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Protein

Glycogenin-2

Gene

GYG2

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

Functioni

Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.

Catalytic activityi

UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin.

Cofactori

Mn2+Note: Divalent metal ions. Required for self-glucosylation. Manganese is the most effective.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei119 – 1191By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS00703-MONOMER.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
REACT_169208. Glycogen synthesis.
REACT_264430. Myoclonic epilepsy of Lafora.
REACT_355557. Lysosomal glycogen catabolism.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogenin-2 (EC:2.4.1.186)
Short name:
GN-2
Short name:
GN2
Gene namesi
Name:GYG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:4700. GYG2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281Y → F: Loss of activity.
Mutagenesisi230 – 2301Y → F: No loss of activity.

Organism-specific databases

PharmGKBiPA29078.

Polymorphism and mutation databases

BioMutaiGYG2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Glycogenin-2PRO_0000215180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi228 – 2281O-linked (Glc...)1 Publication
Modified residuei368 – 3681Phosphoserine1 Publication
Modified residuei399 – 3991Phosphoserine1 Publication
Modified residuei459 – 4591Phosphoserine1 Publication

Post-translational modificationi

Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-228.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO15488.
PaxDbiO15488.
PRIDEiO15488.

PTM databases

PhosphoSiteiO15488.

Expressioni

Tissue specificityi

Expressed preferentially in liver, heart, and pancreas.

Gene expression databases

BgeeiO15488.
CleanExiHS_GYG2.
ExpressionAtlasiO15488. baseline and differential.
GenevestigatoriO15488.

Organism-specific databases

HPAiHPA005495.
HPA064686.

Interactioni

Subunit structurei

Homodimer, tightly complexed to glycogen synthase.

Protein-protein interaction databases

BioGridi114422. 7 interactions.
IntActiO15488. 3 interactions.
MINTiMINT-5003813.
STRINGi9606.ENSP00000370555.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 437Combined sources
Turni46 – 483Combined sources
Helixi49 – 6113Combined sources
Beta strandi66 – 727Combined sources
Helixi78 – 847Combined sources
Turni85 – 873Combined sources
Beta strandi89 – 935Combined sources
Helixi101 – 1099Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 1207Combined sources
Helixi121 – 1244Combined sources
Beta strandi128 – 1347Combined sources
Beta strandi138 – 1403Combined sources
Helixi145 – 1495Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi164 – 1729Combined sources
Helixi176 – 18914Combined sources
Helixi196 – 2038Combined sources
Turni204 – 2096Combined sources
Helixi212 – 2143Combined sources
Helixi218 – 2203Combined sources
Helixi232 – 2376Combined sources
Helixi238 – 2403Combined sources
Beta strandi242 – 2454Combined sources
Helixi252 – 2543Combined sources
Helixi277 – 29014Combined sources
Helixi292 – 2987Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UEGX-ray1.93A/B35-300[»]
ProteinModelPortaliO15488.
SMRiO15488. Positions 35-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5597.
GeneTreeiENSGT00390000004721.
HOGENOMiHOG000008282.
HOVERGENiHBG000681.
InParanoidiO15488.
KOiK00750.
OMAiNTAYTYS.
OrthoDBiEOG7BKCV8.
PhylomeDBiO15488.
TreeFamiTF312839.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11183. PTHR11183. 1 hit.
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform Alpha (identifier: O15488-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSETEFHHGA QAGLELLRSS NSPTSASQSA GMTVTDQAFV TLATNDIYCQ
60 70 80 90 100
GALVLGQSLR RHRLTRKLVV LITPQVSSLL RVILSKVFDE VIEVNLIDSA
110 120 130 140 150
DYIHLAFLKR PELGLTLTKL HCWTLTHYSK CVFLDADTLV LSNVDELFDR
160 170 180 190 200
GEFSAAPDPG WPDCFNSGVF VFQPSLHTHK LLLQHAMEHG SFDGADQGLL
210 220 230 240 250
NSFFRNWSTT DIHKHLPFIY NLSSNTMYTY SPAFKQFGSS AKVVHFLGSM
260 270 280 290 300
KPWNYKYNPQ SGSVLEQGSA SSSQHQAAFL HLWWTVYQNN VLPLYKSVQA
310 320 330 340 350
GEARASPGHT LCHSDVGGPC ADSASGVGEP CENSTPSAGV PCANSPLGSN
360 370 380 390 400
QPAQGLPEPT QIVDETLSLP EGRRSEDMIA CPETETPAVI TCDPLSQPSP
410 420 430 440 450
QPADFTETET ILQPANKVES VSSEETFEPS QELPAEALRD PSLQDALEVD
460 470 480 490 500
LAVSVSQISI EEKVKELSPE EERRKWEEGR IDYMGKDAFA RIQEKLDRFL

Q
Length:501
Mass (Da):55,184
Last modified:March 20, 2007 - v2
Checksum:i8488A09D6E564693
GO
Isoform Beta (identifier: O15488-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-33: Missing.

Show »
Length:470
Mass (Da):51,999
Checksum:iB846651872D5D26E
GO
Isoform Gamma (identifier: O15488-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-42: Missing.

Show »
Length:461
Mass (Da):51,024
Checksum:iA04519016F2221BB
GO
Isoform Delta (identifier: O15488-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     378-448: Missing.

Show »
Length:430
Mass (Da):47,530
Checksum:i940F41982ACB1650
GO
Isoform Epsilon (identifier: O15488-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-501: Missing.

Show »
Length:406
Mass (Da):44,295
Checksum:i6370F23C7DC32423
GO
Isoform Zeta (identifier: O15488-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     413-448: Missing.

Show »
Length:465
Mass (Da):51,260
Checksum:iAB2B130A1FD5EA73
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti413 – 4131Missing in AAB84378 (PubMed:9346895).Curated
Sequence conflicti462 – 4643EKV → AGI in AAB84376 (PubMed:9346895).Curated

Mass spectrometryi

Molecular mass is 55211.89 Da from positions 1 - 501. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71H → Y.
Corresponds to variant rs11797037 [ dbSNP | Ensembl ].
VAR_053110
Natural varianti194 – 1941G → R Found in a renal cell carcinoma case; somatic mutation. 1 Publication
VAR_064717
Natural varianti270 – 2701A → V.
Corresponds to variant rs2306734 [ dbSNP | Ensembl ].
VAR_010401
Natural varianti313 – 3131H → R.1 Publication
Corresponds to variant rs2306735 [ dbSNP | Ensembl ].
VAR_024457
Natural varianti373 – 3731R → C.
Corresponds to variant rs17330993 [ dbSNP | Ensembl ].
VAR_031224

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3 – 4240Missing in isoform Gamma. CuratedVSP_001771Add
BLAST
Alternative sequencei3 – 3331Missing in isoform Beta. 1 PublicationVSP_001770Add
BLAST
Alternative sequencei378 – 44871Missing in isoform Delta. CuratedVSP_001772Add
BLAST
Alternative sequencei407 – 50195Missing in isoform Epsilon. CuratedVSP_001773Add
BLAST
Alternative sequencei413 – 44836Missing in isoform Zeta. CuratedVSP_001774Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94362 mRNA. Translation: AAB84377.1.
U94363 mRNA. Translation: AAB84378.1.
U94364 mRNA. Translation: AAB84379.1.
U94357 mRNA. Translation: AAB84373.1.
U94358 mRNA. Translation: AAB84374.1.
U94360 mRNA. Translation: AAB84375.1.
U94361 mRNA. Translation: AAB84376.1.
AF179624
, AF179615, AF179616, AF179617, AF179618, AF179619, AF179620, AF179621, AF179622, AF179623 Genomic DNA. Translation: AAF61855.1.
AC138085 Genomic DNA. No translation available.
BC023152 mRNA. Translation: AAH23152.1.
CCDSiCCDS14121.1. [O15488-1]
CCDS48074.1. [O15488-2]
RefSeqiNP_001073324.1. NM_001079855.1. [O15488-2]
NP_001171631.1. NM_001184702.1.
NP_001171632.1. NM_001184703.1. [O15488-4]
NP_001171633.1. NM_001184704.1.
NP_003909.2. NM_003918.2. [O15488-1]
UniGeneiHs.567381.
Hs.701629.

Genome annotation databases

EnsembliENST00000353656; ENSP00000487294; ENSG00000056998. [O15488-4]
ENST00000381163; ENSP00000370555; ENSG00000056998. [O15488-1]
ENST00000398806; ENSP00000381786; ENSG00000056998. [O15488-2]
GeneIDi8908.
KEGGihsa:8908.
UCSCiuc004cqs.1. human. [O15488-1]
uc004cqt.1. human. [O15488-2]
uc004cqv.1. human. [O15488-4]
uc004cqw.1. human. [O15488-3]
uc010ndc.1. human. [O15488-6]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94362 mRNA. Translation: AAB84377.1.
U94363 mRNA. Translation: AAB84378.1.
U94364 mRNA. Translation: AAB84379.1.
U94357 mRNA. Translation: AAB84373.1.
U94358 mRNA. Translation: AAB84374.1.
U94360 mRNA. Translation: AAB84375.1.
U94361 mRNA. Translation: AAB84376.1.
AF179624
, AF179615, AF179616, AF179617, AF179618, AF179619, AF179620, AF179621, AF179622, AF179623 Genomic DNA. Translation: AAF61855.1.
AC138085 Genomic DNA. No translation available.
BC023152 mRNA. Translation: AAH23152.1.
CCDSiCCDS14121.1. [O15488-1]
CCDS48074.1. [O15488-2]
RefSeqiNP_001073324.1. NM_001079855.1. [O15488-2]
NP_001171631.1. NM_001184702.1.
NP_001171632.1. NM_001184703.1. [O15488-4]
NP_001171633.1. NM_001184704.1.
NP_003909.2. NM_003918.2. [O15488-1]
UniGeneiHs.567381.
Hs.701629.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UEGX-ray1.93A/B35-300[»]
ProteinModelPortaliO15488.
SMRiO15488. Positions 35-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114422. 7 interactions.
IntActiO15488. 3 interactions.
MINTiMINT-5003813.
STRINGi9606.ENSP00000370555.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

PTM databases

PhosphoSiteiO15488.

Polymorphism and mutation databases

BioMutaiGYG2.

Proteomic databases

MaxQBiO15488.
PaxDbiO15488.
PRIDEiO15488.

Protocols and materials databases

DNASUi8908.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353656; ENSP00000487294; ENSG00000056998. [O15488-4]
ENST00000381163; ENSP00000370555; ENSG00000056998. [O15488-1]
ENST00000398806; ENSP00000381786; ENSG00000056998. [O15488-2]
GeneIDi8908.
KEGGihsa:8908.
UCSCiuc004cqs.1. human. [O15488-1]
uc004cqt.1. human. [O15488-2]
uc004cqv.1. human. [O15488-4]
uc004cqw.1. human. [O15488-3]
uc010ndc.1. human. [O15488-6]

Organism-specific databases

CTDi8908.
GeneCardsiGC0XP002740.
H-InvDBHIX0016632.
HIX0025849.
HGNCiHGNC:4700. GYG2.
HPAiHPA005495.
HPA064686.
MIMi300198. gene.
neXtProtiNX_O15488.
PharmGKBiPA29078.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5597.
GeneTreeiENSGT00390000004721.
HOGENOMiHOG000008282.
HOVERGENiHBG000681.
InParanoidiO15488.
KOiK00750.
OMAiNTAYTYS.
OrthoDBiEOG7BKCV8.
PhylomeDBiO15488.
TreeFamiTF312839.

Enzyme and pathway databases

UniPathwayiUPA00164.
BioCyciMetaCyc:HS00703-MONOMER.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
REACT_169208. Glycogen synthesis.
REACT_264430. Myoclonic epilepsy of Lafora.
REACT_355557. Lysosomal glycogen catabolism.

Miscellaneous databases

ChiTaRSiGYG2. human.
GenomeRNAii8908.
NextBioi33471.
PROiO15488.
SOURCEiSearch...

Gene expression databases

BgeeiO15488.
CleanExiHS_GYG2.
ExpressionAtlasiO15488. baseline and differential.
GenevestigatoriO15488.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11183. PTHR11183. 1 hit.
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glycogenin-2, a novel self-glucosylating protein involved in liver glycogen biosynthesis."
    Mu J., Skurat A.V., Roach P.J.
    J. Biol. Chem. 272:27589-27597(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Liver.
  2. "Structure and chromosomal localization of the human glycogenin-2 gene GYG2."
    Zhai L., Mu J., Zong H., DePaoli-Roach A.A., Roach P.J.
    Gene 242:229-235(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM BETA), VARIANT ARG-313.
    Tissue: Skin.
  5. "Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism."
    Mu J., Roach P.J.
    J. Biol. Chem. 273:34850-34856(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, GLYCOSYLATION AT TYR-228.
  6. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  7. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-399 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: VARIANT ARG-194.

Entry informationi

Entry nameiGLYG2_HUMAN
AccessioniPrimary (citable) accession number: O15488
Secondary accession number(s): B7WNN6
, O15485, O15486, O15487, O15489, O15490
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: March 20, 2007
Last modified: May 27, 2015
This is version 149 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.