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Protein

Secretogranin-1

Gene

CHGB

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

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
Complete GO annotation...

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 3 chains:
Gene namesi
Name:CHGB
Synonyms:SCG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: 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: InterPro
Complete GO annotation...

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
Peptidei575 – 58511PE-11By similarityPRO_0000432730Add
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 – 3771Phosphoserine1 Publication
Modified residuei380 – 3801PhosphoserineBy similarity
Modified residuei405 – 4051Phosphoserine3 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.
GeneTreeiENSGT00730000111312.
HOVERGENiHBG057317.
InParanoidiP05060.
OMAiNWGYEKR.
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

        10         20         30         40         50
MQPTLLLSLL GAVGLAAVNS MPVDNRNHNE GMVTRCIIEV LSNALSKSSA
60 70 80 90 100
PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS
110 120 130 140 150
RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE
160 170 180 190 200
EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN
210 220 230 240 250
ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EETGSQENHP
260 270 280 290 300
QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP
310 320 330 340 350
SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG
360 370 380 390 400
VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG
410 420 430 440 450
YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE
460 470 480 490 500
NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR
510 520 530 540 550
FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE
560 570 580 590 600
EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ
610 620 630 640 650
YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE
660 670
DEKKELENLA AMDLELQKIA EKFSQRG
Length:677
Mass (Da):78,276
Last modified:November 1, 2010 - v2
Checksum:iBFDC97F7B21245B3
GO

Sequence cautioni

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP05060.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP05060.

Polymorphism databases

DMDMi311033509.

Proteomic databases

PaxDbiP05060.
PeptideAtlasiP05060.
PRIDEiP05060.

Protocols and materials databases

DNASUi1114.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1114.
GeneCardsiGC20P005891.
H-InvDBHIX0015625.
HGNCiHGNC:1930. CHGB.
HPAiCAB009403.
HPA008759.
HPA012602.
MIMi118920. gene.
neXtProtiNX_P05060.
PharmGKBiPA26462.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39839.
GeneTreeiENSGT00730000111312.
HOVERGENiHBG057317.
InParanoidiP05060.
OMAiNWGYEKR.
OrthoDBiEOG74N5GF.
PhylomeDBiP05060.
TreeFamiTF336596.

Miscellaneous databases

ChiTaRSiCHGB. human.
GeneWikiiSecretoneurin.
GenomeRNAii1114.
NextBioi4622.
PROiP05060.
SOURCEiSearch...

Gene expression databases

BgeeiP05060.
CleanExiHS_CHGB.
GenevestigatoriP05060.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1986) [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(2003) [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 (MAY-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 (FEB-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(2000) [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(2003) [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(1990) [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(1994) [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(1984) [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(1986) [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(2003) [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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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 12, 1987
Last sequence update: November 1, 2010
Last modified: March 31, 2015
This is version 156 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.