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Protein

AP2-associated protein kinase 1

Gene

AAK1

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

Functioni

Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Stimulated by clathrin.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741ATPPROSITE-ProRule annotation
Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi52 – 609ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. AP-2 adaptor complex binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. Notch binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. positive regulation of Notch signaling pathway Source: UniProtKB
  3. protein autophosphorylation Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
  5. protein stabilization Source: UniProtKB
  6. regulation of clathrin-mediated endocytosis Source: UniProtKB
  7. regulation of protein localization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ2M2I8.

Names & Taxonomyi

Protein namesi
Recommended name:
AP2-associated protein kinase 1 (EC:2.7.11.1)
Alternative name(s):
Adaptor-associated kinase 1
Gene namesi
Name:AAK1
Synonyms:KIAA1048
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:19679. AAK1.

Subcellular locationi

  1. Cell membrane By similarity; Peripheral membrane protein By similarity
  2. Membraneclathrin-coated pit By similarity

  3. Note: Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity).By similarity

GO - Cellular componenti

  1. cell leading edge Source: UniProtKB
  2. clathrin-coated vesicle Source: UniProtKB
  3. coated pit Source: UniProtKB-SubCell
  4. extrinsic component of plasma membrane Source: UniProtKB
  5. terminal bouton Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741K → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Does not interact with monoubiquitinated NOTCH1. 3 Publications
Mutagenesisi176 – 1761D → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. 2 Publications
Mutagenesisi777 – 7793DPF → AAA: Does not affect interaction with NOTCH1 but abolishes interaction with ESP15. 1 Publication

Organism-specific databases

PharmGKBiPA134990616.

Polymorphism and mutation databases

BioMutaiAAK1.
DMDMi300669613.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 961961AP2-associated protein kinase 1PRO_0000250578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei234 – 2341Phosphotyrosine1 Publication
Modified residuei235 – 2351Phosphoserine1 Publication
Modified residuei354 – 3541Phosphothreonine1 Publication
Modified residuei389 – 3891Phosphothreonine6 Publications
Modified residuei441 – 4411Phosphothreonine1 Publication
Modified residuei606 – 6061Phosphothreonine4 Publications
Modified residuei620 – 6201Phosphothreonine4 Publications
Modified residuei623 – 6231Phosphoserine2 Publications
Modified residuei624 – 6241Phosphoserine3 Publications
Modified residuei637 – 6371Phosphoserine7 Publications
Modified residuei650 – 6501Phosphoserine1 Publication
Modified residuei653 – 6531Phosphothreonine1 Publication
Modified residuei687 – 6871Phosphotyrosine1 Publication
Modified residuei731 – 7311Phosphoserine2 Publications

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ2M2I8.
PaxDbiQ2M2I8.
PRIDEiQ2M2I8.

PTM databases

PhosphoSiteiQ2M2I8.

Expressioni

Tissue specificityi

Detected in brain, heart and liver. Isoform 1 is the predominant isoform in brain.1 Publication

Gene expression databases

BgeeiQ2M2I8.
CleanExiHS_AAK1.
ExpressionAtlasiQ2M2I8. baseline and differential.
GenevestigatoriQ2M2I8.

Organism-specific databases

HPAiHPA017931.
HPA020289.

Interactioni

Subunit structurei

Interacts with alpha-adaptin, AP-2, clathrin, NUMB and EPS15 isoform 2. Interacts with membrane-bound activated NOTCH1 but not with the inactive full-length form of NOTCH1. Preferentially interacts with monoubiquitinated activated NOTCH1 compared to the non-ubiquitinated form.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP13A2Q9NQ112EBI-1383433,EBI-6308763

Protein-protein interaction databases

BioGridi116520. 3 interactions.
IntActiQ2M2I8. 3 interactions.
STRINGi9606.ENSP00000386456.

Structurei

Secondary structure

1
961
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 345Combined sources
Beta strandi38 – 414Combined sources
Beta strandi44 – 5310Combined sources
Beta strandi56 – 6510Combined sources
Beta strandi70 – 789Combined sources
Helixi81 – 9717Combined sources
Beta strandi106 – 11813Combined sources
Beta strandi120 – 1278Combined sources
Helixi134 – 1396Combined sources
Turni140 – 1445Combined sources
Helixi148 – 16619Combined sources
Beta strandi168 – 1703Combined sources
Helixi179 – 1813Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi189 – 1924Combined sources
Helixi205 – 2084Combined sources
Helixi210 – 22011Combined sources
Helixi223 – 2253Combined sources
Helixi228 – 2314Combined sources
Helixi242 – 25716Combined sources
Turni261 – 2644Combined sources
Helixi266 – 2716Combined sources
Helixi284 – 29310Combined sources
Turni298 – 3003Combined sources
Helixi304 – 31411Combined sources
Helixi339 – 3446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WSQX-ray1.95A/B29-345[»]
ProteinModelPortaliQ2M2I8.
SMRiQ2M2I8. Positions 37-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 315270Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 4231Gly-richAdd
BLAST
Compositional biasi397 – 614218Gln-richAdd
BLAST
Compositional biasi658 – 6636Poly-Ala

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00510000046552.
HOGENOMiHOG000232173.
HOVERGENiHBG080803.
InParanoidiQ2M2I8.
KOiK08853.
OMAiQAPIRQQ.
PhylomeDBiQ2M2I8.
TreeFamiTF317300.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q2M2I8-1) [UniParc]FASTAAdd to basket

Also known as: AAK1L

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
MKKFFDSRRE QGGSGLGSGS SGGGGSTSGL GSGYIGRVFG IGRQQVTVDE
60 70 80 90 100
VLAEGGFAIV FLVRTSNGMK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH
110 120 130 140 150
KNIVGYIDSS INNVSSGDVW EVLILMDFCR GGQVVNLMNQ RLQTGFTENE
160 170 180 190 200
VLQIFCDTCE AVARLHQCKT PIIHRDLKVE NILLHDRGHY VLCDFGSATN
210 220 230 240 250
KFQNPQTEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT TKADIWALGC
260 270 280 290 300
LLYKLCYFTL PFGESQVAIC DGNFTIPDNS RYSQDMHCLI RYMLEPDPDK
310 320 330 340 350
RPDIYQVSYF SFKLLKKECP IPNVQNSPIP AKLPEPVKAS EAAAKKTQPK
360 370 380 390 400
ARLTDPIPTT ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRATVQPPP
410 420 430 440 450
QAAGSSNQPG LLASVPQPKP QAPPSQPLPQ TQAKQPQAPP TPQQTPSTQA
460 470 480 490 500
QGLPAQAQAT PQHQQQLFLK QQQQQQQPPP AQQQPAGTFY QQQQAQTQQF
510 520 530 540 550
QAVHPATQKP AIAQFPVVSQ GGSQQQLMQN FYQQQQQQQQ QQQQQQLATA
560 570 580 590 600
LHQQQLMTQQ AALQQKPTMA AGQQPQPQPA AAPQPAPAQE PAIQAPVRQQ
610 620 630 640 650
PKVQTTPPPA VQGQKVGSLT PPSSPKTQRA GHRRILSDVT HSAVFGVPAS
660 670 680 690 700
KSTQLLQAAA AEASLNKSKS ATTTPSGSPR TSQQNVYNPS EGSTWNPFDD
710 720 730 740 750
DNFSKLTAEE LLNKDFAKLG EGKHPEKLGG SAESLIPGFQ STQGDAFATT
760 770 780 790 800
SFSAGTAEKR KGGQTVDSGL PLLSVSDPFI PLQVPDAPEK LIEGLKSPDT
810 820 830 840 850
SLLLPDLLPM TDPFGSTSDA VIEKADVAVE SLIPGLEPPV PQRLPSQTES
860 870 880 890 900
VTSNRTDSLT GEDSLLDCSL LSNPTTDLLE EFAPTAISAP VHKAAEDSNL
910 920 930 940 950
ISGFDVPEGS DKVAEDEFDP IPVLITKNPQ GGHSRNSSGS SESSLPNLAR
960
SLLLVDQLID L
Length:961
Mass (Da):103,885
Last modified:July 13, 2010 - v3
Checksum:i1FB44D0FDEF6CAD0
GO
Isoform 2 (identifier: Q2M2I8-2) [UniParc]FASTAAdd to basket

Also known as: AAK1S

The sequence of this isoform differs from the canonical sequence as follows:
     823-961: EKADVAVESL...LLLVDQLIDL → GKVIISVSSV...SPATPEAKAI

Show »
Length:863
Mass (Da):93,578
Checksum:i012198AEE90CC0E7
GO

Sequence cautioni

The sequence BAA83000.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591I → V.1 Publication
Corresponds to variant rs34535244 [ dbSNP | Ensembl ].
VAR_040348
Natural varianti509 – 5091K → Q.2 Publications
Corresponds to variant rs6715776 [ dbSNP | Ensembl ].
VAR_031129
Natural varianti533 – 5331Q → H.1 Publication
VAR_040349
Natural varianti603 – 6031V → A.1 Publication
Corresponds to variant rs56038532 [ dbSNP | Ensembl ].
VAR_040350
Natural varianti694 – 6941T → M.1 Publication
Corresponds to variant rs55889248 [ dbSNP | Ensembl ].
VAR_040351
Natural varianti725 – 7251P → T.1 Publication
Corresponds to variant rs35285785 [ dbSNP | Ensembl ].
VAR_040352
Natural varianti771 – 7711P → R.1 Publication
Corresponds to variant rs34422616 [ dbSNP | Ensembl ].
VAR_040353
Natural varianti835 – 8351G → D.1 Publication
VAR_040354

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei823 – 961139EKADV…QLIDL → GKVIISVSSVMHDMCACFKN DKYLVNQSLGNSPATPEAKA I in isoform 2. 2 PublicationsVSP_039459Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028971 mRNA. Translation: BAA83000.2. Different initiation.
AC092431 Genomic DNA. Translation: AAX88861.1.
AC079121 Genomic DNA. Translation: AAY14931.1.
AC136007 Genomic DNA. No translation available.
BC104842 mRNA. Translation: AAI04843.1.
BC111965 mRNA. Translation: AAI11966.1.
CCDSiCCDS1893.2. [Q2M2I8-1]
RefSeqiNP_055726.3. NM_014911.3.
UniGeneiHs.468878.

Genome annotation databases

EnsembliENST00000406297; ENSP00000385181; ENSG00000115977. [Q2M2I8-2]
ENST00000409085; ENSP00000386456; ENSG00000115977. [Q2M2I8-1]
GeneIDi22848.
KEGGihsa:22848.
UCSCiuc002sfp.2. human. [Q2M2I8-1]
uc010fdk.2. human. [Q2M2I8-2]

Polymorphism and mutation databases

BioMutaiAAK1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028971 mRNA. Translation: BAA83000.2. Different initiation.
AC092431 Genomic DNA. Translation: AAX88861.1.
AC079121 Genomic DNA. Translation: AAY14931.1.
AC136007 Genomic DNA. No translation available.
BC104842 mRNA. Translation: AAI04843.1.
BC111965 mRNA. Translation: AAI11966.1.
CCDSiCCDS1893.2. [Q2M2I8-1]
RefSeqiNP_055726.3. NM_014911.3.
UniGeneiHs.468878.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WSQX-ray1.95A/B29-345[»]
ProteinModelPortaliQ2M2I8.
SMRiQ2M2I8. Positions 37-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116520. 3 interactions.
IntActiQ2M2I8. 3 interactions.
STRINGi9606.ENSP00000386456.

Chemistry

BindingDBiQ2M2I8.
ChEMBLiCHEMBL3830.
GuidetoPHARMACOLOGYi1921.

PTM databases

PhosphoSiteiQ2M2I8.

Polymorphism and mutation databases

BioMutaiAAK1.
DMDMi300669613.

Proteomic databases

MaxQBiQ2M2I8.
PaxDbiQ2M2I8.
PRIDEiQ2M2I8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000406297; ENSP00000385181; ENSG00000115977. [Q2M2I8-2]
ENST00000409085; ENSP00000386456; ENSG00000115977. [Q2M2I8-1]
GeneIDi22848.
KEGGihsa:22848.
UCSCiuc002sfp.2. human. [Q2M2I8-1]
uc010fdk.2. human. [Q2M2I8-2]

Organism-specific databases

CTDi22848.
GeneCardsiGC02M069685.
H-InvDBHIX0161871.
HGNCiHGNC:19679. AAK1.
HPAiHPA017931.
HPA020289.
neXtProtiNX_Q2M2I8.
PharmGKBiPA134990616.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00510000046552.
HOGENOMiHOG000232173.
HOVERGENiHBG080803.
InParanoidiQ2M2I8.
KOiK08853.
OMAiQAPIRQQ.
PhylomeDBiQ2M2I8.
TreeFamiTF317300.

Enzyme and pathway databases

SignaLinkiQ2M2I8.

Miscellaneous databases

ChiTaRSiAAK1. human.
GeneWikiiAAK1.
GenomeRNAii22848.
NextBioi43313.
PROiQ2M2I8.

Gene expression databases

BgeeiQ2M2I8.
CleanExiHS_AAK1.
ExpressionAtlasiQ2M2I8. baseline and differential.
GenevestigatoriQ2M2I8.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel AAK1 splice variant functions at multiple steps of the endocytic pathway."
    Henderson D.M., Conner S.D.
    Mol. Biol. Cell 18:2698-2706(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CLATHRIN, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-509.
    Tissue: Brain.
  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. "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), VARIANT GLN-509.
    Tissue: Cerebellum.
  5. "Differential requirements for AP-2 in clathrin-mediated endocytosis."
    Conner S.D., Schmid S.L.
    J. Cell Biol. 162:773-779(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-74 AND ASP-176.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389 AND THR-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  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 THR-389; THR-441; SER-637 AND SER-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234; SER-235; THR-389; THR-606; THR-620; SER-623; SER-624 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "AAK1 regulates Numb function at an early step in clathrin-mediated endocytosis."
    Sorensen E.B., Conner S.D.
    Traffic 9:1791-1800(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUMB, MUTAGENESIS OF LYS-74 AND ASP-176.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-354; THR-389; SER-637; SER-650; TYR-687 AND SER-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 THR-389; THR-606; SER-637 AND THR-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-620; SER-623; SER-624 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "The adaptor-associated kinase 1, AAK1, is a positive regulator of the Notch pathway."
    Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J., Olivo-Marin J.C., Israel A.
    J. Biol. Chem. 286:18720-18730(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EPS15 AND NOTCH1, MUTAGENESIS OF LYS-74 AND 777-ASP--PHE-779.
  19. "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 THR-606; THR-620; SER-624 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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 THR-620, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-59; HIS-533; ALA-603; MET-694; THR-725; ARG-771 AND ASP-835.

Entry informationi

Entry nameiAAK1_HUMAN
AccessioniPrimary (citable) accession number: Q2M2I8
Secondary accession number(s): Q4ZFZ3, Q53RX6, Q9UPV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 13, 2010
Last modified: April 29, 2015
This is version 97 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. 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.