P35611 (ADDA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-adducin

Alternative name(s):
Erythrocyte adducin subunit alpha

Gene names

Name:	ADD1
Synonyms:	ADDA

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	737 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. 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 component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Actin-binding Calmodulin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 barbed-end actin filament capping Inferred from direct assay PubMed 8626479. Source: BHF-UCL cell morphogenesis Inferred from electronic annotation. Source: Compara cell volume homeostasis Inferred from electronic annotation. Source: Compara cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome cellular response to retinoic acid Inferred from electronic annotation. Source: Compara erythrocyte differentiation Inferred from electronic annotation. Source: Compara hemoglobin metabolic process Inferred from electronic annotation. Source: Compara homeostasis of number of cells within a tissue Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara positive regulation of endocytosis Inferred from electronic annotation. Source: Compara positive regulation of protein binding Inferred from direct assay PubMed 3693401PubMed 7642559. Source: BHF-UCL
Cellular_component	F-actin capping protein complex Inferred from direct assay PubMed 8626479. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 16289097. Source: BHF-UCL perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from electronic annotation. Source: Compara
Molecular_function	actin filament binding Inferred from direct assay PubMed 7642559. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: InterPro spectrin binding Inferred from direct assay PubMed 7642559. Source: BHF-UCL structural molecule activity Inferred from electronic annotation. Source: Compara
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 737	737	Alpha-adducin		PRO_0000218530
Regions
	Region	717 – 734	18	Interaction with calmodulin Potential
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.10 Ref.14
	Modified residue	59	1	Phosphoserine; by PKA Ref.6
	Modified residue	331	1	Phosphothreonine Ref.10
	Modified residue	334	1	Phosphoserine Ref.10
	Modified residue	355	1	Phosphoserine By similarity
	Modified residue	358	1	Phosphoserine Ref.9 Ref.10 Ref.14
	Modified residue	408	1	Phosphoserine; by PKA Ref.6
	Modified residue	431	1	Phosphoserine Ref.10
	Modified residue	436	1	Phosphoserine; by PKA Ref.6 Ref.10
	Modified residue	445	1	Phosphothreonine; by ROCK2 Ref.7
	Modified residue	465	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14
	Modified residue	480	1	Phosphothreonine; by ROCK2 Ref.7
	Modified residue	481	1	Phosphoserine; by PKA Ref.6
	Modified residue	483	1	Phosphoserine By similarity
	Modified residue	586	1	Phosphoserine Ref.14
	Modified residue	614	1	Phosphothreonine By similarity
	Modified residue	707	1	Phosphoserine Ref.8 Ref.14
	Modified residue	710	1	Phosphoserine Ref.8 Ref.14
	Modified residue	714	1	Phosphoserine Ref.14
	Modified residue	716	1	Phosphoserine; by PKC Ref.6
	Modified residue	726	1	Phosphoserine; by PKA and PKC Ref.6
Natural variations
	Alternative sequence	471	1	K → KVWTNITHDHVKPLLQSLSS GVCVPSCITNCL in isoform 3.		VSP_000174
	Alternative sequence	621 – 631	11	DLVPEPTTGDD → GDGCAREYLLP in isoform 2.		VSP_000175
	Alternative sequence	632 – 737	106	Missing in isoform 2.		VSP_000176
	Natural variant	6	1	R → C. Corresponds to variant rs2295497 [ dbSNP | Ensembl ].		VAR_022108
	Natural variant	270	1	Y → N. Corresponds to variant rs4971 [ dbSNP | Ensembl ].		VAR_014863
	Natural variant	376	1	E → D. Corresponds to variant rs4972 [ dbSNP | Ensembl ].		VAR_014864
	Natural variant	460	1	G → W. Ref.15 Ref.16 Corresponds to variant rs4961 [ dbSNP | Ensembl ].		VAR_014184
	Natural variant	510	1	N → I. Corresponds to variant rs4962 [ dbSNP | Ensembl ].		VAR_014865
	Natural variant	586	1	S → C. Ref.1 Ref.16 Corresponds to variant rs4963 [ dbSNP | Ensembl ].		VAR_014185
Experimental info
	Mutagenesis	445	1	T → D: Abolishes phosphorylation by ROCK2; when associated with D-480. Ref.7
	Mutagenesis	480	1	T → D: Abolishes phosphorylation by ROCK2; when associated with D-445. Ref.7
	Sequence conflict	606	1	A → E in AAB05645. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: DF13AB30B12F20B6	FASTA	737	80,955
	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
	Isoform 2 [UniParc]. Checksum: 350DDCF58AB61357	FASTA	631	69,985
	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 PPDQPAVPHP PPSTPIKLEE GDGCAREYLL P
	Isoform 3 [UniParc]. Checksum: D97BFFA790F661CA	FASTA	768	84,303
	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 KVWTNITHDH 490 500 510 520 530 540 VKPLLQSLSS GVCVPSCITN CLWTKEDGHR TSTSAVPNLF VPLNTNPKEV QEMRNKIREQ 550 560 570 580 590 600 NLQDIKTAGP QSQVLCGVVM DRSLVQGELV TASKAIIEKE YQPHVIVSTT GPNPFTTLTD 610 620 630 640 650 660 RELEEYRREV ERKQKGSEEN LDEAREQKEK SPPDQPAVPH PPPSTPIKLE EDLVPEPTTG 670 680 690 700 710 720 DDSDAATFKP TLPDLSPDEP SEALGFPMLE KEEEAHRPPS PTEAPTEASP EPAPDPAPVA 730 740 750 760 EEAAPSAVEE GAAADPGSDG SPGKSPSKKK KKFRTPSFLK KSKKKSDS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"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, MASS SPECTROMETRY.
[15]	"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.
[16]	"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 , 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.
IPI	IPI00019901. IPI00220158. IPI00253279.
PIR	S18207.
RefSeq	NP_001110.2. NM_001119.4. NP_054908.2. NM_014189.3. NP_054909.2. NM_014190.3. NP_789771.1. NM_176801.2.
UniGene	Hs.183706.
3D structure databases
DisProt	DP00240.
ProteinModelPortal	P35611.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35611. 5 interactions.
MINT	MINT-1499912.
STRING	9606.ENSP00000264758.
PTM databases
PhosphoSite	P35611.
Polymorphism databases
DMDM	12644231.
Proteomic databases
PaxDb	P35611.
PRIDE	P35611.
Protocols and materials databases
DNASU	118.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264758; ENSP00000264758; ENSG00000087274. ENST00000398129; ENSP00000381197; ENSG00000087274. ENST00000446856; ENSP00000399828; ENSG00000087274.
GeneID	118.
KEGG	hsa:118.
UCSC	uc003gfp.3. human. uc003gfq.3. human. uc003gfr.3. human.
Organism-specific databases
CTD	118.
GeneCards	GC04P002849.
HGNC	HGNC:243. ADD1.
HPA	CAB009794.
MIM	102680. gene.
neXtProt	NX_P35611.
PharmGKB	PA31.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0235.
HOVERGEN	HBG004180.
OMA	WTKEDGH.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	P35611.
Bgee	P35611.
CleanEx	HS_ADD1.
Genevestigator	P35611.
Family and domain databases
Gene3D	3.40.225.10. 1 hit.
InterPro	IPR001303. Aldolase_II/adducin_N. [Graphical view]
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
SMART	SM01007. Aldolase_II. 1 hit. [Graphical view]
SUPFAM	SSF53639. Aldolase_II_N. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	ADD1. human.
GenomeRNAi	118.
NextBio	459.
PMAP-CutDB	P35611.
SOURCE	Search...

Entry information

Entry name

ADDA_HUMAN

Accession

Primary (citable) accession number: P35611
Secondary accession number(s): A2A3P0 , 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:	May 1, 2013
This is version 132 of the entry and version 2 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.