KIFC1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KIFC1_MOUSE
• UniProt AC: Q9QWT9
• Protein Name: Kinesin-like protein KIFC1
• Gene Name: Kifc1 {ECO:0000312|MGI:MGI:109596}
• Organism: Mus musculus (Mouse).
• Sequence Length: 674
• Subcellular Localization: Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Early endosome . Associated with nucleus during interphase, centrosomes in early and spindle in later mitosis.
• Protein Description: Minus end-directed microtubule-dependent motor required for bipolar spindle formation. [PubMed: 16638812 May contribute to movement of early endocytic vesicles]
• Protein Sequence: MDVQAQRPPLLEVKRNVELKAALVKSSSRVPLSASRLKRGPDQMEDALEPAKKRTRVMGAVTKVDTSRPRGPLLSTVSQTQGHTAAQKGPKKTGPRGCSAIGTVLRSQKPVPAAPAQKPGTSTAPVVVGKRAGKRPAWDLKGQLCDLNEELKRYREKTQTLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQERRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNIRVFCRVRPVLEGESTPSPGFLVFPPGPAGPSDPPTGLSLSRSDDRRSTLTGAPAPTVRHDFSFDRVFPPGSKQEEVFEEIAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDPQLEGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYNETVRDLLATGPRKGQGGECEIRRASPGSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISGEHAARGLQCGAPLNLVDLAGSERLDPGLHLGPGERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIGTAQANKK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Phosphorylation	AALVKSSSRVPLSAS HHHHHCCCCCCCCHH	44.37	-
33	Phosphorylation	SSSRVPLSASRLKRG CCCCCCCCHHHHCCC	20.37	29514104
35	Phosphorylation	SRVPLSASRLKRGPD CCCCCCHHHHCCCCC	34.47	19367708
66	Phosphorylation	GAVTKVDTSRPRGPL EEEEEECCCCCCCCC	29.62	-
67	Phosphorylation	AVTKVDTSRPRGPLL EEEEECCCCCCCCCC	35.50	25177544
103	Phosphorylation	RGCSAIGTVLRSQKP CCCCCHHHHHCCCCC	15.39	-
264	Phosphorylation	QATEAALSSSQEEVV HHHHHHHCCCCCEEE	24.18	23140645
277	Phosphorylation	VVCLRQKTEAQVTLL EEEEECCCHHHEEEE	28.37	-
350	Phosphorylation	SDPPTGLSLSRSDDR CCCCCCCCCCCCCCC	26.16	29899451
354	Phosphorylation	TGLSLSRSDDRRSTL CCCCCCCCCCCHHCC	40.25	-
359	Phosphorylation	SRSDDRRSTLTGAPA CCCCCCHHCCCCCCC	28.76	28066266
360	Phosphorylation	RSDDRRSTLTGAPAP CCCCCHHCCCCCCCC	26.91	25266776
362	Phosphorylation	DDRRSTLTGAPAPTV CCCHHCCCCCCCCCC	31.24	28066266
480	Ubiquitination	LLATGPRKGQGGECE HHHCCCCCCCCCCEE	59.73	-
492	Phosphorylation	ECEIRRASPGSEELT CEEEEECCCCCCEEE	28.16	26824392
495	Phosphorylation	IRRASPGSEELTVTN EEECCCCCCEEEEEE	31.14	25266776
499	Phosphorylation	SPGSEELTVTNARYV CCCCCEEEEEEEEEE	28.67	25168779
501	Phosphorylation	GSEELTVTNARYVPV CCCEEEEEEEEEEEC	20.23	25777480

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of KIFC1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KIFC1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KIFC1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAGP1_HUMAN	RANGAP1	physical	20360068
IMB1_HUMAN	KPNB1	physical	20360068
IMA1_HUMAN	KPNA2	physical	20360068
TPR_HUMAN	TPR	physical	20360068
RBP2_HUMAN	RANBP2	physical	20360068
NUP50_HUMAN	NUP50	physical	20360068
NU153_HUMAN	NUP153	physical	20360068

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.
PubMed: 19367708