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Q69Z38

- PEAK1_MOUSE

UniProt

Q69Z38 - PEAK1_MOUSE

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Protein
Pseudopodium-enriched atypical kinase 1
Gene
Peak1, Kiaa2002, Sgk269
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Tyrosine kinase that may play a role in cell spreading and migration on fibronectin. May directly or indirectly affect phosphorylation levels of cytoskeleton-associated proteins MAPK1/ERK and PXN By similarity.

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1348 – 13481ATP By similarity
Active sitei1505 – 15051Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1308 – 13169ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. cell migration Source: UniProtKB
  2. peptidyl-tyrosine phosphorylation Source: GOC
  3. protein autophosphorylation Source: Ensembl
  4. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pseudopodium-enriched atypical kinase 1 (EC:2.7.10.2)
Alternative name(s):
Sugen kinase 269
Tyrosine-protein kinase SgK269
Gene namesi
Name:Peak1
Synonyms:Kiaa2002, Sgk269
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:2442366. Peak1.

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctionfocal adhesion
Note: Colocalizes with actin.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. focal adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17351735Pseudopodium-enriched atypical kinase 1
PRO_0000250590Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei282 – 2821Phosphoserine1 Publication
Modified residuei537 – 5371Phosphoserine By similarity
Modified residuei584 – 5841Phosphoserine By similarity
Modified residuei632 – 6321Phosphotyrosine2 Publications
Modified residuei638 – 6381Phosphotyrosine1 Publication

Post-translational modificationi

Autophosphorylated in vitro By similarity. Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ69Z38.
PaxDbiQ69Z38.
PRIDEiQ69Z38.

PTM databases

PhosphoSiteiQ69Z38.

Expressioni

Gene expression databases

BgeeiQ69Z38.
CleanExiMM_C230081A13RIK.
GenevestigatoriQ69Z38.

Interactioni

Subunit structurei

Interacts with BCAR1 and CRK By similarity.

Protein-protein interaction databases

IntActiQ69Z38. 1 interaction.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1302 – 1664363Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi145 – 1484Poly-Asn
Compositional biasi775 – 87298Pro-rich
Add
BLAST
Compositional biasi938 – 94710Poly-Glu
Compositional biasi963 – 9664Poly-Pro

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG115841.
GeneTreeiENSGT00460000041554.
HOVERGENiHBG093946.
InParanoidiQ69Z38.
KOiK17538.
OMAiGRFCYPE.
OrthoDBiEOG7B8S2Z.
TreeFamiTF333340.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q69Z38-1 [UniParc]FASTAAdd to Basket

« Hide

MSACNTFTEH VWKPGECKNC FKPKSLHQLP PDSEKTPITH GSGKTNANHS     50
NNHRVRSTGN FRPPVAKKPT IAVKPTMMVA DGQSVCGELS IQEHCENKPV 100
ILGWNQNKTS LSQKPLNNNS EGDAEGFGSD PQQCANNDSA QKISNNNNGL 150
TEVLKEIAGL EATPPVRGNE TNARETFLGR INDCYKRSLE RKIPPSCMTG 200
SMKDSQGKHV ILSGSAEVIS NEGGRFCYPE FSSGEESEED VLFSNMEEEH 250
ESWDESDEEL LAMEIRMRGQ PRFANFRANT LSPVRFFVSK KWNTIPLRNK 300
SLQRICAVDY DDSYDEILNG YEENSGVSYG QGSVQSTISS DCTSPGSSFT 350
EESRSETASS LSQKVCNGGI SPGNPGNSKD IAETESNFES PPGNNEEKDE 400
SLTSKSSVKV PETHKAVLAL RLQEKDGKIA VHTEKPESKA STDIAGQAVT 450
ISLVPVEEQT KPYRVVNLEQ PLCKPYTVVD VSAAMASEHL GRPKIKGSSS 500
TPNSPVTSPA LTPGQINAHL KKSSAIRYQE VWTSSTSPRQ KIPKIELSTG 550
GPGPNVPPRK NCHKSAPTSP TATNISSKTI PVKSPNLSEI KFNSYNNAGM 600
PPFPIIIHDE PSYARSSKNA IKVPIVINPN AYDNLAIYKS FLGTSGELSV 650
KEKTTSVISH TYEEIETESK VSDSTPSKLT DCPQAKGFSN STERKRGSVA 700
QKVQEFNNCL NRGQSSPQRS YSSTHSSPAK IQRPTQEPAG KTEGAQGSQV 750
PGSSSNSTRE KASAVLCQIV ASIQPPQTPP EAPQSSPKAC SVEELYAVPP 800
DADTTKSIPK NPPVRPKSLF TSQSSGEGEA HQTTESPTAK IQKDPSTKPV 850
TSPPSKLVTS AQSEPPPPFP PPRSTSSPYH ASNLLQRHFT NWTKPTSPTR 900
STEAESILHS EGSRRAADAK PKRWISFKSF FRRRKTDEEE EKEKEREKGK 950
LVGLDGTVIH MLPPPPVQRH HWFTEAKGEA SEKPAIVFMY RCDPDQGHLS 1000
VDQSKAGAEK GRAEEVLLRN SEEKKSSYLP SQIPDKACSR VTHEVAGELS 1050
PRDPRTPAGK QDGTSVTPTL PPPDLEREEE KDDTLDPTDV SPCSATYSNL 1100
GQSRAAMIPP KHPRHPKGAV DDAIAFGEKT DQEGLNASQP TPPPLPKKMI 1150
RANTEPISKD LQKAMESSLC VMANPTYDID PNWDASSAGS SISYELKGLD 1200
VESYESLERP LHKERPVPSA ANSISSLATL SVKDRFSNSM ESLSSRRGLS 1250
YRQTRSIQKP QRQALYRGLD NREEVVGKLR SLHTDALKRL AVKCEDLFMA 1300
GQKDQLRFGV DSWSDFRLTS DKPCCEAGDA VYYTASYAKD PLSNYAVKIC 1350
KSKAKESQQY YHSLAVRQSL PVHFNIQQDC GHFLAEVPSR LLPWEDPDAP 1400
EKAEDGTEDS EEEGKAETLG GNPEPCSETE PSQKENQRVT NRKQRSHVVV 1450
ITREVPHLTV ADFVRDSLAH HGNSPDLYER QVCLLLLQLC SGLEHLKPYH 1500
VTHCDLRLEN LLLVQHQPGG AAQGPSPADP CPTLACPTRL IVSNFSQAKQ 1550
KSHLVDPQIL RDQSRLAPEI ITATQYKKCD EFQTGILIYE MLHLPNPFDE 1600
NPELKEKEYT RTDLPRIPLR SPYSWGLQQL ASCLLNPNPS ERILISDAKG 1650
ILQCLLWGPR EDLFQIFTTS ATLAQKNALL QNWLDIKRTL LMIKFAEKSL 1700
DREGGISLED WLCAQYLAFA TTDSLSYIVK ILQYR 1735
Length:1,735
Mass (Da):191,097
Last modified:July 27, 2011 - v4
Checksum:i99A629E9061A0BF0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti560 – 5601K → R in BAC33490. 1 Publication
Sequence conflicti965 – 99127PPVQR…VFMYR → SSPAPSLVHRGQRRGQREAC YSLHVQV in BAC33490. 1 Publication
Add
BLAST
Sequence conflicti1026 – 103914SSYLP…DKACS → GDPVKMSLNGELCD in BAD32606. 1 Publication
Add
BLAST
Sequence conflicti1085 – 10851L → S in BAD32606. 1 Publication
Sequence conflicti1534 – 15363LAC → PTR in AAH26466. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC157474 Genomic DNA. No translation available.
AC159819 Genomic DNA. No translation available.
AC160935 Genomic DNA. No translation available.
AK048912 mRNA. Translation: BAC33490.1.
AK173328 mRNA. Translation: BAD32606.1.
BC026466 mRNA. Translation: AAH26466.1.
CCDSiCCDS52804.1.
RefSeqiNP_766512.2. NM_172924.3.
XP_006511230.1. XM_006511167.1.
XP_006511231.1. XM_006511168.1.
XP_006511232.1. XM_006511169.1.
UniGeneiMm.490331.

Genome annotation databases

EnsembliENSMUST00000061552; ENSMUSP00000109901; ENSMUSG00000074305.
GeneIDi244895.
KEGGimmu:244895.
UCSCiuc009psz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC157474 Genomic DNA. No translation available.
AC159819 Genomic DNA. No translation available.
AC160935 Genomic DNA. No translation available.
AK048912 mRNA. Translation: BAC33490.1 .
AK173328 mRNA. Translation: BAD32606.1 .
BC026466 mRNA. Translation: AAH26466.1 .
CCDSi CCDS52804.1.
RefSeqi NP_766512.2. NM_172924.3.
XP_006511230.1. XM_006511167.1.
XP_006511231.1. XM_006511168.1.
XP_006511232.1. XM_006511169.1.
UniGenei Mm.490331.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q69Z38. 1 interaction.

PTM databases

PhosphoSitei Q69Z38.

Proteomic databases

MaxQBi Q69Z38.
PaxDbi Q69Z38.
PRIDEi Q69Z38.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000061552 ; ENSMUSP00000109901 ; ENSMUSG00000074305 .
GeneIDi 244895.
KEGGi mmu:244895.
UCSCi uc009psz.2. mouse.

Organism-specific databases

CTDi 79834.
MGIi MGI:2442366. Peak1.
Rougei Search...

Phylogenomic databases

eggNOGi NOG115841.
GeneTreei ENSGT00460000041554.
HOVERGENi HBG093946.
InParanoidi Q69Z38.
KOi K17538.
OMAi GRFCYPE.
OrthoDBi EOG7B8S2Z.
TreeFami TF333340.

Miscellaneous databases

NextBioi 386480.
PROi Q69Z38.
SOURCEi Search...

Gene expression databases

Bgeei Q69Z38.
CleanExi MM_C230081A13RIK.
Genevestigatori Q69Z38.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-991.
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1026-1735.
    Tissue: Embryonic intestine.
  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] OF 1534-1735.
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-632 AND TYR-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CSK.

Entry informationi

Entry nameiPEAK1_MOUSE
AccessioniPrimary (citable) accession number: Q69Z38
Secondary accession number(s): E9QKY2, Q8BX56, Q8R365
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 82 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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