Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q7Z4S6

- KI21A_HUMAN

UniProt

Q7Z4S6 - KI21A_HUMAN

Protein

Kinesin-like protein KIF21A

Gene

KIF21A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Microtubule-binding motor protein probably involved in neuronal axonal transport. In vitro, has a plus-end directed motor activity By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 958ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule motor activity Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. microtubule-based movement Source: InterPro

    Keywords - Molecular functioni

    Motor protein

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ7Z4S6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin-like protein KIF21A
    Alternative name(s):
    Kinesin-like protein KIF2
    Renal carcinoma antigen NY-REN-62
    Gene namesi
    Name:KIF21A
    Synonyms:KIAA1708, KIF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:19349. KIF21A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. kinesin complex Source: InterPro
    3. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Congenital fibrosis of extraocular muscles 1 (CFEOM1) [MIM:135700]: A congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Patients affected by congenital fibrosis of extraocular muscles type 1 show an absence of the superior division of the oculomotor nerve (cranial nerve III) and corresponding oculomotor subnuclei.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti356 – 3561M → T in CFEOM1. 1 Publication
    VAR_019399
    Natural varianti947 – 9471M → R in CFEOM1. 1 Publication
    VAR_019400
    Natural varianti947 – 9471M → T in CFEOM1. 1 Publication
    VAR_027021
    Natural varianti947 – 9471M → V in CFEOM1. 1 Publication
    VAR_019401
    Natural varianti954 – 9541R → Q in CFEOM1. 1 Publication
    VAR_019402
    Natural varianti954 – 9541R → W in CFEOM1. 1 Publication
    VAR_019403
    Natural varianti1010 – 10101I → T in CFEOM1. 1 Publication
    VAR_019404

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi135700. phenotype.
    Orphaneti45358. Congenital fibrosis of extraocular muscles.
    PharmGKBiPA134882934.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16741674Kinesin-like protein KIF21APRO_0000125462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei524 – 5241Phosphoserine1 Publication
    Modified residuei1212 – 12121Phosphoserine3 Publications
    Modified residuei1239 – 12391Phosphoserine3 Publications
    Modified residuei1662 – 16621Phosphoserine1 Publication
    Modified residuei1664 – 16641Phosphothreonine1 Publication
    Modified residuei1673 – 16731Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z4S6.
    PaxDbiQ7Z4S6.
    PeptideAtlasiQ7Z4S6.
    PRIDEiQ7Z4S6.

    PTM databases

    PhosphoSiteiQ7Z4S6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7Z4S6.
    BgeeiQ7Z4S6.
    CleanExiHS_KIF21A.
    GenevestigatoriQ7Z4S6.

    Organism-specific databases

    HPAiCAB022079.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARFGEF1Q9Y6D64EBI-6251716,EBI-1044254
    KANK1Q146782EBI-2691397,EBI-2556221
    KANK1Q14678-23EBI-2691397,EBI-6173812

    Protein-protein interaction databases

    BioGridi120746. 5 interactions.
    DIPiDIP-56253N.
    IntActiQ7Z4S6. 5 interactions.
    MINTiMINT-2808104.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7Z4S6.
    SMRiQ7Z4S6. Positions 10-379, 1308-1655.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 371363Kinesin motorPROSITE-ProRule annotationAdd
    BLAST
    Repeati1345 – 138238WD 1Add
    BLAST
    Repeati1385 – 142339WD 2Add
    BLAST
    Repeati1449 – 148739WD 3Add
    BLAST
    Repeati1490 – 153243WD 4Add
    BLAST
    Repeati1541 – 157838WD 5Add
    BLAST
    Repeati1582 – 162140WD 6Add
    BLAST
    Repeati1624 – 166138WD 7Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili365 – 575211Sequence AnalysisAdd
    BLAST
    Coiled coili931 – 101989Sequence AnalysisAdd
    BLAST
    Coiled coili1053 – 108331Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
    Contains 1 kinesin motor domain.PROSITE-ProRule annotation
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOVERGENiHBG052247.
    KOiK10395.
    PhylomeDBiQ7Z4S6.
    TreeFamiTF105224.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    3.40.850.10. 1 hit.
    InterProiIPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    IPR009053. Prefoldin.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR24115. PTHR24115. 1 hit.
    PfamiPF00225. Kinesin. 1 hit.
    PF00400. WD40. 4 hits.
    [Graphical view]
    PRINTSiPR00380. KINESINHEAVY.
    SMARTiSM00129. KISc. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF46579. SSF46579. 1 hit.
    SSF50978. SSF50978. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z4S6-1) [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

    MLGAPDESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT     50
    FDYVFDIDSQ QEQIYIQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT 100
    GFDVNIVEEE LGIISRAVKH LFKSIEEKKH IAIKNGLPAP DFKVNAQFLE 150
    LYNEEVLDLF DTTRDIDAKS KKSNIRIHED STGGIYTVGV TTRTVNTESE 200
    MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC PQIDADNATD 250
    NKIISESAQM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG 300
    LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP 350
    SDRDFMETLN TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL 400
    MEYKTGKRII DEEGVESIND MFHENAMLQT ENNNLRVRIK AMQETVDALR 450
    SRITQLVSDQ ANHVLARAGE GNEEISNMIH SYIKEIEDLR AKLLESEAVN 500
    ENLRKNLTRA TARAPYFSGS STFSPTILSS DKETIEIIDL AKKDLEKLKR 550
    KEKRKKKRLQ KLEESNREER SVAGKEDNTD TDQEKKEEKG VSERENNELE 600
    VEESQEVSDH EDEEEEEEEE EDDIDGGESS DESDSESDEK ANYQADLANI 650
    TCEIAIKQKL IDELENSQKR LQTLKKQYEE KLMMLQHKIR DTQLERDQVL 700
    QNLGSVESYS EEKAKKVRSE YEKKLQAMNK ELQRLQAAQK EHARLLKNQS 750
    QYEKQLKKLQ QDVMEMKKTK VRLMKQMKEE QEKARLTESR RNREIAQLKK 800
    DQRKRDHQLR LLEAQKRNQE VVLRRKTEEV TALRRQVRPM SDKVAGKVTR 850
    KLSSSDAPAQ DTGSSAAAVE TDASRTGAQQ KMRIPVARVQ ALPTPATNGN 900
    RKKYQRKGLT GRVFISKTAR MKWQLLERRV TDIIMQKMTI SNMEADMNRL 950
    LKQREELTKR REKLSKRREK IVKENGEGDK NVANINEEME SLTANIDYIN 1000
    DSISDCQANI MQMEEAKEEG ETLDVTAVIN ACTLTEARYL LDHFLSMGIN 1050
    KGLQAAQKEA QIKVLEGRLK QTEITSATQN QLLFHMLKEK AELNPELDAL 1100
    LGHALQDLDS VPLENVEDST DEDAPLNSPG SEGSTLSSDL MKLCGEVKPK 1150
    NKARRRTTTQ MELLYADSSE LASDTSTGDA SLPGPLTPVA EGQEIGMNTE 1200
    TSGTSAREKE LSPPPGLPSK IGSISRQSSL SEKKIPEPSP VTRRKAYEKA 1250
    EKSKAKEQKH SDSGTSEASL SPPSSPPSRP RNELNVFNRL TVSQGNTSVQ 1300
    QDKSDESDSS LSEVHRSSRR GIINPFPASK GIRAFPLQCI HIAEGHTKAV 1350
    LCVDSTDDLL FTGSKDRTCK VWNLVTGQEI MSLGGHPNNV VSVKYCNYTS 1400
    LVFTVSTSYI KVWDIRDSAK CIRTLTSSGQ VTLGDACSAS TSRTVAIPSG 1450
    ENQINQIALN PTGTFLYAAS GNAVRMWDLK RFQSTGKLTG HLGPVMCLTV 1500
    DQISSGQDLI ITGSKDHYIK MFDVTEGALG TVSPTHNFEP PHYDGIEALT 1550
    IQGDNLFSGS RDNGIKKWDL TQKDLLQQVP NAHKDWVCAL GVVPDHPVLL 1600
    SGCRGGILKV WNMDTFMPVG EMKGHDSPIN AICVNSTHIF TAADDRTVRI 1650
    WKARNLQDGQ ISDTGDLGED IASN 1674
    Length:1,674
    Mass (Da):187,179
    Last modified:July 19, 2004 - v2
    Checksum:i292AFA5F2C0C6F9A
    GO
    Isoform 2 (identifier: Q7Z4S6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         558-570: Missing.

    Show »
    Length:1,661
    Mass (Da):185,510
    Checksum:i62AAF4804167A918
    GO
    Isoform 3 (identifier: Q7Z4S6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1260-1319: HSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSLSEVHRSSR → QSDESDSSLSEVH

    Note: No experimental confirmation available.

    Show »
    Length:1,627
    Mass (Da):182,129
    Checksum:iB4B2415E2E95010F
    GO
    Isoform 4 (identifier: Q7Z4S6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1315-1315: H → HS

    Note: No experimental confirmation available.

    Show »
    Length:1,675
    Mass (Da):187,266
    Checksum:iDA1BD09FE7D3C1AF
    GO
    Isoform 5 (identifier: Q7Z4S6-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         558-570: Missing.
         1107-1113: Missing.
         1304-1320: Missing.

    Show »
    Length:1,637
    Mass (Da):182,854
    Checksum:iC65E7231C1EEA1B1
    GO
    Isoform 6 (identifier: Q7Z4S6-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         558-570: Missing.
         807-829: Missing.
         1304-1320: Missing.

    Show »
    Length:1,621
    Mass (Da):180,738
    Checksum:iC58AFA881A960A85
    GO

    Sequence cautioni

    The sequence AAH41430.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAA90916.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAD42883.1 differs from that shown. Reason: Frameshift at positions 185, 191, 380 and 405.
    The sequence AAP97680.1 differs from that shown. Reason: Frameshift at positions 185 and 191.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti172 – 1721K → R in CAJ45483. 1 PublicationCurated
    Sequence conflicti176 – 1761R → G in CAJ45483. 1 PublicationCurated
    Sequence conflicti215 – 2151A → G in CAJ45483. 1 PublicationCurated
    Sequence conflicti315 – 3151S → C in CAJ45483. 1 PublicationCurated
    Sequence conflicti596 – 5972NN → TQ in AAP97680. 1 PublicationCurated
    Sequence conflicti596 – 5972NN → TQ in AAD42883. (PubMed:10508479)Curated
    Sequence conflicti653 – 6531E → D in AAP97680. 1 PublicationCurated
    Sequence conflicti801 – 8022DQ → AP in AAP97680. 1 PublicationCurated
    Sequence conflicti801 – 8011D → G in CAJ45483. 1 PublicationCurated
    Sequence conflicti813 – 8131E → G in AAP97680. 1 PublicationCurated
    Sequence conflicti826 – 8261K → Q in AAP97680. 1 PublicationCurated
    Sequence conflicti875 – 8751R → G in CAJ45483. 1 PublicationCurated
    Sequence conflicti892 – 8921L → S in CAJ45483. 1 PublicationCurated
    Sequence conflicti1071 – 10711Q → R in CAJ45483. 1 PublicationCurated
    Sequence conflicti1167 – 11671D → G in CAJ45483. 1 PublicationCurated
    Sequence conflicti1237 – 12371E → D in AAI36415. (PubMed:15489334)Curated
    Sequence conflicti1341 – 13411H → N in CAJ45483. 1 PublicationCurated
    Sequence conflicti1378 – 13792QE → HR in CAJ45483. 1 PublicationCurated
    Sequence conflicti1429 – 14291G → A in CAJ45483. 1 PublicationCurated
    Sequence conflicti1503 – 15031I → T in CAD97863. (PubMed:17974005)Curated
    Sequence conflicti1511 – 15111I → T in CAD97863. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti356 – 3561M → T in CFEOM1. 1 Publication
    VAR_019399
    Natural varianti947 – 9471M → R in CFEOM1. 1 Publication
    VAR_019400
    Natural varianti947 – 9471M → T in CFEOM1. 1 Publication
    VAR_027021
    Natural varianti947 – 9471M → V in CFEOM1. 1 Publication
    VAR_019401
    Natural varianti954 – 9541R → Q in CFEOM1. 1 Publication
    VAR_019402
    Natural varianti954 – 9541R → W in CFEOM1. 1 Publication
    VAR_019403
    Natural varianti1010 – 10101I → T in CFEOM1. 1 Publication
    VAR_019404

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei558 – 57013Missing in isoform 2, isoform 5 and isoform 6. 7 PublicationsVSP_010870Add
    BLAST
    Alternative sequencei807 – 82923Missing in isoform 6. 1 PublicationVSP_046790Add
    BLAST
    Alternative sequencei1107 – 11137Missing in isoform 5. 1 PublicationVSP_046791
    Alternative sequencei1260 – 131960HSDSG…HRSSR → QSDESDSSLSEVH in isoform 3. 1 PublicationVSP_010871Add
    BLAST
    Alternative sequencei1304 – 132017Missing in isoform 5 and isoform 6. 2 PublicationsVSP_046792Add
    BLAST
    Alternative sequencei1315 – 13151H → HS in isoform 4. 1 PublicationVSP_010872

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY368076 mRNA. Translation: AAR04774.1.
    AM177179 mRNA. Translation: CAJ45483.1.
    AF450487 mRNA. Translation: AAP97680.1. Frameshift.
    AB290166 mRNA. Translation: BAG06720.1.
    AC084373 Genomic DNA. No translation available.
    AC090668 Genomic DNA. No translation available.
    AC121334 Genomic DNA. No translation available.
    AF155117 mRNA. Translation: AAD42883.1. Sequence problems.
    AK000059 mRNA. Translation: BAA90916.1. Sequence problems.
    CH471111 Genomic DNA. Translation: EAW57803.1.
    BC041430 mRNA. Translation: AAH41430.1. Sequence problems.
    BC047572 mRNA. Translation: AAH47572.1.
    BC136414 mRNA. Translation: AAI36415.1.
    AB051495 mRNA. Translation: BAB21799.2.
    BX537855 mRNA. Translation: CAD97863.1.
    CCDSiCCDS31773.1. [Q7Z4S6-2]
    CCDS53774.1. [Q7Z4S6-6]
    CCDS53775.1. [Q7Z4S6-5]
    CCDS53776.1. [Q7Z4S6-1]
    RefSeqiNP_001166934.1. NM_001173463.1. [Q7Z4S6-5]
    NP_001166935.1. NM_001173464.1. [Q7Z4S6-1]
    NP_001166936.1. NM_001173465.1. [Q7Z4S6-6]
    NP_060111.2. NM_017641.3. [Q7Z4S6-2]
    XP_005269064.1. XM_005269007.1. [Q7Z4S6-4]
    XP_005269070.1. XM_005269013.1. [Q7Z4S6-3]
    UniGeneiHs.374201.

    Genome annotation databases

    EnsembliENST00000361418; ENSP00000354878; ENSG00000139116. [Q7Z4S6-1]
    ENST00000361961; ENSP00000354851; ENSG00000139116. [Q7Z4S6-2]
    ENST00000541463; ENSP00000438075; ENSG00000139116. [Q7Z4S6-6]
    ENST00000544797; ENSP00000445606; ENSG00000139116. [Q7Z4S6-5]
    GeneIDi55605.
    KEGGihsa:55605.
    UCSCiuc001rlx.3. human. [Q7Z4S6-2]
    uc001rly.3. human. [Q7Z4S6-1]

    Polymorphism databases

    DMDMi50400977.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY368076 mRNA. Translation: AAR04774.1 .
    AM177179 mRNA. Translation: CAJ45483.1 .
    AF450487 mRNA. Translation: AAP97680.1 . Frameshift.
    AB290166 mRNA. Translation: BAG06720.1 .
    AC084373 Genomic DNA. No translation available.
    AC090668 Genomic DNA. No translation available.
    AC121334 Genomic DNA. No translation available.
    AF155117 mRNA. Translation: AAD42883.1 . Sequence problems.
    AK000059 mRNA. Translation: BAA90916.1 . Sequence problems.
    CH471111 Genomic DNA. Translation: EAW57803.1 .
    BC041430 mRNA. Translation: AAH41430.1 . Sequence problems.
    BC047572 mRNA. Translation: AAH47572.1 .
    BC136414 mRNA. Translation: AAI36415.1 .
    AB051495 mRNA. Translation: BAB21799.2 .
    BX537855 mRNA. Translation: CAD97863.1 .
    CCDSi CCDS31773.1. [Q7Z4S6-2 ]
    CCDS53774.1. [Q7Z4S6-6 ]
    CCDS53775.1. [Q7Z4S6-5 ]
    CCDS53776.1. [Q7Z4S6-1 ]
    RefSeqi NP_001166934.1. NM_001173463.1. [Q7Z4S6-5 ]
    NP_001166935.1. NM_001173464.1. [Q7Z4S6-1 ]
    NP_001166936.1. NM_001173465.1. [Q7Z4S6-6 ]
    NP_060111.2. NM_017641.3. [Q7Z4S6-2 ]
    XP_005269064.1. XM_005269007.1. [Q7Z4S6-4 ]
    XP_005269070.1. XM_005269013.1. [Q7Z4S6-3 ]
    UniGenei Hs.374201.

    3D structure databases

    ProteinModelPortali Q7Z4S6.
    SMRi Q7Z4S6. Positions 10-379, 1308-1655.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120746. 5 interactions.
    DIPi DIP-56253N.
    IntActi Q7Z4S6. 5 interactions.
    MINTi MINT-2808104.

    PTM databases

    PhosphoSitei Q7Z4S6.

    Polymorphism databases

    DMDMi 50400977.

    Proteomic databases

    MaxQBi Q7Z4S6.
    PaxDbi Q7Z4S6.
    PeptideAtlasi Q7Z4S6.
    PRIDEi Q7Z4S6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361418 ; ENSP00000354878 ; ENSG00000139116 . [Q7Z4S6-1 ]
    ENST00000361961 ; ENSP00000354851 ; ENSG00000139116 . [Q7Z4S6-2 ]
    ENST00000541463 ; ENSP00000438075 ; ENSG00000139116 . [Q7Z4S6-6 ]
    ENST00000544797 ; ENSP00000445606 ; ENSG00000139116 . [Q7Z4S6-5 ]
    GeneIDi 55605.
    KEGGi hsa:55605.
    UCSCi uc001rlx.3. human. [Q7Z4S6-2 ]
    uc001rly.3. human. [Q7Z4S6-1 ]

    Organism-specific databases

    CTDi 55605.
    GeneCardsi GC12M039687.
    GeneReviewsi KIF21A.
    HGNCi HGNC:19349. KIF21A.
    HPAi CAB022079.
    MIMi 135700. phenotype.
    608283. gene.
    neXtProti NX_Q7Z4S6.
    Orphaneti 45358. Congenital fibrosis of extraocular muscles.
    PharmGKBi PA134882934.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOVERGENi HBG052247.
    KOi K10395.
    PhylomeDBi Q7Z4S6.
    TreeFami TF105224.

    Enzyme and pathway databases

    SignaLinki Q7Z4S6.

    Miscellaneous databases

    ChiTaRSi KIF21A. human.
    GeneWikii KIF21A.
    GenomeRNAii 55605.
    NextBioi 60157.
    PROi Q7Z4S6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z4S6.
    Bgeei Q7Z4S6.
    CleanExi HS_KIF21A.
    Genevestigatori Q7Z4S6.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    3.40.850.10. 1 hit.
    InterProi IPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    IPR009053. Prefoldin.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR24115. PTHR24115. 1 hit.
    Pfami PF00225. Kinesin. 1 hit.
    PF00400. WD40. 4 hits.
    [Graphical view ]
    PRINTSi PR00380. KINESINHEAVY.
    SMARTi SM00129. KISc. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF46579. SSF46579. 1 hit.
    SSF50978. SSF50978. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS CFEOM1 THR-356; ARG-947; VAL-947; GLN-954; TRP-954 AND THR-1010.
    2. "Differential expression analysis of molecular motors in ALS motor neuron disease."
      Pantelidou M., Lederer C.W., Zographos S.E., Pfaffl M.W., Cavallaro S., Santama N.
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
      Tissue: Brain cortex.
    3. Zan Q., Guo J.H., Yu L.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free recombination: preparation of full-length cDNA clones encoding motor proteins."
      Yamakawa H., Kikuno R.F., Nagase T., Ohara O.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1243-1674 (ISOFORM 4).
      Tissue: Adrenal cortex, Brain and Testis.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-597 (ISOFORM 2), IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-586 (ISOFORM 2).
      Tissue: Colon.
    10. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1674 (ISOFORM 2).
      Tissue: Brain.
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 654-1674 (ISOFORM 3).
      Tissue: Liver.
    12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212; SER-1239 AND SER-1673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-1212; SER-1239; SER-1662; THR-1664 AND SER-1673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212 AND SER-1239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "A novel KIF21A mutation in a patient with congenital fibrosis of the extraocular muscles and Marcus Gunn jaw-winking phenomenon."
      Yamada K., Hunter D.G., Andrews C., Engle E.C.
      Arch. Ophthalmol. 123:1254-1259(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CFEOM1 THR-947.

    Entry informationi

    Entry nameiKI21A_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z4S6
    Secondary accession number(s): A8MX28
    , B0I1R9, B9EGE4, F5H0C3, F5H219, Q2UVF1, Q6UKL9, Q7Z668, Q86WZ5, Q8IVZ8, Q9C0F5, Q9NXU4, Q9Y590
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3