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Q9Y4B5

- MTCL1_HUMAN

UniProt

Q9Y4B5 - MTCL1_HUMAN

Protein

Microtubule cross-linking factor 1

Gene

MTCL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 5 (18 Apr 2012)
      Previous versions | rss
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    Functioni

    Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation. Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells.1 Publication

    GO - Molecular functioni

    1. microtubule binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
    2. microtubule bundle formation Source: UniProtKB
    3. positive regulation of microtubule motor activity Source: UniProtKB
    4. positive regulation of protein targeting to membrane Source: UniProtKB
    5. regulation of autophagy Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule cross-linking factor 1
    Alternative name(s):
    Coiled-coil domain-containing protein 165
    PAR-1-interacting protein
    SOGA family member 2
    Gene namesi
    Name:MTCL1
    Synonyms:CCDC165, KIAA0802, SOGA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:29121. MTCL1.

    Subcellular locationi

    Lateral cell membrane By similarity. Apical cell membrane By similarity. Cytoplasmcytoskeletonspindle pole 1 Publication. Midbody 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Colocalized with microtubules at the base of cilia. Gradually accumulates on the apicobasal microtubule bundles during epithelial cell polarization By similarity. Colocalized with the apicobasal microtubule bundles running beneath the lateral membrane. Colocalized with microtubule bundles in the spindle pole in mitotic cells and in the midbodies at the end of cytokinesis.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. apicolateral plasma membrane Source: UniProtKB
    3. cytoplasm Source: UniProtKB-KW
    4. cytoskeleton Source: UniProtKB
    5. extracellular space Source: InterPro
    6. lateral plasma membrane Source: UniProtKB
    7. microtubule bundle Source: UniProtKB
    8. midbody Source: UniProtKB
    9. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394616.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19051905Microtubule cross-linking factor 1PRO_0000280113Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771Phosphoserine1 Publication
    Modified residuei263 – 2631Phosphoserine1 Publication
    Modified residuei549 – 5491Phosphoserine3 Publications
    Modified residuei618 – 6181Phosphoserine1 Publication
    Modified residuei621 – 6211Phosphothreonine1 Publication
    Modified residuei685 – 6851Phosphoserine1 Publication
    Modified residuei776 – 7761Phosphoserine2 Publications
    Modified residuei901 – 9011Phosphoserine1 Publication
    Modified residuei923 – 9231Phosphoserine1 Publication
    Modified residuei1385 – 13851Phosphoserine1 Publication
    Modified residuei1388 – 13881Phosphoserine1 Publication
    Modified residuei1399 – 13991Phosphoserine1 Publication
    Modified residuei1417 – 14171Phosphothreonine2 Publications
    Modified residuei1421 – 14211Phosphoserine2 Publications
    Modified residuei1427 – 14271Phosphotyrosine1 Publication
    Modified residuei1561 – 15611Phosphoserine1 Publication
    Modified residuei1578 – 15781Phosphoserine1 Publication
    Modified residuei1583 – 15831Phosphoserine1 Publication
    Modified residuei1592 – 15921Phosphoserine1 Publication
    Modified residuei1661 – 16611Phosphoserine1 Publication
    Modified residuei1667 – 16671Phosphothreonine1 Publication
    Modified residuei1675 – 16751Phosphothreonine2 Publications
    Modified residuei1679 – 16791Phosphoserine1 Publication
    Modified residuei1683 – 16831Phosphoserine1 Publication
    Modified residuei1812 – 18121Phosphoserine1 Publication
    Modified residuei1814 – 18141Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y4B5.
    PaxDbiQ9Y4B5.
    PRIDEiQ9Y4B5.

    PTM databases

    PhosphoSiteiQ9Y4B5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y4B5.
    BgeeiQ9Y4B5.
    CleanExiHS_KIAA0802.
    GenevestigatoriQ9Y4B5.

    Organism-specific databases

    HPAiHPA046245.

    Interactioni

    Subunit structurei

    Isoform 1 interacts with MARK2; the interaction increases MARK2 microtubule-binding ability By similarity. Homodimer. Associates (via N- and C-terminus domains) with microtubule filaments. Isoform 2 interacts with MARK2; the interaction is direct.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi116859. 8 interactions.
    IntActiQ9Y4B5. 8 interactions.
    MINTiMINT-7945170.
    STRINGi9606.ENSP00000352927.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4B5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 508508Necessary for self-assembly, microtubule bundling activity and apicobasal microtubule organizationBy similarityAdd
    BLAST
    Regioni1 – 249249Necessary for colocalization and binding with microtubulesBy similarityAdd
    BLAST
    Regioni1265 – 1382118Necessary for interaction with MARK2 and apicobasal microtubule bundle formation in polarized epithelial cellsAdd
    BLAST
    Regioni1678 – 177396Necessary for colocalization and binding with microtubulesAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili330 – 40475Sequence AnalysisAdd
    BLAST
    Coiled coili432 – 48352Sequence AnalysisAdd
    BLAST
    Coiled coili513 – 718206Sequence AnalysisAdd
    BLAST
    Coiled coili1143 – 120159Sequence AnalysisAdd
    BLAST
    Coiled coili1238 – 127841Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi42 – 319278Pro-richAdd
    BLAST
    Compositional biasi54 – 198145Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SOGA family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG80576.
    HOVERGENiHBG080205.
    OMAiPIGNLGK.
    OrthoDBiEOG70GMF8.
    TreeFamiTF331853.

    Family and domain databases

    InterProiIPR027882. DUF4482.
    IPR027881. SOGA.
    [Graphical view]
    PfamiPF11365. DUF3166. 2 hits.
    PF14818. DUF4482. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y4B5-1) [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

    METLNGPAGG GAPDAKLQPP GQHHRHHHLH PVAERRRLHR APSPARPFLK     50
    DLHARPAAPG PAVPSSGRAP APAAPRSPNL AGKAPPSPGS LAAPGRLSRR 100
    SGGVPGAKDK PPPGAGARAA GGAKAALGSR RAARVAPAEP LSRAGKPPGA 150
    EPPSAAAKGR KAKRGSRAPP ARTVGPPTPA ARIPAVTLAV TSVAGSPARC 200
    SRISHTDSSS DLSDCPSEPL SDEQRLLPAA SSDAESGTGS SDREPPRGAP 250
    TPSPAARGAP PGSPEPPALL AAPLAAGACP GGRSIPSGVS GGFAGPGVAE 300
    DVRGRSPPER PVPGTPKEPS LGEQSRLVPA AEEEELLREM EELRSENDYL 350
    KDELDELRAE MEEMRDSYLE EDVYQLQELR RELDRANKNC RILQYRLRKA 400
    EQKSLKVAET GQVDGELIRS LEQDLKVAKD VSVRLHHELK TVEEKRAKAE 450
    DENETLRQQM IEVEISKQAL QNELERLKES SLKRRSTREM YKEKKTFNQD 500
    DSADLRCQLQ FAKEEAFLMR KKMAKLGREK DELEQELQKY KSLYGDVDSP 550
    LPTGEAGGPP STREAELKLR LKLVEEEANI LGRKIVELEV ENRGLKAEME 600
    DMRGQQEREG PGRDHAPSIP TSPFGDSLES STELRRHLQF VEEEAELLRR 650
    SISEIEDHNR QLTHELSKFK FEPPREPGWL GEGASPGAGG GAPLQEELKS 700
    ARLQISELSG KVLKLQHENH ALLSNIQRCD LAAHLGLRAP SPRDSDAESD 750
    AGKKESDGEE SRLPQPKREG PVGGESDSEE MFEKTSGFGS GKPSEASEPC 800
    PTELLKARED SEYLVTLKHE AQRLERTVER LITDTDSFLH DAGLRGGAPL 850
    PGPGLQGEEE QGEGDQQEPQ LLGTINAKMK AFKKELQAFL EQVNRIGDGL 900
    SPLPHLTESS SFLSTVTSVS RDSPIGNLGK ELGPDLQSRL KEQLEWQLGP 950
    ARGDERESLR LRAARELHRR ADGDTGSHGL GGQTCFSLEM EEEHLYALRW 1000
    KELEMHSLAL QNTLHERTWS DEKNLMQQEL RSLKQNIFLF YVKLRWLLKH 1050
    WRQGKQMEEE GEEFTEGEHP ETLSRLGELG VQGGHQADGP DHDSDRGCGF 1100
    PVGEHSPHSR VQIGDHSLRL QTADRGQPHK QVVENQQLFS AFKALLEDFR 1150
    AELREDERAR LRLQQQYASD KAAWDVEWAV LKCRLEQLEE KTENKLGELG 1200
    SSAESKGALK KEREVHQKLL ADSHSLVMDL RWQIHHSEKN WNREKVELLD 1250
    RLDRDRQEWE RQKKEFLWRI EQLQKENSPR RGGSFLCDQK DGNVRPFPHQ 1300
    GSLRMPRPVA MWPCADADSI PFEDRPLSKL KESDRCSASE NLYLDALSLD 1350
    DEPEEPPAHR PEREFRNRLP EEEENHKGNL QRAVSVSSMS EFQRLMDISP 1400
    FLPEKGLPST SSKEDVTPPL SPDDLKYIEE FNKSWDYTPN RGHNGGGPDL 1450
    WADRTEVGRA GHEDSTEPFP DSSWYLTTSV TMTTDTMTSP EHCQKQPLRS 1500
    HVLTEQSGLR VLHSPPAVRR VDSITAAGGE GPFPTSRARG SPGDTKGGPP 1550
    EPMLSRWPCT SPRHSRDYVE GARRPLDSPL CTSLGFASPL HSLEMSKNLS 1600
    DDMKEVAFSV RNAICSGPGE LQVKDMACQT NGSRTMGTQT VQTISVGLQT 1650
    EALRGSGVTS SPHKCLTPKA GGGATPVSSP SRSLRSRQVA PAIEKVQAKF 1700
    ERTCCSPKYG SPKLQRKPLP KADQPNNRTS PGMAQKGYSE SAWARSTTTR 1750
    ESPVHTTIND GLSSLFNIID HSPVVQDPFQ KGLRAGSRSR SAEPRPELGP 1800
    GQETGTNSRG RSPSPIGVGS EMCREEGGEG TPVKQDLSAP PGYTLTENVA 1850
    RILNKKLLEH ALKEERRQAA HGPPGLHSDS HSLGDTAEPG PMENQTVLLT 1900
    APWGL 1905
    Length:1,905
    Mass (Da):209,526
    Last modified:April 18, 2012 - v5
    Checksum:iBD7455BB2B822CE0
    GO
    Isoform 2 (identifier: Q9Y4B5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-360: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,545
    Mass (Da):173,310
    Checksum:iDF457AEFCFAFB40A
    GO
    Isoform 3 (identifier: Q9Y4B5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-360: Missing.
         989-989: E → ELRGPPVLPEQSVSIEELQGQLVQAARLHQEETETFTNKIHK

    Show »
    Length:1,586
    Mass (Da):177,945
    Checksum:i1D44ACAC4C4977A3
    GO
    Isoform 4 (identifier: Q9Y4B5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1004: Missing.
         1187-1187: Q → QNCCGYPRINIEEETLGFTRLPAGSTVKTLKSLGLQRLE
         1273-1300: Missing.
         1894-1905: NQTVLLTAPWGL → ELPCSALAPS...LHGLSQYNSL

    Note: Contains a phosphoserine at position 941. Contains a phosphoserine at position 975.

    Show »
    Length:976
    Mass (Da):108,707
    Checksum:iF49E33A334D49052
    GO

    Sequence cautioni

    The sequence BAA34522.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti602 – 6021M → T.
    Corresponds to variant rs35739383 [ dbSNP | Ensembl ].
    VAR_055942
    Natural varianti861 – 8611Q → R.1 Publication
    Corresponds to variant rs1965665 [ dbSNP | Ensembl ].
    VAR_031073
    Natural varianti898 – 8981D → G.2 Publications
    Corresponds to variant rs3744979 [ dbSNP | Ensembl ].
    VAR_031074
    Natural varianti1097 – 10971G → S.1 Publication
    Corresponds to variant rs12386117 [ dbSNP | Ensembl ].
    VAR_031075
    Natural varianti1211 – 12111K → Q.
    Corresponds to variant rs11874468 [ dbSNP | Ensembl ].
    VAR_031076

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 10041004Missing in isoform 4. 1 PublicationVSP_023549Add
    BLAST
    Alternative sequencei1 – 360360Missing in isoform 2 and isoform 3. 2 PublicationsVSP_023550Add
    BLAST
    Alternative sequencei989 – 9891E → ELRGPPVLPEQSVSIEELQG QLVQAARLHQEETETFTNKI HK in isoform 3. 1 PublicationVSP_023551
    Alternative sequencei1187 – 11871Q → QNCCGYPRINIEEETLGFTR LPAGSTVKTLKSLGLQRLE in isoform 4. 1 PublicationVSP_023552
    Alternative sequencei1273 – 130028Missing in isoform 4. 1 PublicationVSP_023553Add
    BLAST
    Alternative sequencei1894 – 190512NQTVL…APWGL → ELPCSALAPSLEPCFSRPER PANRRPPSRWAPHSPTASQP QSPGDPTSLEEHGGEEPPEE QPHRDASLHGLSQYNSL in isoform 4. 1 PublicationVSP_023554Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018345 mRNA. Translation: BAA34522.2. Different initiation.
    AK131528 mRNA. Translation: BAD18666.1.
    AP000864 Genomic DNA. No translation available.
    AP001531 Genomic DNA. No translation available.
    BC040542 mRNA. Translation: AAH40542.2.
    CCDSiCCDS11841.1. [Q9Y4B5-3]
    RefSeqiNP_056025.2. NM_015210.3. [Q9Y4B5-3]
    XP_005258156.1. XM_005258099.2. [Q9Y4B5-1]
    UniGeneiHs.707920.

    Genome annotation databases

    EnsembliENST00000306329; ENSP00000305027; ENSG00000168502. [Q9Y4B5-1]
    ENST00000359865; ENSP00000352927; ENSG00000168502. [Q9Y4B5-3]
    ENST00000400050; ENSP00000382924; ENSG00000168502. [Q9Y4B5-2]
    ENST00000517570; ENSP00000429556; ENSG00000168502. [Q9Y4B5-2]
    ENST00000518815; ENSP00000463465; ENSG00000168502. [Q9Y4B5-4]
    GeneIDi23255.
    KEGGihsa:23255.
    UCSCiuc002knq.2. human. [Q9Y4B5-1]
    uc002knr.2. human. [Q9Y4B5-3]
    uc002kns.2. human. [Q9Y4B5-4]

    Polymorphism databases

    DMDMi384872711.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018345 mRNA. Translation: BAA34522.2 . Different initiation.
    AK131528 mRNA. Translation: BAD18666.1 .
    AP000864 Genomic DNA. No translation available.
    AP001531 Genomic DNA. No translation available.
    BC040542 mRNA. Translation: AAH40542.2 .
    CCDSi CCDS11841.1. [Q9Y4B5-3 ]
    RefSeqi NP_056025.2. NM_015210.3. [Q9Y4B5-3 ]
    XP_005258156.1. XM_005258099.2. [Q9Y4B5-1 ]
    UniGenei Hs.707920.

    3D structure databases

    ProteinModelPortali Q9Y4B5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116859. 8 interactions.
    IntActi Q9Y4B5. 8 interactions.
    MINTi MINT-7945170.
    STRINGi 9606.ENSP00000352927.

    PTM databases

    PhosphoSitei Q9Y4B5.

    Polymorphism databases

    DMDMi 384872711.

    Proteomic databases

    MaxQBi Q9Y4B5.
    PaxDbi Q9Y4B5.
    PRIDEi Q9Y4B5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306329 ; ENSP00000305027 ; ENSG00000168502 . [Q9Y4B5-1 ]
    ENST00000359865 ; ENSP00000352927 ; ENSG00000168502 . [Q9Y4B5-3 ]
    ENST00000400050 ; ENSP00000382924 ; ENSG00000168502 . [Q9Y4B5-2 ]
    ENST00000517570 ; ENSP00000429556 ; ENSG00000168502 . [Q9Y4B5-2 ]
    ENST00000518815 ; ENSP00000463465 ; ENSG00000168502 . [Q9Y4B5-4 ]
    GeneIDi 23255.
    KEGGi hsa:23255.
    UCSCi uc002knq.2. human. [Q9Y4B5-1 ]
    uc002knr.2. human. [Q9Y4B5-3 ]
    uc002kns.2. human. [Q9Y4B5-4 ]

    Organism-specific databases

    CTDi 23255.
    GeneCardsi GC18P008708.
    HGNCi HGNC:29121. MTCL1.
    HPAi HPA046245.
    MIMi 615766. gene.
    neXtProti NX_Q9Y4B5.
    PharmGKBi PA128394616.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80576.
    HOVERGENi HBG080205.
    OMAi PIGNLGK.
    OrthoDBi EOG70GMF8.
    TreeFami TF331853.

    Miscellaneous databases

    GeneWikii KIAA0802.
    GenomeRNAii 23255.
    NextBioi 44978.
    PROi Q9Y4B5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4B5.
    Bgeei Q9Y4B5.
    CleanExi HS_KIAA0802.
    Genevestigatori Q9Y4B5.

    Family and domain databases

    InterProi IPR027882. DUF4482.
    IPR027881. SOGA.
    [Graphical view ]
    Pfami PF11365. DUF3166. 2 hits.
    PF14818. DUF4482. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ARG-861 AND SER-1097.
      Tissue: Brain.
    2. Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "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] (ISOFORM 3), VARIANT GLY-898.
      Tissue: Cerebellum.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 4).
      Tissue: Testis.
    6. "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.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1417; SER-1421; THR-1675 AND SER-1679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-618; THR-621; SER-776; SER-901; SER-923; SER-1385; SER-1388; THR-1417; SER-1421; TYR-1427; SER-1561; SER-1578; SER-1583; SER-1592; SER-1661; THR-1667; THR-1675; SER-1683; SER-1812 AND SER-1814, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941 AND SER-975 (ISOFORM 4), VARIANT [LARGE SCALE ANALYSIS] GLY-898, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-77; SER-263; SER-685; SER-776 AND SER-1399, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "The novel PAR-1-binding protein MTCL1 has crucial roles in organizing microtubules in polarizing epithelial cells."
      Sato Y., Akitsu M., Amano Y., Yamashita K., Ide M., Shimada K., Yamashita A., Hirano H., Arakawa N., Maki T., Hayashi I., Ohno S., Suzuki A.
      J. Cell Sci. 126:4671-4683(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH MARK2, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiMTCL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4B5
    Secondary accession number(s): E9PAY7, Q6ZMQ9, Q8IWA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: April 18, 2012
    Last modified: October 1, 2014
    This is version 96 of the entry and version 5 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 18
      Human chromosome 18: 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