Reviewed, UniProtKB/Swiss-Prot Q869N2 (PAKB_DICDI)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase pakB
      Short name=dPAKb
    EC=2.7.11.1
Alternative name(s):
    Myosin I heavy chain kinase

Gene names

Name:	pakB
Synonyms:	Ddpak, mihck
ORF Names:	DDB_G0276459

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	852 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Regulator of the myosin I component of the cytoskeleton: required for regulation of cytokinesis, phagocytosis and pinocytosis. Ref.1 Ref.2 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.2 Ref.6
Cofactor	Magnesium. Ref.1 Ref.2 Ref.6
Subunit structure	Interacts with rac1A, rac1B, rac1C, racA, racB, racC and racF1. Ref.6
Subcellular location	Membrane. Cytoplasm › cytoskeleton. Note: Mainly cytosolic but enriched at the leading edge of migrating cells and at macropinocytic and phagocytic cups, possibly due to binding to acidic phospholipids. Ref.2 Ref.6
Post-translational modification	Autophosphorylated at Ser-8. This may stimulate interaction with GTP-bound Rac family members which then further stimulates autophosphorylation and kinase activity. Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Ref.1 Ref.2 Ref.6 Contains 1 CRIB domain. Contains 1 protein kinase domain.
Sequence caution	The sequence CAA71240.1 differs from that shown. Reason: Frameshift at positions 124 and 132.

Ontologies

Keywords
Biological process	Phagocytosis
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	phagocytosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 Ref.2 (identifier: Q869N2-1)

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 Ref.3 (identifier: Q869N2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     413-440: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 852	852	Serine/threonine-protein kinase pakB		PRO_0000361051
Regions
	Domain	356 – 369	14	CRIB
	Domain	570 – 823	254	Protein kinase
	Nucleotide binding	576 – 584	9	ATP By similarity UniProtKB P28523
	Compositional bias	25 – 284	260	Pro-rich
	Compositional bias	115 – 146	32	Ser-rich
	Compositional bias	137 – 163	27	Asn-rich
	Compositional bias	285 – 313	29	Asn-rich
	Compositional bias	413 – 526	114	Gln-rich
	Compositional bias	492 – 507	16	Asn-rich
Sites
	Active site	691	1	Proton acceptor By similarity UniProtKB P28523
	Binding site	599	1	ATP By similarity UniProtKB P28523
Amino acid modifications
	Modified residue	8	1	Phosphoserine; by autocatalysis Ref.2
Natural variations
	Alternative sequence	413 – 440	28	Missing in isoform 2. Ref.3		VSP_052996
Experimental info
	Mutagenesis	4	1	S → A: No effect on autophosphorylation. Ref.2
	Sequence conflict	310	1	Missing in AAC71063. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 49C134B3DC077C1E	FASTA	852	93,123
	10 20 30 40 50 60 MEQSKRVSMM REKFEAQSNE AESSPPPNRK PPPPNKRVQT NGTSSLNSSG SSFVSPSPSP 70 80 90 100 110 120 SPSPQQPVKR PLPSPGVNKQ APPALPTQPR PQQQQPEIPV RPTTPTRTPP NLINSNGTSG 130 140 150 160 170 180 GSGFSSSSGN SGYSSSNNNN SNSNSSINMN GNHSNGLNGG SSNPVPMRKV SSPINIANGT 190 200 210 220 230 240 TPPPPPQPTP SQQPQQSPSS ASHNNTQHNI PSPPPLPNNK PKKLAPTAVP AGLGSIIGGP 250 260 270 280 290 300 KTPAISPGST SPSLGSSNGN IPISTTSTPI TPTPPISVPL ATSPNNSHKD SISNSNSNNN 310 320 330 340 350 360 NNNNNNNNNN SSNATTSPPS PPVSNVGNKQ DEEKKGFLSI FTNKKKNKDK KKEFSVGSPF 370 380 390 400 410 420 NVKHNIHVNY HSVTGFEGLP KEWEVILQSS GITREDVVEH SEVVIDVLDF HMQQQQQQAQ 430 440 450 460 470 480 QEQQALMQKQ MQQSGIPAHM LNNPKPPTIP IRDANKQPHN QLQPTPHQPP QHHHQQQPPQ 490 500 510 520 530 540 QHHHQQQQQQ HNNNNNNNNN NNNNNNNQQS AQQQSAGILS QQQEQQLEEM MCGGAYDDEQ 550 560 570 580 590 600 YDLNNQPLPD ETNVSLYDLV SQEDPTKLFG EGSTKIGEGA AGEVFVVTQL KTNNKVAIKK 610 620 630 640 650 660 MPLNQQNMKL IVTEIGIMKS CRHQNIIDYI DSYLVGDSLW VAMEFMGGGC LTEILEQFNS 670 680 690 700 710 720 VKLVEAQIAY VCAETLKGLA YIHSQHRIHR DIKSDNILLG SDGSVKLADF GYAAQLTKSK 730 740 750 760 770 780 QKRVTIVGTP YWMAPELIRG QNYDRKVDIW SLGIMAMEMA ESEPPYMSFP PLRALFLITT 790 800 810 820 830 840 KGIPDLKDQN KWSDDFKDFV KKCLDKDVEN RPEAKVLLNH PFLKTACNSN GLVPAIMEAK 850 KAKEAHSKFS IH
	Isoform 2. Checksum: 8582ACB04C467A8D	FASTA	824	89,860
	10 20 30 40 50 60 MEQSKRVSMM REKFEAQSNE AESSPPPNRK PPPPNKRVQT NGTSSLNSSG SSFVSPSPSP 70 80 90 100 110 120 SPSPQQPVKR PLPSPGVNKQ APPALPTQPR PQQQQPEIPV RPTTPTRTPP NLINSNGTSG 130 140 150 160 170 180 GSGFSSSSGN SGYSSSNNNN SNSNSSINMN GNHSNGLNGG SSNPVPMRKV SSPINIANGT 190 200 210 220 230 240 TPPPPPQPTP SQQPQQSPSS ASHNNTQHNI PSPPPLPNNK PKKLAPTAVP AGLGSIIGGP 250 260 270 280 290 300 KTPAISPGST SPSLGSSNGN IPISTTSTPI TPTPPISVPL ATSPNNSHKD SISNSNSNNN 310 320 330 340 350 360 NNNNNNNNNN SSNATTSPPS PPVSNVGNKQ DEEKKGFLSI FTNKKKNKDK KKEFSVGSPF 370 380 390 400 410 420 NVKHNIHVNY HSVTGFEGLP KEWEVILQSS GITREDVVEH SEVVIDVLDF HMLNNPKPPT 430 440 450 460 470 480 IPIRDANKQP HNQLQPTPHQ PPQHHHQQQP PQQHHHQQQQ QQHNNNNNNN NNNNNNNNNQ 490 500 510 520 530 540 QSAQQQSAGI LSQQQEQQLE EMMCGGAYDD EQYDLNNQPL PDETNVSLYD LVSQEDPTKL 550 560 570 580 590 600 FGEGSTKIGE GAAGEVFVVT QLKTNNKVAI KKMPLNQQNM KLIVTEIGIM KSCRHQNIID 610 620 630 640 650 660 YIDSYLVGDS LWVAMEFMGG GCLTEILEQF NSVKLVEAQI AYVCAETLKG LAYIHSQHRI 670 680 690 700 710 720 HRDIKSDNIL LGSDGSVKLA DFGYAAQLTK SKQKRVTIVG TPYWMAPELI RGQNYDRKVD 730 740 750 760 770 780 IWSLGIMAME MAESEPPYMS FPPLRALFLI TTKGIPDLKD QNKWSDDFKD FVKKCLDKDV 790 800 810 820 ENRPEAKVLL NHPFLKTACN SNGLVPAIME AKKAKEAHSK FSIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a Dictyostelium myosin I heavy chain kinase activated by Cdc42 and Rac." Lee S.-F., Egelhoff T.T., Mahasneh A., Cote G.P. J. Biol. Chem. 271:27044-27048(1996) [PubMed: 8900194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 242-250; 353-358 AND 364-370, FUNCTION, AUTOPHOSPHORYLATION. Strain: AX3.
[2]	"Regulation of the p21-activated kinase-related Dictyostelium myosin I heavy chain kinase by autophosphorylation, acidic phospholipids, and Ca2+-calmodulin." Lee S.-F., Mahasneh A., de la Roche M., Cote G.P. J. Biol. Chem. 273:27911-27917(1998) [PubMed: 9774403] [Abstract] Cited for: SEQUENCE REVISION TO N-TERMINUS, PROTEIN SEQUENCE OF 6-11 AND 740-745, FUNCTION, PHOSPHOLIPID-BINDING ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-4, AUTOPHOSPHORYLATION AT SER-8. Strain: AX3.
[3]	"Cloning and characterization of a ste20 homolog from Dictyostelium discoideum." Strom M. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: AX2.
[4]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed: 12097910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[5]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[6]	"Cellular distribution and functions of wild-type and constitutively activated Dictyostelium PakB." de la Roche M., Mahasneh A., Lee S.-F., Rivero F., Cote G.P. Mol. Biol. Cell 16:238-247(2005) [PubMed: 15509655] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAC1A; RAC1B; RAC1C; RACA; RACB; RACC AND RACF1, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U67716 mRNA. Translation: AAC71063.1. Y10158 mRNA. Translation: CAA71240.1. Frameshift. AC115606 Genomic DNA. Translation: AAO53078.1. AAFI02000015 Genomic DNA. Translation: EAL69183.1.
RefSeq	XP_643105.1.
3D structure databases
HSSP	HSSP built from PDB template 1F3M based on UniProtKB Q13153.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q869N2. 11 interactions.
Genome annotation databases
GeneID	3394245.
GenomeReviews	Gene locus pakB in contig CM000151_GR.
KEGG	ddi:DDB_0191345.
Organism-specific databases
dictyBase	DDB_G0276459. pakB.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000095. PAK_box_Rho_bd. IPR000719. Prot_kinase_cat_dom. IPR017442. Se/Thr_prot_kinase-like_dom. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00786. PBD. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00285. PBD. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS50108. CRIB. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PAKB_DICDI

Accession

Primary (citable) accession number: Q869N2
Secondary accession number(s): O00911, Q551M5, Q94488

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	June 1, 2003
Last modified:	November 24, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)