 140 150
EDELSEVLEN QSSQAELKEA VEEPSSKDVM EKREDSKEAE KSGEATDGAR
160 170 180 190 200
PQALPEPMQE SKAEGNNQAP GEEEEEEEEA TNTHPPASLP SQKYPGPQAE
210 220 230 240 250
GDSEGLSQGL VDREKGLSAE PGWQAKREEE EEEEEEAEAG EEAVPEEEGP
260 270 280 290 300
TVVLNPHPSL GYKEIRKGES RSEALAVDGA GKPGAEEAQD PEGKGEQEHS
310 320 330 340 350
QQKEEEEEMA VVPQGLFRGG KSGELEQEEE RLSKEWEDSK RWSKMDQLAK
360 370 380 390 400
ELTAEKRLEG QEEEEDNRDS SMKLSFRARA YGFRGPGPQL RRGWRPSSRE
410 420 430 440 450
DSLEAGLPLQ VRGYPEEKKE EEGSANRRPE DQELESLSAI EAELEKVAHQ

LQALRRG
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.
GeneTreei ENSGT00730000111266.
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

Bgeei P10645.
CleanExi HS_CHGA.
ExpressionAtlasi P10645. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 160 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