Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kinesin-like protein KIFC1

Gene

Kifc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Minus end-directed microtubule-dependent motor required for bipolar spindle formation (PubMed:16638812). May contribute to movement of early endocytic vesicles (PubMed:17360972). Regulates cilium formation and structure (PubMed:23807208).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi411 – 4188ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent microtubule motor activity, minus-end-directed Source: MGI
  • microtubule motor activity Source: MGI

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • minus-end-directed vesicle transport along microtubule Source: MGI
  • mitotic metaphase plate congression Source: UniProtKB
  • mitotic spindle assembly Source: UniProtKB
  • negative regulation of centrosome duplication Source: MGI
  • vesicle transport along microtubule Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIFC1
Gene namesi
Name:Kifc1Imported
Synonyms:Kifc41 Publication, Kifc5a1 Publication, Kifc5b1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:109596. Kifc1.

Subcellular locationi

GO - Cellular componenti

  • early endosome Source: UniProtKB-SubCell
  • endocytic vesicle Source: MGI
  • kinesin complex Source: GO_Central
  • membrane Source: MGI
  • microtubule Source: UniProtKB-KW
  • mitotic spindle Source: MGI
  • nucleus Source: MGI
  • spindle pole centrosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endosome, Microtubule, Nucleus

Pathology & Biotechi

Disruption phenotypei

Centrosome amplification as well as multipolar spindles. Cells overexpressing Kifc1 show a single microtubule aster and growth arrest in prometaphase.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 674674Kinesin-like protein KIFC1PRO_0000302089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei360 – 3601PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9QWT9.
MaxQBiQ9QWT9.
PaxDbiQ9QWT9.
PeptideAtlasiQ9QWT9.
PRIDEiQ9QWT9.

PTM databases

iPTMnetiQ9QWT9.
PhosphoSiteiQ9QWT9.

Expressioni

Tissue specificityi

Highly expressed in E14 embryos, spleen and NIH3T3 cells. Also expressed in testis, brain, lung, kidney and cultured astrocytes. Very low levels in skeletal muscle and heart.2 Publications

Developmental stagei

Highly expressed in hippocampus of E13 embryos declining to low levels by E18 and to undetectable levels in juvenile and adult hippocampus.1 Publication

Gene expression databases

BgeeiQ9QWT9.
CleanExiMM_KIFC1.
ExpressionAtlasiQ9QWT9. baseline and differential.
GenevisibleiQ9QWT9. MM.

Interactioni

Subunit structurei

Binds NUBP1 and NUBP2 (PubMed:16638812). Interacts with PPP1R42 (PubMed:18237440).2 Publications

Protein-protein interaction databases

BioGridi200952. 7 interactions.
224976. 49 interactions.
IntActiQ9QWT9. 9 interactions.
STRINGi10090.ENSMUSP00000134572.

Structurei

3D structure databases

ProteinModelPortaliQ9QWT9.
SMRiQ9QWT9. Positions 269-664.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini311 – 664354Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili146 – 315170Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0239. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00550000074610.
HOVERGENiHBG001080.
InParanoidiQ9QWT9.
KOiK10405.
OMAiMSRLPVM.
OrthoDBiEOG72G16X.
PhylomeDBiQ9QWT9.
TreeFamiTF105237.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 3 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q9QWT9-1) [UniParc]FASTAAdd to basket

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
MDVQAQRPPL LEVKRNVELK AALVKSSSRV PLSASRLKRG PDQMEDALEP
60 70 80 90 100
AKKRTRVMGA VTKVDTSRPR GPLLSTVSQT QGHTAAQKGP KKTGPRGCSA
110 120 130 140 150
IGTVLRSQKP VPAAPAQKPG TSTAPVVVGK RAGKRPAWDL KGQLCDLNEE
160 170 180 190 200
LKRYREKTQT LELENRGLRE QLREVQEQAT TLGTERNTLE GELASVRSRA
210 220 230 240 250
EQDQQRLETL SARVLELEEC LGTRERLLQE LQGERLQLQE ERSTLSTQLE
260 270 280 290 300
EQERRFQATE AALSSSQEEV VCLRQKTEAQ VTLLAEQGDR LYGLEMERRR
310 320 330 340 350
LHNQLQELKG NIRVFCRVRP VLEGESTPSP GFLVFPPGPA GPSDPPTGLS
360 370 380 390 400
LSRSDDRRST LTGAPAPTVR HDFSFDRVFP PGSKQEEVFE EIAMLVQSAL
410 420 430 440 450
DGYPVCIFAY GQTGSGKTFT MEGGPRGDPQ LEGLIPRAMR HLFSVAQEMS
460 470 480 490 500
GQGWTYSFVA SYVEIYNETV RDLLATGPRK GQGGECEIRR ASPGSEELTV
510 520 530 540 550
TNARYVPVSC EKEVEALLHL AHQNRAVAHT AQNKRSSRSH SVFQLQISGE
560 570 580 590 600
HAARGLQCGA PLNLVDLAGS ERLDPGLHLG PGERDRLRET QAINSSLSTL
610 620 630 640 650
GLVIMALSNK ESHVPYRNSK LTYLLQNSLG GSAKMLMFVN ISPLEENVSE
660 670
SLNSLRFASK VNQCVIGTAQ ANKK
Length:674
Mass (Da):74,153
Last modified:September 11, 2007 - v2
Checksum:iA99B6FB6F9BC1B03
GO
Isoform 21 Publication (identifier: Q9QWT9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Show »
Length:631
Mass (Da):69,401
Checksum:iE74F26745611BCB4
GO
Isoform 31 Publication (identifier: Q9QWT9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.
     203-222: Missing.

Show »
Length:611
Mass (Da):67,117
Checksum:iBF5B0CA4DE84A5C3
GO

Sequence cautioni

The sequence BAA19676.1 differs from that shown. Reason: Frameshift at positions 223 and 244. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011I → V in BAA19676 (PubMed:9115736).Curated
Sequence conflicti101 – 1011I → V in AAF34646 (PubMed:10775188).Curated
Sequence conflicti101 – 1011I → V in CAJ19646 (PubMed:16638812).Curated
Sequence conflicti101 – 1011I → V in AAH03753 (PubMed:15489334).Curated
Sequence conflicti101 – 1011I → V in AAH57162 (PubMed:15489334).Curated
Sequence conflicti101 – 1011I → V in AAI00329 (PubMed:15489334).Curated
Sequence conflicti111 – 1111V → A in BAA19676 (PubMed:9115736).Curated
Sequence conflicti111 – 1111V → A in AAF34646 (PubMed:10775188).Curated
Sequence conflicti111 – 1111V → A in CAJ19646 (PubMed:16638812).Curated
Sequence conflicti111 – 1111V → A in AAH03753 (PubMed:15489334).Curated
Sequence conflicti111 – 1111V → A in AAH57162 (PubMed:15489334).Curated
Sequence conflicti111 – 1111V → A in AAI00329 (PubMed:15489334).Curated
Sequence conflicti160 – 1601T → M in BAA19676 (PubMed:9115736).Curated
Sequence conflicti160 – 1601T → M in AAF34646 (PubMed:10775188).Curated
Sequence conflicti160 – 1601T → M in CAJ19646 (PubMed:16638812).Curated
Sequence conflicti253 – 2531E → K in BAA19676 (PubMed:9115736).Curated
Sequence conflicti253 – 2531E → K in AAF34646 (PubMed:10775188).Curated
Sequence conflicti253 – 2531E → K in CAJ19646 (PubMed:16638812).Curated
Sequence conflicti253 – 2531E → K in AAH03753 (PubMed:15489334).Curated
Sequence conflicti271 – 2711V → L in AAH57162 (PubMed:15489334).Curated
Sequence conflicti315 – 3151F → L in CAJ19646 (PubMed:16638812).Curated
Sequence conflicti323 – 3231E → A in BAA19676 (PubMed:9115736).Curated
Sequence conflicti323 – 3231E → A in AAF34646 (PubMed:10775188).Curated
Sequence conflicti323 – 3231E → A in CAJ19646 (PubMed:16638812).Curated
Sequence conflicti323 – 3231E → A in AAH03753 (PubMed:15489334).Curated
Sequence conflicti323 – 3231E → A in AAI00329 (PubMed:15489334).Curated
Sequence conflicti345 – 3451P → L in AAI00329 (PubMed:15489334).Curated
Sequence conflicti432 – 4321E → A in BAC38230 (PubMed:16141072).Curated
Sequence conflicti478 – 4781P → L in BAA19676 (PubMed:9115736).Curated
Sequence conflicti503 – 5031A → V in BAA19676 (PubMed:9115736).Curated
Sequence conflicti566 – 5661D → G in AAF34646 (PubMed:10775188).Curated
Sequence conflicti578 – 5781H → P in BAC38230 (PubMed:16141072).Curated
Sequence conflicti619 – 6191S → R in BAA19676 (PubMed:9115736).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform 2 and isoform 3. 2 PublicationsVSP_052526Add
BLAST
Alternative sequencei203 – 22220Missing in isoform 3. 1 PublicationVSP_052527Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49544 mRNA. Translation: BAA19676.1. Frameshift.
AF221102 mRNA. Translation: AAF34646.1.
AM051187 mRNA. Translation: CAJ19646.1.
AF110520 Genomic DNA. Translation: AAC97970.1.
BC003753 mRNA. Translation: AAH03753.1.
BC057162 mRNA. Translation: AAH57162.1.
BC100328 mRNA. Translation: AAI00329.1.
AK081484 mRNA. Translation: BAC38230.1.
AF013117 mRNA. Translation: AAC39966.1.
CCDSiCCDS57065.1. [Q9QWT9-1]
RefSeqiNP_001182227.1. NM_001195298.1. [Q9QWT9-1]
NP_444403.2. NM_053173.2.
UniGeneiMm.335713.
Mm.491138.

Genome annotation databases

EnsembliENSMUST00000114361; ENSMUSP00000110001; ENSMUSG00000079553. [Q9QWT9-3]
ENSMUST00000173492; ENSMUSP00000134572; ENSMUSG00000079553. [Q9QWT9-1]
GeneIDi100502766.
16580.
KEGGimmu:100502766.
mmu:16580.
UCSCiuc008bzw.2. mouse. [Q9QWT9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49544 mRNA. Translation: BAA19676.1. Frameshift.
AF221102 mRNA. Translation: AAF34646.1.
AM051187 mRNA. Translation: CAJ19646.1.
AF110520 Genomic DNA. Translation: AAC97970.1.
BC003753 mRNA. Translation: AAH03753.1.
BC057162 mRNA. Translation: AAH57162.1.
BC100328 mRNA. Translation: AAI00329.1.
AK081484 mRNA. Translation: BAC38230.1.
AF013117 mRNA. Translation: AAC39966.1.
CCDSiCCDS57065.1. [Q9QWT9-1]
RefSeqiNP_001182227.1. NM_001195298.1. [Q9QWT9-1]
NP_444403.2. NM_053173.2.
UniGeneiMm.335713.
Mm.491138.

3D structure databases

ProteinModelPortaliQ9QWT9.
SMRiQ9QWT9. Positions 269-664.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200952. 7 interactions.
224976. 49 interactions.
IntActiQ9QWT9. 9 interactions.
STRINGi10090.ENSMUSP00000134572.

PTM databases

iPTMnetiQ9QWT9.
PhosphoSiteiQ9QWT9.

Proteomic databases

EPDiQ9QWT9.
MaxQBiQ9QWT9.
PaxDbiQ9QWT9.
PeptideAtlasiQ9QWT9.
PRIDEiQ9QWT9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114361; ENSMUSP00000110001; ENSMUSG00000079553. [Q9QWT9-3]
ENSMUST00000173492; ENSMUSP00000134572; ENSMUSG00000079553. [Q9QWT9-1]
GeneIDi100502766.
16580.
KEGGimmu:100502766.
mmu:16580.
UCSCiuc008bzw.2. mouse. [Q9QWT9-1]

Organism-specific databases

CTDi16580.
3833.
MGIiMGI:109596. Kifc1.

Phylogenomic databases

eggNOGiKOG0239. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00550000074610.
HOVERGENiHBG001080.
InParanoidiQ9QWT9.
KOiK10405.
OMAiMSRLPVM.
OrthoDBiEOG72G16X.
PhylomeDBiQ9QWT9.
TreeFamiTF105237.

Miscellaneous databases

PROiQ9QWT9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QWT9.
CleanExiMM_KIFC1.
ExpressionAtlasiQ9QWT9. baseline and differential.
GenevisibleiQ9QWT9. MM.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 3 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles."
    Saito N., Okada Y., Noda Y., Kinoshita Y., Kondo S., Hirokawa N.
    Neuron 18:425-438(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    Strain: ICRImported.
    Tissue: BrainImported.
  2. "Identification of isoforms of a mitotic motor in mammalian spermatogenesis."
    Navolanic P.M., Sperry A.O.
    Biol. Reprod. 62:1360-1369(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of centrosome duplication."
    Christodoulou A., Lederer C.W., Surrey T., Vernos I., Santama N.
    J. Cell Sci. 119:2035-2047(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH NUBP1 AND NUBP2, DISRUPTION PHENOTYPE.
    Strain: C57BL/6 X SJLImported.
    Tissue: HippocampusImported.
  4. "Sequence of the mouse major histocompatibility complex class II region."
    Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M., Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129Imported.
  5. "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 1).
    Strain: Czech IIImported and NMRIImported.
    Tissue: Mammary glandImported and ThyroidImported.
  6. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 97-131, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. "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 387-674.
    Strain: C57BL/6JImported.
    Tissue: HeadImported.
  8. "Identification, partial characterization, and genetic mapping of kinesin-like protein genes in mouse."
    Yang Z., Hanlon D.W., Marszalek J.R., Goldstein L.S.
    Genomics 45:123-131(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 416-570.
  9. "Kif5B and Kifc1 interact and are required for motility and fission of early endocytic vesicles in mouse liver."
    Nath S., Bananis E., Sarkar S., Stockert R.J., Sperry A.O., Murray J.W., Wolkoff A.W.
    Mol. Biol. Cell 18:1839-1849(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Identification of a novel Leucine-rich repeat protein and candidate PP1 regulatory subunit expressed in developing spermatids."
    Wang R., Sperry A.O.
    BMC Cell Biol. 9:9-9(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R42.
  11. Cited for: FUNCTION.

Entry informationi

Entry nameiKIFC1_MOUSE
AccessioniPrimary (citable) accession number: Q9QWT9
Secondary accession number(s): O08671
, O35230, Q497Y3, Q4A1N2, Q6PG90, Q8BV06, Q99L84, Q9JKZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Purified early endocytic vesicles bind minus end-directed Kifc1 as well as plus end-directed Kif5b. Addition of anti-Kifc1 antibodies leads to a decrease in minus end-directed vesicle motility in vitro.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.