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P35611 (ADDA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-adducin
Alternative name(s):
Erythrocyte adducin subunit alpha
Gene names
Name:ADD1
Synonyms:ADDA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Heterodimer of an alpha and a beta subunit or an alpha and a gamma subunit.

Subcellular location

Cytoplasmcytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.

Tissue specificity

Expressed in all tissues. Found in much higher levels in reticulocytes than the beta subunit.

Domain

Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region.

Sequence similarities

Belongs to the aldolase class II family. Adducin subfamily.

Sequence caution

The sequence CAA98970.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandActin-binding
Calmodulin-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred by curator PubMed 3693401. Source: BHF-UCL

actin filament bundle assembly

Inferred from direct assay PubMed 3693401. Source: BHF-UCL

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

barbed-end actin filament capping

Inferred from direct assay PubMed 8626479. Source: BHF-UCL

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell volume homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

hemoglobin metabolic process

Inferred from electronic annotation. Source: Ensembl

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of endocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein binding

Inferred from direct assay PubMed 3693401PubMed 7642559. Source: BHF-UCL

   Cellular_componentF-actin capping protein complex

Inferred from direct assay PubMed 8626479. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: Ensembl

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 16289097. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay. Source: HPA

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin binding

Traceable author statement Ref.1. Source: ProtInc

actin filament binding

Inferred from direct assay PubMed 7642559. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 7642559. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction PubMed 7642559. Source: BHF-UCL

spectrin binding

Inferred from direct assay PubMed 7642559. Source: BHF-UCL

structural molecule activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from physical interaction PubMed 16289097. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P35611-1)

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.
Isoform 2 (identifier: P35611-2)

The sequence of this isoform differs from the canonical sequence as follows:
     621-631: DLVPEPTTGDD → GDGCAREYLLP
     632-737: Missing.
Isoform 3 (identifier: P35611-3)

The sequence of this isoform differs from the canonical sequence as follows:
     471-471: K → KVWTNITHDHVKPLLQSLSSGVCVPSCITNCL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 737737Alpha-adducin
PRO_0000218530

Regions

Region717 – 73418Interaction with calmodulin Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue121Phosphoserine Ref.10 Ref.15
Modified residue591Phosphoserine; by PKA Ref.6
Modified residue3311Phosphothreonine Ref.10
Modified residue3341Phosphoserine Ref.10
Modified residue3581Phosphoserine Ref.9 Ref.10 Ref.15
Modified residue4081Phosphoserine; by PKA Ref.6
Modified residue4311Phosphoserine Ref.10
Modified residue4361Phosphoserine; by PKA Ref.6 Ref.10
Modified residue4451Phosphothreonine; by ROCK2 Ref.7
Modified residue4651Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
Modified residue4801Phosphothreonine; by ROCK2 Ref.7
Modified residue4811Phosphoserine; by PKA Ref.6
Modified residue5861Phosphoserine Ref.15
Modified residue7071Phosphoserine Ref.8 Ref.15
Modified residue7101Phosphoserine Ref.8 Ref.15
Modified residue7141Phosphoserine Ref.15
Modified residue7161Phosphoserine; by PKC Ref.6
Modified residue7261Phosphoserine; by PKA and PKC Ref.6

Natural variations

Alternative sequence4711K → KVWTNITHDHVKPLLQSLSS GVCVPSCITNCL in isoform 3.
VSP_000174
Alternative sequence621 – 63111DLVPEPTTGDD → GDGCAREYLLP in isoform 2.
VSP_000175
Alternative sequence632 – 737106Missing in isoform 2.
VSP_000176
Natural variant61R → C.
Corresponds to variant rs2295497 [ dbSNP | Ensembl ].
VAR_022108
Natural variant2701Y → N.
Corresponds to variant rs4971 [ dbSNP | Ensembl ].
VAR_014863
Natural variant3761E → D.
Corresponds to variant rs4972 [ dbSNP | Ensembl ].
VAR_014864
Natural variant4601G → W. Ref.16 Ref.17
Corresponds to variant rs4961 [ dbSNP | Ensembl ].
VAR_014184
Natural variant5101N → I.
Corresponds to variant rs4962 [ dbSNP | Ensembl ].
VAR_014865
Natural variant5861S → C. Ref.1 Ref.17
Corresponds to variant rs4963 [ dbSNP | Ensembl ].
VAR_014185

Experimental info

Mutagenesis4451T → D: Abolishes phosphorylation by ROCK2; when associated with D-480. Ref.7
Mutagenesis4801T → D: Abolishes phosphorylation by ROCK2; when associated with D-445. Ref.7
Sequence conflict6061A → E in AAB05645. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: DF13AB30B12F20B6

FASTA73780,955
        10         20         30         40         50         60 
MNGDSRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM 

        70         80         90        100        110        120 
ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTT NVPNVYPAAP QGGMAALNMS 

       130        140        150        160        170        180 
LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF 

       190        200        210        220        230        240 
LIVPFGLLYS EVTASSLVKI NLQGDIVDRG STNLGVNQAG FTLHSAIYAA RPDVKCVVHI 

       250        260        270        280        290        300 
HTPAGAAVSA MKCGLLPISP EALSLGEVAY HDYHGILVDE EEKVLIQKNL GPKSKVLILR 

       310        320        330        340        350        360 
NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLNPEKYK AKSRSPGSPV 

       370        380        390        400        410        420 
GEGTGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL REKSKKYSDV EVPASVTGYS 

       430        440        450        460        470        480 
FASDGDSGTC SPLRHSFQKQ QREKTRWLNS GRGDEASEEG QNGSSPKSKT KWTKEDGHRT 

       490        500        510        520        530        540 
STSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLCGVVMD RSLVQGELVT 

       550        560        570        580        590        600 
ASKAIIEKEY QPHVIVSTTG PNPFTTLTDR ELEEYRREVE RKQKGSEENL DEAREQKEKS 

       610        620        630        640        650        660 
PPDQPAVPHP PPSTPIKLEE DLVPEPTTGD DSDAATFKPT LPDLSPDEPS EALGFPMLEK 

       670        680        690        700        710        720 
EEEAHRPPSP TEAPTEASPE PAPDPAPVAE EAAPSAVEEG AAADPGSDGS PGKSPSKKKK 

       730 
KFRTPSFLKK SKKKSDS 

« Hide

Isoform 2 [UniParc].

Checksum: 350DDCF58AB61357
Show »

FASTA63169,985
Isoform 3 [UniParc].

Checksum: D97BFFA790F661CA
Show »

FASTA76884,303

References

« Hide 'large scale' references
[1]"Primary structure and domain organization of human alpha and beta adducin."
Joshi R.L., Gilligan D.M., Otto E., McLaughlin T., Bennett V.D.
J. Cell Biol. 115:665-675(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-36; 41-47; 516-569 AND 722-729, VARIANT CYS-586.
Tissue: Reticulocyte.
[2]"Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms."
Lin B., Nasir J., McDonald H., Graham R., Rommens J.M., Goldberg Y.P., Hayden M.R.
Genomics 25:93-99(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification."
Taylor S.A., Snell R.G., Buckler A., Ambrose C., Duyao M., Church D., Lin C.S., Altherr M., Bates G.P., Groot N.
Nat. Genet. 2:223-227(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 531-737 (ISOFORMS 1/3).
[6]"Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C."
Matsuoka Y., Hughes C.A., Bennett V.
J. Biol. Chem. 271:25157-25166(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-59; SER-408; SER-436; SER-481; SER-716 AND SER-726, PARTIAL PROTEIN SEQUENCE.
[7]"Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility."
Fukata Y., Oshiro N., Kinoshita N., Kawano Y., Matsuoka Y., Bennett V., Matsuura Y., Kaibuchi K.
J. Cell Biol. 145:347-361(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-445 AND THR-480, MUTAGENESIS OF THR-445 AND THR-480.
[8]"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-707 AND SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-331; SER-334; SER-358; SER-431; SER-436 AND SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-12; SER-358; SER-465; SER-586; SER-707; SER-710 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Human alpha-adducin gene, blood pressure, and sodium metabolism."
Kamitani A., Wong Z.Y., Fraser R., Davies D.L., Connor J.M., Foy C.J., Watt G.C., Harrap S.B.
Hypertension 32:138-143(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TRP-460.
[17]"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TRP-460 AND CYS-586.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58141 mRNA. Translation: CAA41149.1.
L29296 expand/collapse EMBL AC list , L29286, L29287, L29289, L29290, L29291, L29292, L29293, L29294, L29295, L29297, L29298 Genomic DNA. Translation: AAB05645.1.
Z74617 Genomic DNA. Translation: CAA98970.1. Sequence problems.
Z68280 Genomic DNA. No translation available.
AL390065, AL121750, BX465861 Genomic DNA. Translation: CAM21299.1.
BX465861, AL121750, AL390065 Genomic DNA. Translation: CAM25274.1.
AL121750, AL390065, BX465861 Genomic DNA. Translation: CAM28232.1.
CH471131 Genomic DNA. Translation: EAW82498.1.
CH471131 Genomic DNA. Translation: EAW82499.1.
CH471131 Genomic DNA. Translation: EAW82501.1.
CH471131 Genomic DNA. Translation: EAW82502.1.
CH471131 Genomic DNA. Translation: EAW82503.1.
CH471131 Genomic DNA. Translation: EAW82505.1.
AH004561 mRNA. Translation: AAB30914.2.
PIRS18207.
RefSeqNP_001110.2. NM_001119.4.
NP_054908.2. NM_014189.3.
NP_054909.2. NM_014190.3.
NP_789771.1. NM_176801.2.
UniGeneHs.183706.

3D structure databases

DisProtDP00240.
ProteinModelPortalP35611.
SMRP35611. Positions 161-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106631. 19 interactions.
IntActP35611. 10 interactions.
MINTMINT-1499912.
STRING9606.ENSP00000264758.

PTM databases

PhosphoSiteP35611.

Polymorphism databases

DMDM12644231.

Proteomic databases

PaxDbP35611.
PRIDEP35611.

Protocols and materials databases

DNASU118.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264758; ENSP00000264758; ENSG00000087274. [P35611-3]
ENST00000398129; ENSP00000381197; ENSG00000087274. [P35611-1]
ENST00000446856; ENSP00000399828; ENSG00000087274. [P35611-1]
GeneID118.
KEGGhsa:118.
UCSCuc003gfp.3. human. [P35611-2]
uc003gfq.3. human. [P35611-3]
uc003gfr.3. human. [P35611-1]

Organism-specific databases

CTD118.
GeneCardsGC04P002849.
HGNCHGNC:243. ADD1.
HPACAB009794.
HPA035873.
HPA035874.
MIM102680. gene.
neXtProtNX_P35611.
PharmGKBPA31.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0235.
HOVERGENHBG004180.
OMAWTKEDGH.
PhylomeDBP35611.
TreeFamTF313003.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP35611.
BgeeP35611.
CleanExHS_ADD1.
GenevestigatorP35611.

Family and domain databases

Gene3D3.40.225.10. 1 hit.
InterProIPR027766. ADD1.
IPR001303. Aldolase_II/adducin_N.
[Graphical view]
PANTHERPTHR10672:SF4. PTHR10672:SF4. 1 hit.
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMSSF53639. SSF53639. 1 hit.
ProtoNetSearch...

Other

ChiTaRSADD1. human.
GeneWikiADD1.
GenomeRNAi118.
NextBio459.
PMAP-CutDBP35611.
PROP35611.
SOURCESearch...

Entry information

Entry nameADDA_HUMAN
AccessionPrimary (citable) accession number: P35611
Secondary accession number(s): A2A3P0 expand/collapse secondary AC list , D3DVR3, D3DVR4, D3DVR5, Q13734, Q14729, Q16156, Q9UJB6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM