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Q9Y4B5 (MTCL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule cross-linking factor 1
Alternative name(s):
Coiled-coil domain-containing protein 165
PAR-1-interacting protein
SOGA family member 2
Gene names
Name:MTCL1
Synonyms:CCDC165, KIAA0802, SOGA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1905 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

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. Ref.13

Subcellular location

Lateral cell membrane By similarity. Apical cell membrane By similarity. Cytoplasmcytoskeletonspindle pole. Midbody. Cytoplasmcytoskeleton. 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. Ref.13

Sequence similarities

Belongs to the SOGA family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processestablishment or maintenance of epithelial cell apical/basal polarity

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule bundle formation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of microtubule motor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of autophagy

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

apicolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from direct assay Ref.13. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: InterPro

lateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule bundle

Inferred from sequence or structural similarity. Source: UniProtKB

midbody

Inferred from direct assay Ref.13. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionmicrotubule binding

Inferred from direct assay Ref.13. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y4B5-1)

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.
Isoform 2 (identifier: Q9Y4B5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-360: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9Y4B5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-360: Missing.
     989-989: E → ELRGPPVLPEQSVSIEELQGQLVQAARLHQEETETFTNKIHK
Isoform 4 (identifier: Q9Y4B5-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19051905Microtubule cross-linking factor 1
PRO_0000280113

Regions

Region1 – 508508Necessary for self-assembly, microtubule bundling activity and apicobasal microtubule organization By similarity
Region1 – 249249Necessary for colocalization and binding with microtubules By similarity
Region1265 – 1382118Necessary for interaction with MARK2 and apicobasal microtubule bundle formation in polarized epithelial cells
Region1678 – 177396Necessary for colocalization and binding with microtubules
Coiled coil330 – 40475 Potential
Coiled coil432 – 48352 Potential
Coiled coil513 – 718206 Potential
Coiled coil1143 – 120159 Potential
Coiled coil1238 – 127841 Potential
Compositional bias42 – 319278Pro-rich
Compositional bias54 – 198145Ala-rich

Amino acid modifications

Modified residue771Phosphoserine Ref.12
Modified residue2631Phosphoserine Ref.12
Modified residue5491Phosphoserine Ref.9 Ref.10 Ref.11
Modified residue6181Phosphoserine Ref.9
Modified residue6211Phosphothreonine Ref.9
Modified residue6851Phosphoserine Ref.12
Modified residue7761Phosphoserine Ref.9 Ref.12
Modified residue9011Phosphoserine Ref.9
Modified residue9231Phosphoserine Ref.9
Modified residue13851Phosphoserine Ref.9
Modified residue13881Phosphoserine Ref.9
Modified residue13991Phosphoserine Ref.12
Modified residue14171Phosphothreonine Ref.7 Ref.9
Modified residue14211Phosphoserine Ref.7 Ref.9
Modified residue14271Phosphotyrosine Ref.9
Modified residue15611Phosphoserine Ref.9
Modified residue15781Phosphoserine Ref.9
Modified residue15831Phosphoserine Ref.9
Modified residue15921Phosphoserine Ref.9
Modified residue16611Phosphoserine Ref.9
Modified residue16671Phosphothreonine Ref.9
Modified residue16751Phosphothreonine Ref.7 Ref.9
Modified residue16791Phosphoserine Ref.7
Modified residue16831Phosphoserine Ref.9
Modified residue18121Phosphoserine Ref.9
Modified residue18141Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 10041004Missing in isoform 4.
VSP_023549
Alternative sequence1 – 360360Missing in isoform 2 and isoform 3.
VSP_023550
Alternative sequence9891E → ELRGPPVLPEQSVSIEELQG QLVQAARLHQEETETFTNKI HK in isoform 3.
VSP_023551
Alternative sequence11871Q → QNCCGYPRINIEEETLGFTR LPAGSTVKTLKSLGLQRLE in isoform 4.
VSP_023552
Alternative sequence1273 – 130028Missing in isoform 4.
VSP_023553
Alternative sequence1894 – 190512NQTVL…APWGL → ELPCSALAPSLEPCFSRPER PANRRPPSRWAPHSPTASQP QSPGDPTSLEEHGGEEPPEE QPHRDASLHGLSQYNSL in isoform 4.
VSP_023554
Natural variant6021M → T.
Corresponds to variant rs35739383 [ dbSNP | Ensembl ].
VAR_055942
Natural variant8611Q → R. Ref.1
Corresponds to variant rs1965665 [ dbSNP | Ensembl ].
VAR_031073
Natural variant8981D → G. Ref.3 Ref.9
Corresponds to variant rs3744979 [ dbSNP | Ensembl ].
VAR_031074
Natural variant10971G → S. Ref.1
Corresponds to variant rs12386117 [ dbSNP | Ensembl ].
VAR_031075
Natural variant12111K → Q.
Corresponds to variant rs11874468 [ dbSNP | Ensembl ].
VAR_031076

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 18, 2012. Version 5.
Checksum: BD7455BB2B822CE0

FASTA1,905209,526
        10         20         30         40         50         60 
METLNGPAGG GAPDAKLQPP GQHHRHHHLH PVAERRRLHR APSPARPFLK DLHARPAAPG 

        70         80         90        100        110        120 
PAVPSSGRAP APAAPRSPNL AGKAPPSPGS LAAPGRLSRR SGGVPGAKDK PPPGAGARAA 

       130        140        150        160        170        180 
GGAKAALGSR RAARVAPAEP LSRAGKPPGA EPPSAAAKGR KAKRGSRAPP ARTVGPPTPA 

       190        200        210        220        230        240 
ARIPAVTLAV TSVAGSPARC SRISHTDSSS DLSDCPSEPL SDEQRLLPAA SSDAESGTGS 

       250        260        270        280        290        300 
SDREPPRGAP TPSPAARGAP PGSPEPPALL AAPLAAGACP GGRSIPSGVS GGFAGPGVAE 

       310        320        330        340        350        360 
DVRGRSPPER PVPGTPKEPS LGEQSRLVPA AEEEELLREM EELRSENDYL KDELDELRAE 

       370        380        390        400        410        420 
MEEMRDSYLE EDVYQLQELR RELDRANKNC RILQYRLRKA EQKSLKVAET GQVDGELIRS 

       430        440        450        460        470        480 
LEQDLKVAKD VSVRLHHELK TVEEKRAKAE DENETLRQQM IEVEISKQAL QNELERLKES 

       490        500        510        520        530        540 
SLKRRSTREM YKEKKTFNQD DSADLRCQLQ FAKEEAFLMR KKMAKLGREK DELEQELQKY 

       550        560        570        580        590        600 
KSLYGDVDSP LPTGEAGGPP STREAELKLR LKLVEEEANI LGRKIVELEV ENRGLKAEME 

       610        620        630        640        650        660 
DMRGQQEREG PGRDHAPSIP TSPFGDSLES STELRRHLQF VEEEAELLRR SISEIEDHNR 

       670        680        690        700        710        720 
QLTHELSKFK FEPPREPGWL GEGASPGAGG GAPLQEELKS ARLQISELSG KVLKLQHENH 

       730        740        750        760        770        780 
ALLSNIQRCD LAAHLGLRAP SPRDSDAESD AGKKESDGEE SRLPQPKREG PVGGESDSEE 

       790        800        810        820        830        840 
MFEKTSGFGS GKPSEASEPC PTELLKARED SEYLVTLKHE AQRLERTVER LITDTDSFLH 

       850        860        870        880        890        900 
DAGLRGGAPL PGPGLQGEEE QGEGDQQEPQ LLGTINAKMK AFKKELQAFL EQVNRIGDGL 

       910        920        930        940        950        960 
SPLPHLTESS SFLSTVTSVS RDSPIGNLGK ELGPDLQSRL KEQLEWQLGP ARGDERESLR 

       970        980        990       1000       1010       1020 
LRAARELHRR ADGDTGSHGL GGQTCFSLEM EEEHLYALRW KELEMHSLAL QNTLHERTWS 

      1030       1040       1050       1060       1070       1080 
DEKNLMQQEL RSLKQNIFLF YVKLRWLLKH WRQGKQMEEE GEEFTEGEHP ETLSRLGELG 

      1090       1100       1110       1120       1130       1140 
VQGGHQADGP DHDSDRGCGF PVGEHSPHSR VQIGDHSLRL QTADRGQPHK QVVENQQLFS 

      1150       1160       1170       1180       1190       1200 
AFKALLEDFR AELREDERAR LRLQQQYASD KAAWDVEWAV LKCRLEQLEE KTENKLGELG 

      1210       1220       1230       1240       1250       1260 
SSAESKGALK KEREVHQKLL ADSHSLVMDL RWQIHHSEKN WNREKVELLD RLDRDRQEWE 

      1270       1280       1290       1300       1310       1320 
RQKKEFLWRI EQLQKENSPR RGGSFLCDQK DGNVRPFPHQ GSLRMPRPVA MWPCADADSI 

      1330       1340       1350       1360       1370       1380 
PFEDRPLSKL KESDRCSASE NLYLDALSLD DEPEEPPAHR PEREFRNRLP EEEENHKGNL 

      1390       1400       1410       1420       1430       1440 
QRAVSVSSMS EFQRLMDISP FLPEKGLPST SSKEDVTPPL SPDDLKYIEE FNKSWDYTPN 

      1450       1460       1470       1480       1490       1500 
RGHNGGGPDL WADRTEVGRA GHEDSTEPFP DSSWYLTTSV TMTTDTMTSP EHCQKQPLRS 

      1510       1520       1530       1540       1550       1560 
HVLTEQSGLR VLHSPPAVRR VDSITAAGGE GPFPTSRARG SPGDTKGGPP EPMLSRWPCT 

      1570       1580       1590       1600       1610       1620 
SPRHSRDYVE GARRPLDSPL CTSLGFASPL HSLEMSKNLS DDMKEVAFSV RNAICSGPGE 

      1630       1640       1650       1660       1670       1680 
LQVKDMACQT NGSRTMGTQT VQTISVGLQT EALRGSGVTS SPHKCLTPKA GGGATPVSSP 

      1690       1700       1710       1720       1730       1740 
SRSLRSRQVA PAIEKVQAKF ERTCCSPKYG SPKLQRKPLP KADQPNNRTS PGMAQKGYSE 

      1750       1760       1770       1780       1790       1800 
SAWARSTTTR ESPVHTTIND GLSSLFNIID HSPVVQDPFQ KGLRAGSRSR SAEPRPELGP 

      1810       1820       1830       1840       1850       1860 
GQETGTNSRG RSPSPIGVGS EMCREEGGEG TPVKQDLSAP PGYTLTENVA RILNKKLLEH 

      1870       1880       1890       1900 
ALKEERRQAA HGPPGLHSDS HSLGDTAEPG PMENQTVLLT APWGL 

« Hide

Isoform 2 [UniParc].

Checksum: DF457AEFCFAFB40A
Show »

FASTA1,545173,310
Isoform 3 [UniParc].

Checksum: 1D44ACAC4C4977A3
Show »

FASTA1,586177,945
Isoform 4 [UniParc].

Checksum: F49E33A334D49052
Show »

FASTA976108,707

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11841.1. [Q9Y4B5-3]
RefSeqNP_056025.2. NM_015210.3. [Q9Y4B5-3]
XP_005258156.1. XM_005258099.2. [Q9Y4B5-1]
UniGeneHs.707920.

3D structure databases

ProteinModelPortalQ9Y4B5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116859. 8 interactions.
IntActQ9Y4B5. 8 interactions.
MINTMINT-7945170.
STRING9606.ENSP00000352927.

PTM databases

PhosphoSiteQ9Y4B5.

Polymorphism databases

DMDM384872711.

Proteomic databases

MaxQBQ9Y4B5.
PaxDbQ9Y4B5.
PRIDEQ9Y4B5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306285; ENSP00000303670; ENSG00000168502. [Q9Y4B5-4]
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]
GeneID23255.
KEGGhsa:23255.
UCSCuc002knq.2. human. [Q9Y4B5-1]
uc002knr.2. human. [Q9Y4B5-3]
uc002kns.2. human. [Q9Y4B5-4]

Organism-specific databases

CTD23255.
GeneCardsGC18P008708.
HGNCHGNC:29121. MTCL1.
HPAHPA046245.
MIM615766. gene.
neXtProtNX_Q9Y4B5.
PharmGKBPA128394616.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80576.
HOVERGENHBG080205.
OMAPIGNLGK.
OrthoDBEOG70GMF8.
TreeFamTF331853.

Gene expression databases

ArrayExpressQ9Y4B5.
BgeeQ9Y4B5.
CleanExHS_KIAA0802.
GenevestigatorQ9Y4B5.

Family and domain databases

InterProIPR027882. DUF4482.
IPR027881. SOGA.
[Graphical view]
PfamPF11365. DUF3166. 2 hits.
PF14818. DUF4482. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKIAA0802.
GenomeRNAi23255.
NextBio44978.
PROQ9Y4B5.
SOURCESearch...

Entry information

Entry nameMTCL1_HUMAN
AccessionPrimary (citable) accession number: Q9Y4B5
Secondary accession number(s): E9PAY7, Q6ZMQ9, Q8IWA9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: April 18, 2012
Last modified: July 9, 2014
This is version 95 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM