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Protein

Gamma-adducin

Gene

ADD3

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

Functioni

Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.

GO - Molecular functioni

  1. structural constituent of cytoskeleton Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-adducin
Alternative name(s):
Adducin-like protein 70
Gene namesi
Name:ADD3
Synonyms:ADDL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:245. ADD3.

Subcellular locationi

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cell cortex Source: Ensembl
  3. condensed nuclear chromosome Source: Ensembl
  4. cytoplasm Source: HPA
  5. cytoskeleton Source: UniProtKB-SubCell
  6. membrane Source: ProtInc
  7. nucleoplasm Source: HPA
  8. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti210141. Inherited congenital spastic tetraplegia.
PharmGKBiPA24567.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 706705Gamma-adducinPRO_0000218536Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei42 – 421Phosphoserine2 Publications
Modified residuei59 – 591PhosphothreonineBy similarity
Modified residuei64 – 641Phosphoserine2 Publications
Modified residuei402 – 4021Phosphoserine1 Publication
Modified residuei423 – 4231Phosphoserine2 Publications
Modified residuei442 – 4421Phosphoserine1 Publication
Modified residuei558 – 5581PhosphothreonineBy similarity
Modified residuei590 – 5901PhosphoserineBy similarity
Modified residuei592 – 5921PhosphoserineBy similarity
Modified residuei598 – 5981PhosphothreonineBy similarity
Modified residuei600 – 6001PhosphoserineBy similarity
Modified residuei673 – 6731Phosphoserine3 Publications
Modified residuei677 – 6771Phosphoserine3 Publications
Modified residuei681 – 6811Phosphoserine3 Publications
Modified residuei683 – 6831Phosphoserine; by PKCBy similarity
Modified residuei693 – 6931PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UEY8.
PaxDbiQ9UEY8.
PRIDEiQ9UEY8.

PTM databases

PhosphoSiteiQ9UEY8.

Miscellaneous databases

PMAP-CutDBQ9UEY8.

Expressioni

Tissue specificityi

Isoform 1 is ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ9UEY8.
CleanExiHS_ADD3.
ExpressionAtlasiQ9UEY8. baseline and differential.
GenevestigatoriQ9UEY8.

Organism-specific databases

HPAiCAB009797.
HPA035696.

Interactioni

Subunit structurei

Heterodimer of an alpha and a gamma subunit.

Protein-protein interaction databases

BioGridi106633. 10 interactions.
IntActiQ9UEY8. 6 interactions.
STRINGi9606.ENSP00000348381.

Structurei

3D structure databases

ProteinModelPortaliQ9UEY8.
SMRiQ9UEY8. Positions 153-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni684 – 70118Interaction with calmodulinSequence AnalysisAdd
BLAST

Domaini

Comprised of three regions: a N-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0235.
GeneTreeiENSGT00390000016462.
HOGENOMiHOG000116349.
HOVERGENiHBG004180.
InParanoidiQ9UEY8.
KOiK18622.
OMAiNRYDLKT.
OrthoDBiEOG7HF1HR.
PhylomeDBiQ9UEY8.
TreeFamiTF313003.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
InterProiIPR027772. ADD3.
IPR001303. Aldolase_II/adducin_N.
[Graphical view]
PANTHERiPTHR10672:SF5. PTHR10672:SF5. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 2 (identifier: Q9UEY8-1) [UniParc]FASTAAdd to basket

Also known as: Long

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
MSSDASQGVI TTPPPPSMPH KERYFDRINE NDPEYIRERN MSPDLRQDFN
60 70 80 90 100
MMEQRKRVTQ ILQSPAFRED LECLIQEQMK KGHNPTGLLA LQQIADYIMA
110 120 130 140 150
NSFSGFSSPP LSLGMVTPIN DLPGADTSSY VKGEKLTRCK LASLYRLVDL
160 170 180 190 200
FGWAHLANTY ISVRISKEQD HIIIIPRGLS FSEATASNLV KVNIIGEVVD
210 220 230 240 250
QGSTNLKIDH TGFSPHAAIY STRPDVKCVI HIHTLATAAV SSMKCGILPI
260 270 280 290 300
SQESLLLGDV AYYDYQGSLE EQEERIQLQK VLGPSCKVLV LRNHGVVALG
310 320 330 340 350
ETLEEAFHYI FNVQLACEIQ VQALAGAGGV DNLHVLDFQK YKAFTYTVAA
360 370 380 390 400
SGGGGVNMGS HQKWKVGEIE FEGLMRTLDN LGYRTGYAYR HPLIREKPRH
410 420 430 440 450
KSDVEIPATV TAFSFEDDTV PLSPLKYMAQ RQQREKTRWL NSPNTYMKVN
460 470 480 490 500
VPEESRNGET SPRTKITWMK AEDSSKVSGG TPIKIEDPNQ FVPLNTNPNE
510 520 530 540 550
VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMQF EDDDHGPPAP
560 570 580 590 600
PNPFSHLTEG ELEEYKRTIE RKQQGLEDAE QELLSDDASS VSQIQSQTQS
610 620 630 640 650
PQNVPEKLEE NHELFSKSFI SMEVPVMVVN GKDDMHDVED ELAKRVSRLS
660 670 680 690 700
TSTTIENIEI TIKSPEKIEE VLSPEGSPSK SPSKKKKKFR TPSFLKKNKK

KEKVEA
Length:706
Mass (Da):79,155
Last modified:May 1, 2000 - v1
Checksum:iEB8EAF602A4D7B41
GO
Isoform 1 (identifier: Q9UEY8-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     576-607: Missing.

Show »
Length:674
Mass (Da):75,671
Checksum:i28935F90F7C17BD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 502FN → SS in BAA23783 (PubMed:8893809).Curated
Sequence conflicti60 – 601Q → R in BAA23783 (PubMed:8893809).Curated
Sequence conflicti362 – 3621Q → P in AAB17126 (Ref. 2) Curated
Sequence conflicti420 – 4201V → M in AAB17126 (Ref. 2) Curated
Sequence conflicti421 – 4211P → L in BAA23783 (PubMed:8893809).Curated
Sequence conflicti426 – 4338KYMAQRQQ → QIHGTRGNK in AAB17126 (Ref. 2) Curated
Sequence conflicti484 – 4841K → Q in AAB17126 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei576 – 60732Missing in isoform 1. 3 PublicationsVSP_000188Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67031 mRNA. Translation: BAA23783.1.
U37122 mRNA. Translation: AAB17126.1.
Y14372
, Y14373, Y14374, Y14375, Y14376, Y14377, Y14378, Y14379, Y14380, Y14381, Y14382, Y14383, Y14384 Genomic DNA. Translation: CAB51805.1.
Y14372
, Y14373, Y14374, Y14375, Y14376, Y14377, Y14378, Y14379, Y14380, Y14381, Y14382, Y14384 Genomic DNA. Translation: CAB51806.1.
BX647403 mRNA. Translation: CAI46048.1.
AL590628 Genomic DNA. Translation: CAH71739.1.
CH471066 Genomic DNA. Translation: EAW49573.1.
CH471066 Genomic DNA. Translation: EAW49574.1.
BC062559 mRNA. Translation: AAH62559.1.
CCDSiCCDS7561.1. [Q9UEY8-1]
CCDS7562.1. [Q9UEY8-2]
PIRiJC7164.
RefSeqiNP_001112.2. NM_001121.2. [Q9UEY8-2]
NP_058432.1. NM_016824.3. [Q9UEY8-1]
NP_063968.1. NM_019903.3. [Q9UEY8-2]
XP_005269586.1. XM_005269529.1. [Q9UEY8-1]
XP_005269587.1. XM_005269530.1. [Q9UEY8-1]
XP_005269588.1. XM_005269531.2. [Q9UEY8-1]
XP_005269590.1. XM_005269533.1. [Q9UEY8-1]
XP_005269591.1. XM_005269534.2. [Q9UEY8-1]
XP_006717689.1. XM_006717626.1. [Q9UEY8-1]
XP_006717690.1. XM_006717627.1. [Q9UEY8-1]
XP_006717691.1. XM_006717628.1. [Q9UEY8-1]
UniGeneiHs.501012.

Genome annotation databases

EnsembliENST00000277900; ENSP00000277900; ENSG00000148700. [Q9UEY8-2]
ENST00000356080; ENSP00000348381; ENSG00000148700. [Q9UEY8-1]
ENST00000360162; ENSP00000353286; ENSG00000148700. [Q9UEY8-2]
GeneIDi120.
KEGGihsa:120.
UCSCiuc001kys.4. human. [Q9UEY8-2]
uc001kyt.4. human. [Q9UEY8-1]

Polymorphism databases

DMDMi12643881.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67031 mRNA. Translation: BAA23783.1.
U37122 mRNA. Translation: AAB17126.1.
Y14372
, Y14373, Y14374, Y14375, Y14376, Y14377, Y14378, Y14379, Y14380, Y14381, Y14382, Y14383, Y14384 Genomic DNA. Translation: CAB51805.1.
Y14372
, Y14373, Y14374, Y14375, Y14376, Y14377, Y14378, Y14379, Y14380, Y14381, Y14382, Y14384 Genomic DNA. Translation: CAB51806.1.
BX647403 mRNA. Translation: CAI46048.1.
AL590628 Genomic DNA. Translation: CAH71739.1.
CH471066 Genomic DNA. Translation: EAW49573.1.
CH471066 Genomic DNA. Translation: EAW49574.1.
BC062559 mRNA. Translation: AAH62559.1.
CCDSiCCDS7561.1. [Q9UEY8-1]
CCDS7562.1. [Q9UEY8-2]
PIRiJC7164.
RefSeqiNP_001112.2. NM_001121.2. [Q9UEY8-2]
NP_058432.1. NM_016824.3. [Q9UEY8-1]
NP_063968.1. NM_019903.3. [Q9UEY8-2]
XP_005269586.1. XM_005269529.1. [Q9UEY8-1]
XP_005269587.1. XM_005269530.1. [Q9UEY8-1]
XP_005269588.1. XM_005269531.2. [Q9UEY8-1]
XP_005269590.1. XM_005269533.1. [Q9UEY8-1]
XP_005269591.1. XM_005269534.2. [Q9UEY8-1]
XP_006717689.1. XM_006717626.1. [Q9UEY8-1]
XP_006717690.1. XM_006717627.1. [Q9UEY8-1]
XP_006717691.1. XM_006717628.1. [Q9UEY8-1]
UniGeneiHs.501012.

3D structure databases

ProteinModelPortaliQ9UEY8.
SMRiQ9UEY8. Positions 153-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106633. 10 interactions.
IntActiQ9UEY8. 6 interactions.
STRINGi9606.ENSP00000348381.

PTM databases

PhosphoSiteiQ9UEY8.

Polymorphism databases

DMDMi12643881.

Proteomic databases

MaxQBiQ9UEY8.
PaxDbiQ9UEY8.
PRIDEiQ9UEY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000277900; ENSP00000277900; ENSG00000148700. [Q9UEY8-2]
ENST00000356080; ENSP00000348381; ENSG00000148700. [Q9UEY8-1]
ENST00000360162; ENSP00000353286; ENSG00000148700. [Q9UEY8-2]
GeneIDi120.
KEGGihsa:120.
UCSCiuc001kys.4. human. [Q9UEY8-2]
uc001kyt.4. human. [Q9UEY8-1]

Organism-specific databases

CTDi120.
GeneCardsiGC10P111755.
H-InvDBHIX0170444.
HGNCiHGNC:245. ADD3.
HPAiCAB009797.
HPA035696.
MIMi601568. gene.
neXtProtiNX_Q9UEY8.
Orphaneti210141. Inherited congenital spastic tetraplegia.
PharmGKBiPA24567.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0235.
GeneTreeiENSGT00390000016462.
HOGENOMiHOG000116349.
HOVERGENiHBG004180.
InParanoidiQ9UEY8.
KOiK18622.
OMAiNRYDLKT.
OrthoDBiEOG7HF1HR.
PhylomeDBiQ9UEY8.
TreeFamiTF313003.

Miscellaneous databases

ChiTaRSiADD3. human.
GeneWikiiADD3.
GenomeRNAii120.
NextBioi481.
PMAP-CutDBQ9UEY8.
PROiQ9UEY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UEY8.
CleanExiHS_ADD3.
ExpressionAtlasiQ9UEY8. baseline and differential.
GenevestigatoriQ9UEY8.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
InterProiIPR027772. ADD3.
IPR001303. Aldolase_II/adducin_N.
[Graphical view]
PANTHERiPTHR10672:SF5. PTHR10672:SF5. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a human cDNA highly homologous to human erythrocyte adducin."
    Katagiri T., Ozaki K., Fujiwara T., Shimizu F., Kawai A., Okuno S., Suzuki M., Nakamura Y., Takahashi E., Hirai Y.
    Cytogenet. Cell Genet. 74:90-95(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Cloning in the gamma quadrant."
    Moorthy S., Bennett V.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Endometrium.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Ovary.
  8. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
    Gocke C.B., Yu H., Kang J.
    J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-423; SER-442; SER-673; SER-677 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-423 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-673 AND SER-677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiADDG_HUMAN
AccessioniPrimary (citable) accession number: Q9UEY8
Secondary accession number(s): D3DRA8
, O43243, Q5VU09, Q92773, Q9UEY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 124 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.