Reviewed, UniProtKB/Swiss-Prot P0C1X8 (AAK1_RAT)

Names and origin

Protein names

Recommended name:
    AP2-associated protein kinase 1
    EC=2.7.11.-
Alternative name(s):
    Adaptor-associated kinase 1

Gene names

Name:

Aak1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	962 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphorylates the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2). May play a role in regulating aspects of clathrin-mediated endocytosis. Ref.2
Enzyme regulation	Stimulated by clathrin.
Subunit structure	Interacts with alpha-adaptin and AP-2. Ref.2
Subcellular location	Membrane; Peripheral membrane protein. Membrane › clathrin-coated pit. Cell membrane. Note: Active when found in clathrin-coated pits at the plasma membrane. Ref.2
Post-translational modification	Autophosphorylated.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Coated pit Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 962	962	AP2-associated protein kinase 1		PRO_0000250580
Regions
	Domain	46 – 314	269	Protein kinase
	Nucleotide binding	52 – 60	9	ATP By similarity
	Compositional bias	22 – 25	4	Poly-Gly
	Compositional bias	396 – 615	220	Gln-rich
	Compositional bias	659 – 664	6	Poly-Ala
Sites
	Active site	176	1	Proton acceptor By similarity
	Binding site	74	1	ATP By similarity
Amino acid modifications
	Modified residue	18	1	Phosphoserine By similarity
	Modified residue	21	1	Phosphoserine By similarity
	Modified residue	221	1	Phosphothreonine By similarity
	Modified residue	222	1	Phosphothreonine By similarity
	Modified residue	234	1	Phosphotyrosine By similarity
	Modified residue	235	1	Phosphoserine By similarity
	Modified residue	326	1	Phosphoserine By similarity
	Modified residue	353	1	Phosphothreonine By similarity
	Modified residue	388	1	Phosphothreonine By similarity
	Modified residue	440	1	Phosphothreonine By similarity
	Modified residue	607	1	Phosphothreonine By similarity
	Modified residue	619	1	Phosphoserine By similarity
	Modified residue	621	1	Phosphothreonine By similarity
	Modified residue	624	1	Phosphoserine By similarity
	Modified residue	625	1	Phosphoserine By similarity
	Modified residue	638	1	Phosphoserine By similarity
	Modified residue	641	1	Phosphothreonine By similarity
	Modified residue	653	1	Phosphoserine By similarity
	Modified residue	671	1	Phosphoserine By similarity
	Modified residue	677	1	Phosphoserine By similarity
	Modified residue	732	1	Phosphoserine By similarity
	Modified residue	938	1	Phosphoserine By similarity
	Modified residue	939	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C1X8-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 755E6F250C7A373E	FASTA	962	103,761
	10 20 30 40 50 60 MKKFFDSRRE QGSSGLGSGS SGGGGSSSGL GSGYIGRVFG IGRQQVTVDE VLAEGGFALV 70 80 90 100 110 120 FLVRTSNGVK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH KNIVGYIDSS INNVSSGDVW 130 140 150 160 170 180 EVLILMDFCR GGQVVNLMNQ RLQTGFTENE VLQIFCDTCE AVARLHQCKT PIIHRDLKVE 190 200 210 220 230 240 NILLHDRGHY VLCDFGSATN KFQNPQAEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT 250 260 270 280 290 300 TKADIWALGC LLYKLCYFTL PFGESQVAIC DGSFTIPDNS RYSQDMHCLI YMLEPDPDKR 310 320 330 340 350 360 PDIYQVSYFS FKLLKKECPV PNVQNSPIPT KLPEPVKASE AAVKKTQPKA RLTDPIPTTE 370 380 390 400 410 420 TSIAPRQRPK AGQTQPNPGI LPIQPALTPR KRATVQPLPQ ATGPSNQPSL LASVSQPKAQ 430 440 450 460 470 480 ATPSQPLQSS QPKQPQAPPT PQQTPAPQTQ GLPTQAQATP QHQQQLLLKQ QQQQQQQQQQ 490 500 510 520 530 540 QQPQQPTAPP QPSGTFYQQQ QPQQQQAQTQ QQFQAVHPAA QQSVTAQFPV VSQGGSQQQL 550 560 570 580 590 600 MQNFYQQQQQ QQQQQQQLMA QQAALQQKTA VVVPQPQAQP ATAPQAAAAQ EPQIQAPARQ 610 620 630 640 650 660 QPKVQTTPPP TIQGQKVGSL TPPSSPKTQR AGHRRILSDV THSAVFGVPA SKSTQLLHAA 670 680 690 700 710 720 AAEASLSKSK SATTTPSGSP RTSQQNVSNA SEGSTWNPFD DDNFSKLTAE ELLNKDFAKL 730 740 750 760 770 780 GEGKLPEKLG GSAESLIPGF QATQGDAFAT SSFSAGTAEK RKGGQAVDSG IPLLSVSDPF 790 800 810 820 830 840 IPLQVPDAPE KLIEGLKSPD TSLLLPDLLP MTDPFGSTSD AVIEKADAAV ESLIPGLEPP 850 860 870 880 890 900 VAQRLPSHTE SVTSNRTDSL TGEDSLLDCS LLSNPTADLL DEFAPIALSA STHKAAEDSN 910 920 930 940 950 960 LISGFGVAEG SEKVAEDEFD PIPVLITKNT QGGHSRNSSG SSESSLPNLA RSLLLVDQLI DL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed: 15057822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis." Conner S.D., Schmid S.L. J. Cell Biol. 156:921-929(2002) [PubMed: 11877461] [Abstract] Cited for: INTERACTION WITH ALPHA-ADAPTIN, SUBCELLULAR LOCATION, FUNCTION.
[3]	"AAK1-mediated micro2 phosphorylation is stimulated by assembled clathrin." Conner S.D., Schroter T., Schmid S.L. Traffic 4:885-890(2003) [PubMed: 14617351] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABR03032075 Genomic DNA. No translation available. AABR03032129 Genomic DNA. No translation available.
IPI	IPI00786812.
UniGene	Rn.203307
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P0C1X8.
Genome annotation databases
Ensembl	ENSRNOG00000018317. Rattus norvegicus. [Contig view]
Organism-specific databases
RGD	1305520. Aak1.
Phylogenomic databases
HOVERGEN	P0C1X8.
Gene expression databases
ArrayExpress	P0C1X8.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAK1_RAT

Accession

Primary (citable) accession number: P0C1X8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 3, 2006
Last modified:	June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)