P10645 (CMGA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromogranin-A
Short name=CgA

Alternative name(s):
Pituitary secretory protein I
Short name=SP-I

Cleaved into the following 13 chains:

1. Vasostatin-1
   Alternative name(s):
   Vasostatin I
2. Vasostatin-2
   Alternative name(s):
   Vasostatin II
3. EA-92
4. ES-43
5. Pancreastatin
6. SS-18
7. WA-8
8. WE-14
9. LF-19
10. AL-11
11. GV-19
12. GR-44
13. ER-37

Gene names

Name:

CHGA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Pancreastatin strongly inhibits glucose induced insulin release from the pancreas.
Subunit structure	Interacts with SCG3 By similarity.
Subcellular location	Cytoplasmic vesicle › secretory vesicle lumen By similarity. Cytoplasmic vesicle › secretory 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.
Post-translational modification	Sulfated on tyrosine residues and/or contains sulfated glycans. O-glycosylated with core 1 or possibly core 8 glycans. Ref.16 Ref.20
Miscellaneous	Binds calcium with a low-affinity.
Sequence similarities	Belongs to the chromogranin/secretogranin protein family.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium
PTM	Amidation Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Sulfation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of blood pressure Traceable author statement PubMed 8406464. Source: ProtInc
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule Inferred from electronic annotation. Source: InterPro transport vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.11

Chain

19 – 457

439

Chromogranin-A

PRO_0000005408

Peptide

19 – 131

113

Vasostatin-2

PRO_0000005409

Peptide

19 – 94

76

Vasostatin-1

PRO_0000005410

Peptide

134 – 225

92

EA-92

PRO_0000005411

Peptide

228 – 260

33

ES-43

PRO_0000005412

Peptide

272 – 319

48

Pancreastatin

PRO_0000005413

Peptide

322 – 339

18

SS-18

PRO_0000005414

Peptide

342 – 355

14

WE-14 Ref.14

PRO_0000005415

Peptide

342 – 349

8

WA-8

PRO_0000005416

Peptide

358 – 376

19

LF-19

PRO_0000005417

Peptide

380 – 390

11

AL-11

PRO_0000005418

Peptide

393 – 411

19

GV-19

PRO_0000005419

Peptide

413 – 456

44

GR-44

PRO_0000005420

Peptide

420 – 456

37

ER-37

PRO_0000005421

Regions

Region

41 – 59

19

O-glycosylated at one site only in cerebrospinal fluid

Region

181 – 191

11

O-glycosylated at one site only in cerebrospinal fluid

Amino acid modifications

Modified residue

142

1

Phosphoserine By similarity

Modified residue

194

1

Phosphotyrosine By similarity

Modified residue

203

1

Phosphoserine Ref.18

Modified residue

218

1

Phosphoserine Ref.16

Modified residue

270

1

Phosphoserine Ref.16

Modified residue

300

1

Phosphoserine Ref.18

Modified residue

319

1

Glycine amide Ref.13

Modified residue

322

1

Phosphoserine Ref.17 Ref.18

Modified residue

333

1

Phosphoserine Ref.16

Modified residue

398

1

Phosphoserine By similarity

Modified residue

402

1

Phosphoserine Ref.18

Modified residue

456

1

Arginine amide

Glycosylation

181

1

O-linked (GalNAc...) Ref.16

CAR_000116

Glycosylation

183

1

O-linked (GalNAc...) Ref.16

CAR_000117

Glycosylation

251

1

O-linked (GalNAc...) Ref.16

CAR_000118

Disulfide bond

35 ↔ 56

Ref.1

Natural variations

Natural variant

61

1

R → Q.
Corresponds to variant rs3742712 [ dbSNP | Ensembl ].

VAR_047417

Natural variant

176

1

E → K.
Corresponds to variant rs9658654 [ dbSNP | Ensembl ].

VAR_025636

Natural variant

264

1

E → D. Ref.7
Corresponds to variant rs9658655 [ dbSNP | Ensembl ].

VAR_025637

Natural variant

271

1

R → W.
Corresponds to variant rs9658662 [ dbSNP | Ensembl ].

VAR_025638

Natural variant

274

1

A → G.
Corresponds to variant rs9658663 [ dbSNP | Ensembl ].

VAR_025639

Natural variant

315

1

G → S.
Corresponds to variant rs9658664 [ dbSNP | Ensembl ].

VAR_025640

Natural variant

332

1

L → P.
Corresponds to variant rs9658665 [ dbSNP | Ensembl ].

VAR_025641

Natural variant

369

1

D → N.
Corresponds to variant rs2228575 [ dbSNP | Ensembl ].

VAR_025642

Natural variant

382

1

G → S Reduces activity 4.7 fold. Ref.22
Corresponds to variant rs9658667 [ dbSNP | Ensembl ].

VAR_025643

Natural variant

388

1

P → L Increases activity 2.3 fold. Ref.22
Corresponds to variant rs9658668 [ dbSNP | Ensembl ].

VAR_025644

Natural variant

399

1

R → W. Ref.1 Ref.3 Ref.6
Corresponds to variant rs729940 [ dbSNP | Ensembl ].

VAR_025645

Experimental info

Sequence conflict

41

1

S → Y in AAA52018. Ref.1

Sequence conflict

54

1

Q → K in AAA52018. Ref.1

Sequence conflict

87

1

A → R in AAA52018. Ref.1

Sequence conflict

119

1

E → Q in AAA52018. Ref.1

Sequence conflict

167

1

N → K in AAA52018. Ref.1

Sequence conflict

200

1

E → K in AAA52018. Ref.1

Sequence conflict

219

1

A → V in AAA52018. Ref.1

Sequence conflict

339 – 340

2

SK → TN in AAA52018. Ref.1

Sequence conflict

370

1

S → R in AAA52018. Ref.1

Sequence conflict

373

1

K → R in AAA52018. Ref.1

Sequence conflict

380

1

A → G in AAA52018. Ref.1

Sequence conflict

394

1

W → S in AAA52018. Ref.1

Sequence conflict

397

1

S → N in AAA52018. Ref.1

Sequence conflict

416

1

E → Q in AAA52018. Ref.1

Secondary structure

1

.

.

.

.

.

457

Helix Strand Turn

Details...

Beta strand

380 – 383

4

Beta strand

385 – 387

3

Sequences

	Sequence		Length	Mass (Da)
	P10645 [UniParc]. Last modified November 25, 2008. Version 7. Checksum: 2F634E1A83FF0BB1	FASTA	457	50,688
	10 20 30 40 50 60 MRSAAVLALL LCAGQVTALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM PVSQECFETL 70 80 90 100 110 120 RGDERILSIL RHQNLLKELQ DLALQGAKER AHQQKKHSGF EDELSEVLEN QSSQAELKEA 130 140 150 160 170 180 VEEPSSKDVM EKREDSKEAE KSGEATDGAR PQALPEPMQE SKAEGNNQAP GEEEEEEEEA 190 200 210 220 230 240 TNTHPPASLP SQKYPGPQAE GDSEGLSQGL VDREKGLSAE PGWQAKREEE EEEEEEAEAG 250 260 270 280 290 300 EEAVPEEEGP TVVLNPHPSL GYKEIRKGES RSEALAVDGA GKPGAEEAQD PEGKGEQEHS 310 320 330 340 350 360 QQKEEEEEMA VVPQGLFRGG KSGELEQEEE RLSKEWEDSK RWSKMDQLAK ELTAEKRLEG 370 380 390 400 410 420 QEEEEDNRDS SMKLSFRARA YGFRGPGPQL RRGWRPSSRE DSLEAGLPLQ VRGYPEEKKE 430 440 450 EEGSANRRPE DQELESLSAI EAELEKVAHQ LQALRRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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. 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. 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.
[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]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-300; SER-322 AND SER-402, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00290315.

PIR

A28468. A54376.

RefSeq

NP_001266.1. NM_001275.3.

UniGene

Hs.150793.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LV4	NMR	-	A	370-390	[»]

ProteinModelPortal

P10645.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000216492.

PTM databases

GlycoSuiteDB

P10645.

PhosphoSite

P10645.

Polymorphism databases

DMDM

215274270.

Proteomic databases

PaxDb

P10645.

PRIDE

P10645.

Protocols and materials databases

DNASU

1113.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216492; ENSP00000216492; ENSG00000100604.

GeneID

1113.

KEGG

hsa:1113.

UCSC

uc001ybc.4. human.

Organism-specific databases

CTD

1113.

GeneCards

GC14P093389.

HGNC

HGNC:1929. CHGA.

HPA

CAB040544.
CAB055506.
HPA017369.

MIM

118910. gene.

neXtProt

NX_P10645.

PharmGKB

PA26461.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41926.

HOVERGEN

HBG001272.

InParanoid

P10645.

OMA

PVNSPMN.

PhylomeDB

P10645.

Gene expression databases

ArrayExpress

P10645.

Bgee

P10645.

CleanEx

HS_CHGA.

Genevestigator

P10645.

GermOnline

ENSG00000100604. Homo sapiens.

Family and domain databases

InterPro

IPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]

PANTHER

PTHR10583. PTHR10583. 1 hit.

Pfam

PF01271. Granin. 2 hits.
[Graphical view]

PRINTS

PR00659. CHROMOGRANIN.

PROSITE

PS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CHGA. human.

EvolutionaryTrace

P10645.

GenomeRNAi

1113.

NextBio

4618.

PMAP-CutDB

Q6NR84.

SOURCE

Search...

Entry information

Entry name

CMGA_HUMAN

Accession

Primary (citable) accession number: P10645
Secondary accession number(s): B2R9E9 , Q53FA8, Q6NR84, Q96E84, Q96GL7, Q9BQB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 149 of the entry and version 7 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.