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Protein

AP-2 complex subunit alpha-1

Gene

AP2A1

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

Functioni

Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_121399. MHC class II antigen presentation.
REACT_12435. Retrograde neurotrophin signalling.
REACT_12484. EGFR downregulation.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_22365. Recycling pathway of L1.
REACT_263890. WNT5A-dependent internalization of FZD4.
REACT_264198. EPH-ephrin mediated repulsion of cells.
SignaLinkiO95782.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-2 complex subunit alpha-1
Alternative name(s):
100 kDa coated vesicle protein A
Adaptor protein complex AP-2 subunit alpha-1
Adaptor-related protein complex 2 subunit alpha-1
Alpha-adaptin A
Alpha1-adaptin
Clathrin assembly protein complex 2 alpha-A large chain
Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit
Gene namesi
Name:AP2A1
Synonyms:ADTAA, CLAPA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:561. AP2A1.

Subcellular locationi

GO - Cellular componenti

  • AP-2 adaptor complex Source: UniProtKB
  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • clathrin-coated endocytic vesicle membrane Source: Reactome
  • clathrin coat of trans-Golgi network vesicle Source: UniProtKB
  • cytosol Source: Reactome
  • endocytic vesicle membrane Source: Reactome
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24852.

Polymorphism and mutation databases

BioMutaiAP2A1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 977976AP-2 complex subunit alpha-1PRO_0000193730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei626 – 6261Phosphoserine1 Publication
Modified residuei652 – 6521Phosphoserine1 Publication
Modified residuei653 – 6531Phosphothreonine2 Publications
Modified residuei655 – 6551Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95782.
PaxDbiO95782.
PRIDEiO95782.

PTM databases

PhosphoSiteiO95782.

Expressioni

Tissue specificityi

Isoform A expressed in forebrain, skeletal muscle, spinal cord, cerebellum, salivary gland, heart and colon. Isoform B is widely expressed in tissues and also in breast cancer and in prostate carcinoma cells.

Gene expression databases

BgeeiO95782.
CleanExiHS_AP2A1.
ExpressionAtlasiO95782. baseline and differential.
GenevisibleiO95782. HS.

Organism-specific databases

HPAiCAB004306.

Interactioni

Subunit structurei

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts with SGIP1 (By similarity). Interacts with HIP1 and RAB11FIP2. Interacts with SLC12A5. Interacts with clathrin.By similarity2 Publications

Protein-protein interaction databases

BioGridi106669. 61 interactions.
IntActiO95782. 25 interactions.
MINTiMINT-5002322.
STRINGi9606.ENSP00000351926.

Structurei

3D structure databases

ProteinModelPortaliO95782.
SMRiO95782. Positions 3-621, 746-977.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG303101.
GeneTreeiENSGT00550000074757.
HOGENOMiHOG000170596.
HOVERGENiHBG050518.
InParanoidiO95782.
KOiK11824.
OMAiLQSHLNV.
OrthoDBiEOG7GQXV2.
PhylomeDBiO95782.
TreeFamiTF300308.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. AP2_complex_asu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR013038. Clathrin_a-adaptin_app_Ig-like.
IPR003164. Clathrin_a-adaptin_app_sub_C.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 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

Isoform A (identifier: O95782-1) [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
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL
60 70 80 90 100
DGYSKKKYVC KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV
110 120 130 140 150
LVNSNSELIR LINNAIKNDL ASRNPTFMCL ALHCIANVGS REMGEAFAAD
160 170 180 190 200
IPRILVAGDS MDSVKQSAAL CLLRLYKASP DLVPMGEWTA RVVHLLNDQH
210 220 230 240 250
MGVVTAAVSL ITCLCKKNPD DFKTCVSLAV SRLSRIVSSA STDLQDYTYY
260 270 280 290 300
FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV
310 320 330 340 350
QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL
360 370 380 390 400
ESMCTLASSE FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS
410 420 430 440 450
NAKQIVSEML RYLETADYAI REEIVLKVAI LAEKYAVDYS WYVDTILNLI
460 470 480 490 500
RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA KTVFEALQAP ACHENMVKVG
510 520 530 540 550
GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL LLSTYIKFIN
560 570 580 590 600
LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE
610 620 630 640 650
EMPPFPERES SILAKLKRKK GPGAGSALDD GRRDPSSNDI NGGMEPTPST
660 670 680 690 700
VSTPSPSADL LGLRAAPPPA APPASAGAGN LLVDVFDGPA AQPSLGPTPE
710 720 730 740 750
EAFLSELEPP APESPMALLA DPAPAADPGP EDIGPPIPEA DELLNKFVCK
760 770 780 790 800
NNGVLFENQL LQIGVKSEFR QNLGRMYLFY GNKTSVQFQN FSPTVVHPGD
810 820 830 840 850
LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL SVRFRYGGAP
860 870 880 890 900
QALTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPQQEAQ KIFKANHPMD
910 920 930 940 950
AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ
960 970
AQMYRLTLRT SKEPVSRHLC ELLAQQF
Length:977
Mass (Da):107,546
Last modified:November 3, 2009 - v3
Checksum:iD9FB569E7EDDF6ED
GO
Isoform B (identifier: O95782-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     706-727: Missing.

Show »
Length:955
Mass (Da):105,361
Checksum:iFCE1AEC87453B17F
GO

Sequence cautioni

The sequence AAD15564.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti804 – 8041Q → H in AAL11039 (PubMed:12036598).Curated
Sequence conflicti804 – 8041Q → H in AAL11040 (PubMed:12036598).Curated
Sequence conflicti924 – 97754ENFVG…LAQQF → GDREDTRVWGMPGTFLRPFV FLFLFICCCLHSGGLGGVPL PPFPPQAQRGEGPGKWMSPP LPPHPVVAPPTPSPSRGCVL L in AAH14214 (PubMed:15489334).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti270 – 2701P → L.1 Publication
Corresponds to variant rs17851121 [ dbSNP | Ensembl ].
VAR_060544

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei706 – 72722Missing in isoform B. 2 PublicationsVSP_000161Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF289221 Genomic DNA. Translation: AAL11039.1.
AF289221 Genomic DNA. Translation: AAL11040.1.
AL136925 mRNA. Translation: CAB66859.1.
AC006942 Genomic DNA. Translation: AAD15564.1. Sequence problems.
AC011495 Genomic DNA. No translation available.
AC098783 Genomic DNA. No translation available.
BC014214 mRNA. Translation: AAH14214.1.
CCDSiCCDS46148.1. [O95782-1]
CCDS46149.1. [O95782-2]
RefSeqiNP_055018.2. NM_014203.2. [O95782-1]
NP_570603.2. NM_130787.2. [O95782-2]
UniGeneiHs.467125.

Genome annotation databases

EnsembliENST00000354293; ENSP00000346246; ENSG00000196961. [O95782-2]
ENST00000359032; ENSP00000351926; ENSG00000196961. [O95782-1]
GeneIDi160.
KEGGihsa:160.
UCSCiuc002ppn.3. human. [O95782-1]
uc002ppo.3. human. [O95782-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF289221 Genomic DNA. Translation: AAL11039.1.
AF289221 Genomic DNA. Translation: AAL11040.1.
AL136925 mRNA. Translation: CAB66859.1.
AC006942 Genomic DNA. Translation: AAD15564.1. Sequence problems.
AC011495 Genomic DNA. No translation available.
AC098783 Genomic DNA. No translation available.
BC014214 mRNA. Translation: AAH14214.1.
CCDSiCCDS46148.1. [O95782-1]
CCDS46149.1. [O95782-2]
RefSeqiNP_055018.2. NM_014203.2. [O95782-1]
NP_570603.2. NM_130787.2. [O95782-2]
UniGeneiHs.467125.

3D structure databases

ProteinModelPortaliO95782.
SMRiO95782. Positions 3-621, 746-977.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106669. 61 interactions.
IntActiO95782. 25 interactions.
MINTiMINT-5002322.
STRINGi9606.ENSP00000351926.

PTM databases

PhosphoSiteiO95782.

Polymorphism and mutation databases

BioMutaiAP2A1.

Proteomic databases

MaxQBiO95782.
PaxDbiO95782.
PRIDEiO95782.

Protocols and materials databases

DNASUi160.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354293; ENSP00000346246; ENSG00000196961. [O95782-2]
ENST00000359032; ENSP00000351926; ENSG00000196961. [O95782-1]
GeneIDi160.
KEGGihsa:160.
UCSCiuc002ppn.3. human. [O95782-1]
uc002ppo.3. human. [O95782-2]

Organism-specific databases

CTDi160.
GeneCardsiGC19P050270.
HGNCiHGNC:561. AP2A1.
HPAiCAB004306.
MIMi601026. gene.
neXtProtiNX_O95782.
PharmGKBiPA24852.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG303101.
GeneTreeiENSGT00550000074757.
HOGENOMiHOG000170596.
HOVERGENiHBG050518.
InParanoidiO95782.
KOiK11824.
OMAiLQSHLNV.
OrthoDBiEOG7GQXV2.
PhylomeDBiO95782.
TreeFamiTF300308.

Enzyme and pathway databases

ReactomeiREACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_121399. MHC class II antigen presentation.
REACT_12435. Retrograde neurotrophin signalling.
REACT_12484. EGFR downregulation.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_22365. Recycling pathway of L1.
REACT_263890. WNT5A-dependent internalization of FZD4.
REACT_264198. EPH-ephrin mediated repulsion of cells.
SignaLinkiO95782.

Miscellaneous databases

ChiTaRSiAP2A1. human.
GeneWikiiAdaptor-related_protein_complex_2,_alpha_1.
GenomeRNAii160.
NextBioi637.
PROiO95782.
SOURCEiSearch...

Gene expression databases

BgeeiO95782.
CleanExiHS_AP2A1.
ExpressionAtlasiO95782. baseline and differential.
GenevisibleiO95782. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. AP2_complex_asu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR013038. Clathrin_a-adaptin_app_Ig-like.
IPR003164. Clathrin_a-adaptin_app_sub_C.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, physical mapping and structural characterization of the human alpha(A)-adaptin gene."
    Scorilas A., Levesque M.A., Ashworth L.K., Diamandis E.P.
    Gene 289:191-199(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Tissue: Uterus.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [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 B), VARIANT LEU-270.
    Tissue: Muscle.
  5. "The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis."
    Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R., Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H., Wanker E.E.
    Hum. Mol. Genet. 10:1807-1817(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIP1.
  6. "Rab11-FIP2, an adaptor protein connecting cellular components involved in internalization and recycling of epidermal growth factor receptors."
    Cullis D.N., Philip B., Baleja J.D., Feig L.A.
    J. Biol. Chem. 277:49158-49166(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB11FIP2.
  7. "Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network."
    Nakatsu F., Ohno H.
    Cell Struct. Funct. 28:419-429(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
  8. "Adaptors for clathrin coats: structure and function."
    Owen D.J., Collins B.M., Evans P.R.
    Annu. Rev. Cell Dev. Biol. 20:153-191(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
  9. "The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway."
    Lau A.W., Chou M.M.
    J. Cell Sci. 121:4008-4017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652; THR-653 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: 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 THR-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAP2A1_HUMAN
AccessioniPrimary (citable) accession number: O95782
Secondary accession number(s): Q96CI7
, Q96PP6, Q96PP7, Q9H070
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 3, 2009
Last modified: June 24, 2015
This is version 142 of the entry and version 3 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 19
    Human chromosome 19: 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.