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Q66K74 (MAP1S_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein 1S

Short name=MAP-1S
Alternative name(s):
BPY2-interacting protein 1
Microtubule-associated protein 8
Variable charge Y chromosome 2-interacting protein 1
Short name=VCY2-interacting protein 1
Short name=VCY2IP-1

Cleaved into the following 2 chains:

  1. MAP1S heavy chain
  2. MAP1S light chain
Gene names
Name:MAP1S
Synonyms:BPY2IP1, C19orf5, MAP8, VCY2IP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1059 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles By similarity. Ref.12 Ref.15

Subunit structure

Heterodimer of a heavy and a light chain. Interacts with microtubules and actin. Both MAP1S heavy and light chains interact with microtubules. MAP1S light chain interacts with actin. Interacts (via C-terminus) with GAN (via Kelch domains) By similarity. Interacts with ESR1, LRPPRC, RASSF1 isoform Aand isoform C microtubules and VCY2. Interacts with WDR47 (via N-terminus of light chain). Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.26

Subcellular location

Nucleus. Cytoplasmcytosol. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonspindle. Note: Detected in filopodia-like protrusions and synapses By similarity. Detected in perinuclear punctate network corresponding to mitochondrial aggregates and in the nucleus in cells exhibiting apoptosis. Associated specifically with microtubules stabilized by paclitaxel and colocalizes with RASSF1 isoform A In interphase cells, shows a diffuse cytoplasmic staining with partial localization to the microtubules. During the different stages of mitosis detected at the spindle microtubules. Ref.8 Ref.11 Ref.12 Ref.15

Tissue specificity

Expressed in neurons (at protein level). Expressed in spermatocytes, spermatids and spermatozoa. Expressed in the cerebral cortex. Highly expressed in testis. Moderately expressed in the brain, colon, heart, kidney, liver, lung, placenta, small intestine, spleen and stomach. Weakly expressed in muscle. Ref.1 Ref.7 Ref.14

Domain

The N-terminus of the heavy chain associates with the C-terminus of the light chain to form the heterodimer complex By similarity. Its C-terminal part of the heavy chain interacts with ESR1.

Miscellaneous

Depletion of MAP1S by RNAi causes mitotic abnormalities that consist of failure to form a stable metaphase plate, premature sister chromatid separation, lagging chromosomes, and multipolar spindles.

Sequence similarities

Belongs to the MAP1 family.

Sequence caution

The sequence AAH07253.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH07253.1 differs from that shown. Reason: Contaminating sequence. At the N-terminus.

The sequence AAH67115.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91743.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB14415.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB55242.1 differs from that shown. Reason: Frameshift at position 851.

The sequence BAB93493.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD38911.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic DNA fragmentation

Traceable author statement Ref.8. Source: BHF-UCL

brain development

Inferred from sequence or structural similarity PubMed 15528209. Source: HGNC

execution phase of apoptosis

Inferred from direct assay Ref.8. Source: BHF-UCL

microtubule bundle formation

Inferred from mutant phenotype PubMed 15528209. Source: HGNC

mitochondrion transport along microtubule

Traceable author statement Ref.8. Source: HGNC

nervous system development

Inferred from sequence or structural similarity Ref.2. Source: HGNC

neuron projection morphogenesis

Inferred from expression pattern PubMed 15528209. Source: HGNC

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

cell projection

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.8. Source: HGNC

dendrite

Inferred from sequence or structural similarity PubMed 15528209. Source: HGNC

microtubule

Inferred from direct assay Ref.14. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity PubMed 15528209. Source: HGNC

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.8. Source: HGNC

perinuclear region of cytoplasm

Inferred from direct assay Ref.8. Source: HGNC

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.10. Source: HGNC

actin filament binding

Inferred from direct assay PubMed 15528209. Source: HGNC

beta-tubulin binding

Inferred from direct assay Ref.8. Source: HGNC

hydrolase activity

Inferred from electronic annotation. Source: InterPro

microtubule binding

Inferred from direct assay PubMed 15528209. Source: HGNC

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

tubulin binding

Inferred from direct assay PubMed 15528209. Source: HGNC

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10591059Microtubule-associated protein 1S
PRO_0000311379
Chain1 – 829829MAP1S heavy chain
PRO_0000311380
Chain830 – 1059230MAP1S light chain
PRO_0000311381

Regions

Region1 – 797797Necessary for the microtubule-organizing center localization
Region666 – 1059394Necessary for interaction with RASSF1 isoform A and isoform C
Region714 – 966253Necessary for association with microtubules
Region960 – 1059100Necessary for association with actin By similarity
Region967 – 99125Necessary for the mitochondrial aggregation and genome destruction
Compositional bias560 – 850291Pro-rich

Amino acid modifications

Modified residue4721Phosphoserine Ref.13 Ref.19 Ref.25
Modified residue6401Phosphoserine Ref.19
Modified residue6571Phosphoserine Ref.19 Ref.25
Modified residue7591Phosphoserine Ref.17 Ref.19 Ref.21 Ref.23 Ref.25
Modified residue8091Phosphoserine Ref.23 Ref.25

Natural variations

Natural variant3721L → V.
Corresponds to variant rs17710707 [ dbSNP | Ensembl ].
VAR_050023
Natural variant4111S → C. Ref.5
Corresponds to variant rs17710707 [ dbSNP | Ensembl ].
VAR_037236
Natural variant5381P → Q.
Corresponds to variant rs7252905 [ dbSNP | Ensembl ].
VAR_037237

Experimental info

Sequence conflict1201P → L in CAD29574. Ref.1
Sequence conflict1201P → L in BAB55242. Ref.3
Sequence conflict1781L → P in CAD29574. Ref.1
Sequence conflict1781L → P in BAB55242. Ref.3
Sequence conflict4401C → Y in CAD38911. Ref.4
Sequence conflict5211T → A in BAB93493. Ref.6
Sequence conflict5261K → R in CAD29574. Ref.1
Sequence conflict5261K → R in BAB55242. Ref.3
Sequence conflict9671F → L in BAB14415. Ref.3
Sequence conflict10431S → G in BAA91743. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q66K74 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 30AB33FFE26DDF91

FASTA1,059112,211
        10         20         30         40         50         60 
MAAVAGSGAA AAPSSLLLVV GSEFGSPGLL TYVLEELERG IRSWDVDPGV CNLDEQLKVF 

        70         80         90        100        110        120 
VSRHSATFSS IVKGQRSLHH RGDNLETLVL LNPSDKSLYD ELRNLLLDPA SHKLLVLAGP 

       130        140        150        160        170        180 
CLEETGELLL QTGGFSPHHF LQVLKDREIR DILATTPPPV QPPILTITCP TFGDWAQLAP 

       190        200        210        220        230        240 
AVPGLQGALR LQLRLNPPAQ LPNSEGLCEF LEYVAESLEP PSPFELLEPP TSGGFLRLGR 

       250        260        270        280        290        300 
PCCYIFPGGL GDAAFFAVNG FTVLVNGGSN PKSSFWKLVR HLDRVDAVLV THPGADSLPG 

       310        320        330        340        350        360 
LNSLLRRKLA ERSEVAAGGG SWDDRLRRLI SPNLGVVFFN ACEAASRLAR GEDEAELALS 

       370        380        390        400        410        420 
LLAQLGITPL PLSRGPVPAK PTVLFEKMGV GRLDMYVLHP PSAGAERTLA SVCALLVWHP 

       430        440        450        460        470        480 
AGPGEKVVRV LFPGCTPPAC LLDGLVRLQH LRFLREPVVT PQDLEGPGRA ESKESVGSRD 

       490        500        510        520        530        540 
SSKREGLLAT HPRPGQERPG VARKEPARAE APRKTEKEAK TPRELKKDPK PSVSRTQPRE 

       550        560        570        580        590        600 
VRRAASSVPN LKKTNAQAAP KPRKAPSTSH SGFPPVANGP RSPPSLRCGE ASPPSAACGS 

       610        620        630        640        650        660 
PASQLVATPS LELGPIPAGE EKALELPLAA SSIPRPRTPS PESHRSPAEG SERLSLSPLR 

       670        680        690        700        710        720 
GGEAGPDASP TVTTPTVTTP SLPAEVGSPH STEVDESLSV SFEQVLPPSA PTSEAGLSLP 

       730        740        750        760        770        780 
LRGPRARRSA SPHDVDLCLV SPCEFEHRKA VPMAPAPASP GSSNDSSARS QERAGGLGAE 

       790        800        810        820        830        840 
ETPPTSVSES LPTLSDSDPV PLAPGAADSD EDTEGFGVPR HDPLPDPLKV PPPLPDPSSI 

       850        860        870        880        890        900 
CMVDPEMLPP KTARQTENVS RTRKPLARPN SRAAAPKATP VAAAKTKGLA GGDRASRPLS 

       910        920        930        940        950        960 
ARSEPSEKGG RAPLSRKSST PKTATRGPSG SASSRPGVSA TPPKSPVYLD LAYLPSGSSA 

       970        980        990       1000       1010       1020 
HLVDEEFFQR VRALCYVISG QDQRKEEGMR AVLDALLASK QHWDRDLQVT LIPTFDSVAM 

      1030       1040       1050 
HTWYAETHAR HQALGITVLG SNSMVSMQDD AFPACKVEF 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a VCY2 interacting protein-1; VCY2IP-1, a MAP-like protein."
Wong E.Y., Tse J.Y., Yao K.-M., Lui V.C., Tam P.-C., Yeung W.S.
Biol. Reprod. 70:775-784(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH VCY2, TISSUE SPECIFICITY.
Tissue: Testis.
[2]"Microtubule-associated protein 8 contains two microtubule binding sites."
Ding J., Valle A., Allen E., Wang W., Nardine T., Zhang Y., Peng L., Yang Y.
Biochem. Biophys. Res. Commun. 339:172-179(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala.
[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], VARIANT CYS-411.
Tissue: Brain, Lung, Lymph and Muscle.
[6]"Identification of immuno-peptidmics that recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 314-1059.
[7]"Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity."
Liu L., McKeehan W.L.
Genomics 79:124-136(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRPPRC, TISSUE SPECIFICITY.
[8]"Novel complex integrating mitochondria and the microtubular cytoskeleton with chromosome remodeling and tumor suppressor RASSF1 deduced by in silico homology analysis, interaction cloning in yeast, and colocalization in cultured cells."
Liu L., Amy V., Liu G., McKeehan W.L.
In Vitro Cell. Dev. Biol. Anim. 38:582-594(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRPPRC, SUBCELLULAR LOCATION.
[9]"RASSF1A interacts with microtubule-associated proteins and modulates microtubule dynamics."
Dallol A., Agathanggelou A., Fenton S.L., Ahmed-Choudhury J., Hesson L., Vos M.D., Clark G.J., Downward J., Maher E.R., Latif F.
Cancer Res. 64:4112-4116(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASSF1.
[10]"Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein."
Liu L., Vo A., Liu G., McKeehan W.L.
Biochem. Biophys. Res. Commun. 332:670-676(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRPPRC, DNA-BINDING.
[11]"Specificity of the methylation-suppressed A isoform of candidate tumor suppressor RASSF1 for microtubule hyperstabilization is determined by cell death inducer C19ORF5."
Liu L., Vo A., McKeehan W.L.
Cancer Res. 65:1830-1838(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASSF1, SUBCELLULAR LOCATION.
[12]"Distinct structural domains within C19ORF5 support association with stabilized microtubules and mitochondrial aggregation and genome destruction."
Liu L., Vo A., Liu G., McKeehan W.L.
Cancer Res. 65:4191-4201(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain."
Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L., Benedikz E., Sundstroem E.
Biochem. Biophys. Res. Commun. 361:127-132(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ESR1, TISSUE SPECIFICITY.
[15]"Depletion of the Ras association domain family 1, isoform A-associated novel microtubule-associated protein, C19ORF5/MAP1S, causes mitotic abnormalities."
Dallol A., Cooper W.N., Al-Mulla F., Agathanggelou A., Maher E.R., Latif F.
Cancer Res. 67:492-500(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site."
Zou B., Yan H., Kawasaki F., Ordway R.W.
Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE SITE.
[17]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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-472; SER-640; SER-657 AND SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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].
[21]"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-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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.
[23]"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-759 AND SER-809, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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-472; SER-657; SER-759 AND SER-809, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Nemitin, a novel Map8/Map1s interacting protein with Wd40 repeats."
Wang W., Lundin V.F., Millan I., Zeng A., Chen X., Yang J., Allen E., Chen N., Bach G., Hsu A., Maloney M.T., Kapur M., Yang Y.
PLoS ONE 7:E33094-E33094(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WDR47.
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ440784 mRNA. Translation: CAD29574.1.
DQ387861 mRNA. Translation: ABD47682.1.
AK027623 mRNA. Translation: BAB55242.1. Frameshift.
AK001531 mRNA. Translation: BAA91743.1. Different initiation.
AK023118 mRNA. Translation: BAB14415.1. Different initiation.
AL834233 mRNA. Translation: CAD38911.1. Different initiation.
BC006358 mRNA. Translation: AAH06358.2.
BC007253 mRNA. Translation: AAH07253.1. Different initiation.
BC008806 mRNA. Translation: AAH08806.2.
BC067115 mRNA. Translation: AAH67115.1. Different initiation.
BC080547 mRNA. Translation: AAH80547.1.
BC113952 mRNA. Translation: AAI13953.1.
AB062430 mRNA. Translation: BAB93493.1. Different initiation.
CCDSCCDS32954.1.
RefSeqNP_060644.4. NM_018174.4.
UniGeneHs.66048.

3D structure databases

ProteinModelPortalQ66K74.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120498. 16 interactions.
IntActQ66K74. 17 interactions.

PTM databases

PhosphoSiteQ66K74.

Polymorphism databases

DMDM160410004.

Proteomic databases

MaxQBQ66K74.
PaxDbQ66K74.
PRIDEQ66K74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324096; ENSP00000325313; ENSG00000130479.
GeneID55201.
KEGGhsa:55201.
UCSCuc002nhe.1. human.

Organism-specific databases

CTD55201.
GeneCardsGC19P017832.
H-InvDBHIX0014899.
HGNCHGNC:15715. MAP1S.
HPAHPA050934.
HPA054637.
MIM607573. gene.
neXtProtNX_Q66K74.
PharmGKBPA38031.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG108117.
InParanoidQ66K74.
KOK10429.
OMAPCEFEHR.
OrthoDBEOG773XKP.
PhylomeDBQ66K74.
TreeFamTF350229.

Gene expression databases

ArrayExpressQ66K74.
BgeeQ66K74.
GenevestigatorQ66K74.

Family and domain databases

Gene3D3.60.15.10. 2 hits.
InterProIPR001279. Beta-lactamas-like.
IPR026074. MAP1.
[Graphical view]
PANTHERPTHR13843. PTHR13843. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAP1S. human.
GeneWikiMAP1S.
GenomeRNAi55201.
NextBio59090.
PROQ66K74.
SOURCESearch...

Entry information

Entry nameMAP1S_HUMAN
AccessionPrimary (citable) accession number: Q66K74
Secondary accession number(s): Q27QB1 expand/collapse secondary AC list , Q6NXF1, Q8N3L8, Q8N3W5, Q8NI88, Q96H94, Q96IT4, Q96SP8, Q9BRC6, Q9H928, Q9NVK7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 93 of the entry and version 2 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 19

Human chromosome 19: entries, gene names and cross-references to MIM