Q66K74 (MAP1S_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1059 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 A and 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.25
Subcellular location	Nucleus. Cytoplasm › cytosol. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › spindle. 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 process	Apoptosis
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from direct assay Ref.8. Source: HGNC brain development Inferred from sequence or structural similarity PubMed 15528209. Source: HGNC microtubule bundle formation Inferred from mutant phenotype PubMed 15528209. Source: HGNC mitochondrion transport along microtubule Traceable author statement Ref.8. Source: HGNC neuron projection morphogenesis Inferred from expression pattern PubMed 15528209. Source: HGNC
Cellular_component	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 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_function	DNA 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 microtubule binding Inferred from direct assay PubMed 15528209. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BPY2B	O14599	3	EBI-2133734,EBI-2133713

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1059	1059	Microtubule-associated protein 1S		PRO_0000311379
	Chain	1 – 829	829	MAP1S heavy chain		PRO_0000311380
	Chain	830 – 1059	230	MAP1S light chain		PRO_0000311381
Regions
	Region	1 – 797	797	Necessary for the microtubule-organizing center localization
	Region	666 – 1059	394	Necessary for interaction with RASSF1 isoform A and isoform C
	Region	714 – 966	253	Necessary for association with microtubules
	Region	960 – 1059	100	Necessary for association with actin By similarity
	Region	967 – 991	25	Necessary for the mitochondrial aggregation and genome destruction
	Compositional bias	560 – 850	291	Pro-rich
Amino acid modifications
	Modified residue	472	1	Phosphoserine Ref.13 Ref.19 Ref.24
	Modified residue	640	1	Phosphoserine Ref.19
	Modified residue	657	1	Phosphoserine Ref.19 Ref.24
	Modified residue	759	1	Phosphoserine Ref.17 Ref.19 Ref.20 Ref.22 Ref.24
	Modified residue	809	1	Phosphoserine Ref.22 Ref.24
	Modified residue	919	1	Phosphoserine By similarity
Natural variations
	Natural variant	372	1	L → V. Corresponds to variant rs17710707 [ dbSNP | Ensembl ].		VAR_050023
	Natural variant	411	1	S → C. Ref.5 Corresponds to variant rs17710707 [ dbSNP | Ensembl ].		VAR_037236
	Natural variant	538	1	P → Q. Corresponds to variant rs7252905 [ dbSNP | Ensembl ].		VAR_037237
Experimental info
	Sequence conflict	120	1	P → L in CAD29574. Ref.1
	Sequence conflict	120	1	P → L in BAB55242. Ref.3
	Sequence conflict	178	1	L → P in CAD29574. Ref.1
	Sequence conflict	178	1	L → P in BAB55242. Ref.3
	Sequence conflict	440	1	C → Y in CAD38911. Ref.4
	Sequence conflict	521	1	T → A in BAB93493. Ref.6
	Sequence conflict	526	1	K → R in CAD29574. Ref.1
	Sequence conflict	526	1	K → R in BAB55242. Ref.3
	Sequence conflict	967	1	F → L in BAB14415. Ref.3
	Sequence conflict	1043	1	S → G in BAA91743. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q66K74 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 30AB33FFE26DDF91	FASTA	1,059	112,211
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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, MASS SPECTROMETRY.
[21]	"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.
[22]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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].
[24]	"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, MASS SPECTROMETRY.
[25]	"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.
+	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.
IPI	IPI00296485.
RefSeq	NP_060644.4. NM_018174.4.
UniGene	Hs.66048.
3D structure databases
ProteinModelPortal	Q66K74.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q66K74. 7 interactions.
PTM databases
PhosphoSite	Q66K74.
Polymorphism databases
DMDM	160410004.
Proteomic databases
PaxDb	Q66K74.
PRIDE	Q66K74.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324096; ENSP00000325313; ENSG00000130479.
GeneID	55201.
KEGG	hsa:55201.
UCSC	uc002nhe.1. human.
Organism-specific databases
CTD	55201.
GeneCards	GC19P017832.
H-InvDB	HIX0014899.
HGNC	HGNC:15715. MAP1S.
HPA	HPA050934. HPA054637.
MIM	607573. gene.
neXtProt	NX_Q66K74.
PharmGKB	PA38031.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG108117.
InParanoid	Q66K74.
KO	K10429.
OMA	LDMYVLH.
OrthoDB	EOG4TF0K2.
Gene expression databases
ArrayExpress	Q66K74.
Bgee	Q66K74.
Genevestigator	Q66K74.
Family and domain databases
InterPro	IPR026074. MAP1. IPR027322. MAP1S. [Graphical view]
PANTHER	PTHR13843. PTHR13843. 1 hit. PTHR13843:SF1. PTHR13843:SF1. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	MAP1S. human.
GenomeRNAi	55201.
NextBio	59090.
SOURCE	Search...

Entry information

Entry name

MAP1S_HUMAN

Accession

Primary (citable) accession number: Q66K74
Secondary accession number(s): Q27QB1 , 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:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.