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Q9Y4B5

- MTCL1_HUMAN

UniProt

Q9Y4B5 - MTCL1_HUMAN

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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

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 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
Complete GO annotation...

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. apicolateral plasma membrane Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB
  4. extracellular space Source: InterPro
  5. lateral plasma membrane Source: UniProtKB
  6. microtubule bundle Source: UniProtKB
  7. midbody Source: UniProtKB
  8. spindle pole Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9Y4B5.
CleanExiHS_KIAA0802.
ExpressionAtlasiQ9Y4B5. baseline and differential.
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. 11 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.
GeneTreeiENSGT00530000063889.
HOVERGENiHBG080205.
InParanoidiQ9Y4B5.
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

        10         20         30         40         50
METLNGPAGG GAPDAKLQPP GQHHRHHHLH PVAERRRLHR APSPARPFLK
60 70 80 90 100
DLHARPAAPG PAVPSSGRAP APAAPRSPNL AGKAPPSPGS LAAPGRLSRR
110 120 130 140 150
SGGVPGAKDK PPPGAGARAA GGAKAALGSR RAARVAPAEP LSRAGKPPGA
160 170 180 190 200
EPPSAAAKGR KAKRGSRAPP ARTVGPPTPA ARIPAVTLAV TSVAGSPARC
210 220 230 240 250
SRISHTDSSS DLSDCPSEPL SDEQRLLPAA SSDAESGTGS SDREPPRGAP
260 270 280 290 300
TPSPAARGAP PGSPEPPALL AAPLAAGACP GGRSIPSGVS GGFAGPGVAE
310 320 330 340 350
DVRGRSPPER PVPGTPKEPS LGEQSRLVPA AEEEELLREM EELRSENDYL
360 370 380 390 400
KDELDELRAE MEEMRDSYLE EDVYQLQELR RELDRANKNC RILQYRLRKA
410 420 430 440 450
EQKSLKVAET GQVDGELIRS LEQDLKVAKD VSVRLHHELK TVEEKRAKAE
460 470 480 490 500
DENETLRQQM IEVEISKQAL QNELERLKES SLKRRSTREM YKEKKTFNQD
510 520 530 540 550
DSADLRCQLQ FAKEEAFLMR KKMAKLGREK DELEQELQKY KSLYGDVDSP
560 570 580 590 600
LPTGEAGGPP STREAELKLR LKLVEEEANI LGRKIVELEV ENRGLKAEME
610 620 630 640 650
DMRGQQEREG PGRDHAPSIP TSPFGDSLES STELRRHLQF VEEEAELLRR
660 670 680 690 700
SISEIEDHNR QLTHELSKFK FEPPREPGWL GEGASPGAGG GAPLQEELKS
710 720 730 740 750
ARLQISELSG KVLKLQHENH ALLSNIQRCD LAAHLGLRAP SPRDSDAESD
760 770 780 790 800
AGKKESDGEE SRLPQPKREG PVGGESDSEE MFEKTSGFGS GKPSEASEPC
810 820 830 840 850
PTELLKARED SEYLVTLKHE AQRLERTVER LITDTDSFLH DAGLRGGAPL
860 870 880 890 900
PGPGLQGEEE QGEGDQQEPQ LLGTINAKMK AFKKELQAFL EQVNRIGDGL
910 920 930 940 950
SPLPHLTESS SFLSTVTSVS RDSPIGNLGK ELGPDLQSRL KEQLEWQLGP
960 970 980 990 1000
ARGDERESLR LRAARELHRR ADGDTGSHGL GGQTCFSLEM EEEHLYALRW
1010 1020 1030 1040 1050
KELEMHSLAL QNTLHERTWS DEKNLMQQEL RSLKQNIFLF YVKLRWLLKH
1060 1070 1080 1090 1100
WRQGKQMEEE GEEFTEGEHP ETLSRLGELG VQGGHQADGP DHDSDRGCGF
1110 1120 1130 1140 1150
PVGEHSPHSR VQIGDHSLRL QTADRGQPHK QVVENQQLFS AFKALLEDFR
1160 1170 1180 1190 1200
AELREDERAR LRLQQQYASD KAAWDVEWAV LKCRLEQLEE KTENKLGELG
1210 1220 1230 1240 1250
SSAESKGALK KEREVHQKLL ADSHSLVMDL RWQIHHSEKN WNREKVELLD
1260 1270 1280 1290 1300
RLDRDRQEWE RQKKEFLWRI EQLQKENSPR RGGSFLCDQK DGNVRPFPHQ
1310 1320 1330 1340 1350
GSLRMPRPVA MWPCADADSI PFEDRPLSKL KESDRCSASE NLYLDALSLD
1360 1370 1380 1390 1400
DEPEEPPAHR PEREFRNRLP EEEENHKGNL QRAVSVSSMS EFQRLMDISP
1410 1420 1430 1440 1450
FLPEKGLPST SSKEDVTPPL SPDDLKYIEE FNKSWDYTPN RGHNGGGPDL
1460 1470 1480 1490 1500
WADRTEVGRA GHEDSTEPFP DSSWYLTTSV TMTTDTMTSP EHCQKQPLRS
1510 1520 1530 1540 1550
HVLTEQSGLR VLHSPPAVRR VDSITAAGGE GPFPTSRARG SPGDTKGGPP
1560 1570 1580 1590 1600
EPMLSRWPCT SPRHSRDYVE GARRPLDSPL CTSLGFASPL HSLEMSKNLS
1610 1620 1630 1640 1650
DDMKEVAFSV RNAICSGPGE LQVKDMACQT NGSRTMGTQT VQTISVGLQT
1660 1670 1680 1690 1700
EALRGSGVTS SPHKCLTPKA GGGATPVSSP SRSLRSRQVA PAIEKVQAKF
1710 1720 1730 1740 1750
ERTCCSPKYG SPKLQRKPLP KADQPNNRTS PGMAQKGYSE SAWARSTTTR
1760 1770 1780 1790 1800
ESPVHTTIND GLSSLFNIID HSPVVQDPFQ KGLRAGSRSR SAEPRPELGP
1810 1820 1830 1840 1850
GQETGTNSRG RSPSPIGVGS EMCREEGGEG TPVKQDLSAP PGYTLTENVA
1860 1870 1880 1890 1900
RILNKKLLEH ALKEERRQAA HGPPGLHSDS HSLGDTAEPG PMENQTVLLT

APWGL
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.Curated

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:
EMBLi
GenBanki
DDBJi
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. [Q9Y4B5-3]
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:
EMBLi
GenBanki
DDBJi
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. 11 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 . [Q9Y4B5-3 ]
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 GC18P008705.
HGNCi HGNC:29121. MTCL1.
HPAi HPA046245.
MIMi 615766. gene.
neXtProti NX_Q9Y4B5.
PharmGKBi PA128394616.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80576.
GeneTreei ENSGT00530000063889.
HOVERGENi HBG080205.
InParanoidi Q9Y4B5.
OMAi PIGNLGK.
OrthoDBi EOG70GMF8.
TreeFami TF331853.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9Y4B5.
CleanExi HS_KIAA0802.
ExpressionAtlasi Q9Y4B5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 97 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

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