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Q66K74

- MAP1S_HUMAN

UniProt

Q66K74 - MAP1S_HUMAN

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Protein

Microtubule-associated protein 1S

Gene

MAP1S

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. actin filament binding Source: HGNC
  2. beta-tubulin binding Source: HGNC
  3. DNA binding Source: HGNC
  4. microtubule binding Source: HGNC
  5. tubulin binding Source: HGNC

GO - Biological processi

  1. apoptotic DNA fragmentation Source: BHF-UCL
  2. brain development Source: HGNC
  3. execution phase of apoptosis Source: BHF-UCL
  4. microtubule bundle formation Source: HGNC
  5. mitochondrion transport along microtubule Source: HGNC
  6. nervous system development Source: HGNC
  7. neuron projection morphogenesis Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:MAP1S
Synonyms:BPY2IP1, C19orf5, MAP8, VCY2IP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:15715. MAP1S.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cell junction Source: HPA
  2. cell projection Source: UniProtKB
  3. cytoplasm Source: HPA
  4. cytosol Source: HGNC
  5. dendrite Source: HGNC
  6. microtubule Source: UniProtKB
  7. neuronal cell body Source: HGNC
  8. nucleolus Source: HPA
  9. nucleus Source: HGNC
  10. perinuclear region of cytoplasm Source: HGNC
  11. synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38031.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10591059Microtubule-associated protein 1SPRO_0000311379Add
BLAST
Chaini1 – 829829MAP1S heavy chainPRO_0000311380Add
BLAST
Chaini830 – 1059230MAP1S light chainPRO_0000311381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei472 – 4721Phosphoserine3 Publications
Modified residuei640 – 6401Phosphoserine1 Publication
Modified residuei657 – 6571Phosphoserine2 Publications
Modified residuei759 – 7591Phosphoserine5 Publications
Modified residuei809 – 8091Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ66K74.
PaxDbiQ66K74.
PRIDEiQ66K74.

PTM databases

PhosphoSiteiQ66K74.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiQ66K74.
ExpressionAtlasiQ66K74. baseline and differential.
GenevestigatoriQ66K74.

Organism-specific databases

HPAiHPA050934.
HPA054637.

Interactioni

Subunit structurei

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).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BPY2BO145993EBI-2133734,EBI-2133713
SOCS3O145436EBI-2133734,EBI-714146

Protein-protein interaction databases

BioGridi120498. 20 interactions.
IntActiQ66K74. 17 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ66K74.
SMRiQ66K74. Positions 247-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 797797Necessary for the microtubule-organizing center localizationAdd
BLAST
Regioni666 – 1059394Necessary for interaction with RASSF1 isoform A and isoform CAdd
BLAST
Regioni714 – 966253Necessary for association with microtubulesAdd
BLAST
Regioni960 – 1059100Necessary for association with actinBy similarityAdd
BLAST
Regioni967 – 99125Necessary for the mitochondrial aggregation and genome destructionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi560 – 850291Pro-richAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the MAP1 family.Curated

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074593.
HOVERGENiHBG108117.
InParanoidiQ66K74.
KOiK10429.
OMAiPCEFEHR.
OrthoDBiEOG773XKP.
PhylomeDBiQ66K74.
TreeFamiTF350229.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR026074. MAP1.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q66K74-1) [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
MAAVAGSGAA AAPSSLLLVV GSEFGSPGLL TYVLEELERG IRSWDVDPGV
60 70 80 90 100
CNLDEQLKVF VSRHSATFSS IVKGQRSLHH RGDNLETLVL LNPSDKSLYD
110 120 130 140 150
ELRNLLLDPA SHKLLVLAGP CLEETGELLL QTGGFSPHHF LQVLKDREIR
160 170 180 190 200
DILATTPPPV QPPILTITCP TFGDWAQLAP AVPGLQGALR LQLRLNPPAQ
210 220 230 240 250
LPNSEGLCEF LEYVAESLEP PSPFELLEPP TSGGFLRLGR PCCYIFPGGL
260 270 280 290 300
GDAAFFAVNG FTVLVNGGSN PKSSFWKLVR HLDRVDAVLV THPGADSLPG
310 320 330 340 350
LNSLLRRKLA ERSEVAAGGG SWDDRLRRLI SPNLGVVFFN ACEAASRLAR
360 370 380 390 400
GEDEAELALS LLAQLGITPL PLSRGPVPAK PTVLFEKMGV GRLDMYVLHP
410 420 430 440 450
PSAGAERTLA SVCALLVWHP AGPGEKVVRV LFPGCTPPAC LLDGLVRLQH
460 470 480 490 500
LRFLREPVVT PQDLEGPGRA ESKESVGSRD SSKREGLLAT HPRPGQERPG
510 520 530 540 550
VARKEPARAE APRKTEKEAK TPRELKKDPK PSVSRTQPRE VRRAASSVPN
560 570 580 590 600
LKKTNAQAAP KPRKAPSTSH SGFPPVANGP RSPPSLRCGE ASPPSAACGS
610 620 630 640 650
PASQLVATPS LELGPIPAGE EKALELPLAA SSIPRPRTPS PESHRSPAEG
660 670 680 690 700
SERLSLSPLR GGEAGPDASP TVTTPTVTTP SLPAEVGSPH STEVDESLSV
710 720 730 740 750
SFEQVLPPSA PTSEAGLSLP LRGPRARRSA SPHDVDLCLV SPCEFEHRKA
760 770 780 790 800
VPMAPAPASP GSSNDSSARS QERAGGLGAE ETPPTSVSES LPTLSDSDPV
810 820 830 840 850
PLAPGAADSD EDTEGFGVPR HDPLPDPLKV PPPLPDPSSI CMVDPEMLPP
860 870 880 890 900
KTARQTENVS RTRKPLARPN SRAAAPKATP VAAAKTKGLA GGDRASRPLS
910 920 930 940 950
ARSEPSEKGG RAPLSRKSST PKTATRGPSG SASSRPGVSA TPPKSPVYLD
960 970 980 990 1000
LAYLPSGSSA HLVDEEFFQR VRALCYVISG QDQRKEEGMR AVLDALLASK
1010 1020 1030 1040 1050
QHWDRDLQVT LIPTFDSVAM HTWYAETHAR HQALGITVLG SNSMVSMQDD

AFPACKVEF
Length:1,059
Mass (Da):112,211
Last modified:November 13, 2007 - v2
Checksum:i30AB33FFE26DDF91
GO
Isoform 2 (identifier: Q66K74-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MAAVAGSGAAAAPSSLLLVVGSEFGSPGLLTYVLEELER → MAGMIDRFSPANT

Note: No experimental confirmation available.

Show »
Length:1,033
Mass (Da):109,788
Checksum:i0CCD0392292B2B08
GO

Sequence cautioni

The sequence AAH07253.1 differs from that shown. Reason: Contaminating sequence. At the N-terminus.Curated
The sequence AAH07253.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH67115.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA91743.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB14415.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB55242.1 differs from that shown. Reason: Frameshift at position 851. Curated
The sequence BAB93493.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAD38911.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201P → L in CAD29574. (PubMed:14627543)Curated
Sequence conflicti120 – 1201P → L in BAB55242. (PubMed:14702039)Curated
Sequence conflicti178 – 1781L → P in CAD29574. (PubMed:14627543)Curated
Sequence conflicti178 – 1781L → P in BAB55242. (PubMed:14702039)Curated
Sequence conflicti440 – 4401C → Y in CAD38911. (PubMed:17974005)Curated
Sequence conflicti521 – 5211T → A in BAB93493. 1 PublicationCurated
Sequence conflicti526 – 5261K → R in CAD29574. (PubMed:14627543)Curated
Sequence conflicti526 – 5261K → R in BAB55242. (PubMed:14702039)Curated
Sequence conflicti967 – 9671F → L in BAB14415. (PubMed:14702039)Curated
Sequence conflicti1043 – 10431S → G in BAA91743. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti372 – 3721L → V.
Corresponds to variant rs17710707 [ dbSNP | Ensembl ].
VAR_050023
Natural varianti411 – 4111S → C.1 Publication
Corresponds to variant rs17710707 [ dbSNP | Ensembl ].
VAR_037236
Natural varianti538 – 5381P → Q.
Corresponds to variant rs7252905 [ dbSNP | Ensembl ].
VAR_037237

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939MAAVA…EELER → MAGMIDRFSPANT in isoform 2. 1 PublicationVSP_056043Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK294936 mRNA. Translation: BAG58014.1.
AL834233 mRNA. Translation: CAD38911.1. Different initiation.
AC008761 Genomic DNA. No translation available.
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.
CCDSiCCDS32954.1. [Q66K74-1]
RefSeqiNP_060644.4. NM_018174.4. [Q66K74-1]
UniGeneiHs.66048.

Genome annotation databases

EnsembliENST00000324096; ENSP00000325313; ENSG00000130479. [Q66K74-1]
ENST00000544059; ENSP00000439243; ENSG00000130479. [Q66K74-2]
GeneIDi55201.
KEGGihsa:55201.
UCSCiuc002nhe.1. human. [Q66K74-1]

Polymorphism databases

DMDMi160410004.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK294936 mRNA. Translation: BAG58014.1 .
AL834233 mRNA. Translation: CAD38911.1 . Different initiation.
AC008761 Genomic DNA. No translation available.
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.
CCDSi CCDS32954.1. [Q66K74-1 ]
RefSeqi NP_060644.4. NM_018174.4. [Q66K74-1 ]
UniGenei Hs.66048.

3D structure databases

ProteinModelPortali Q66K74.
SMRi Q66K74. Positions 247-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120498. 20 interactions.
IntActi Q66K74. 17 interactions.

PTM databases

PhosphoSitei Q66K74.

Polymorphism databases

DMDMi 160410004.

Proteomic databases

MaxQBi Q66K74.
PaxDbi Q66K74.
PRIDEi Q66K74.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324096 ; ENSP00000325313 ; ENSG00000130479 . [Q66K74-1 ]
ENST00000544059 ; ENSP00000439243 ; ENSG00000130479 . [Q66K74-2 ]
GeneIDi 55201.
KEGGi hsa:55201.
UCSCi uc002nhe.1. human. [Q66K74-1 ]

Organism-specific databases

CTDi 55201.
GeneCardsi GC19P017932.
H-InvDB HIX0014899.
HGNCi HGNC:15715. MAP1S.
HPAi HPA050934.
HPA054637.
MIMi 607573. gene.
neXtProti NX_Q66K74.
PharmGKBi PA38031.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00550000074593.
HOVERGENi HBG108117.
InParanoidi Q66K74.
KOi K10429.
OMAi PCEFEHR.
OrthoDBi EOG773XKP.
PhylomeDBi Q66K74.
TreeFami TF350229.

Miscellaneous databases

ChiTaRSi MAP1S. human.
GeneWikii MAP1S.
GenomeRNAii 55201.
NextBioi 35471927.
PROi Q66K74.
SOURCEi Search...

Gene expression databases

Bgeei Q66K74.
ExpressionAtlasi Q66K74. baseline and differential.
Genevestigatori Q66K74.

Family and domain databases

Gene3Di 3.60.15.10. 2 hits.
InterProi IPR001279. Beta-lactamas-like.
IPR026074. MAP1.
[Graphical view ]
PANTHERi PTHR13843. PTHR13843. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1), VARIANT CYS-411.
    Tissue: Brain, Lung, Lymph and Muscle.
  7. "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 (ISOFORM 1/2).
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. 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.
  21. "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].
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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.
  24. "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.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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].
  27. Cited for: INTERACTION WITH WDR47.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP1S_HUMAN
AccessioniPrimary (citable) accession number: Q66K74
Secondary accession number(s): B4DH53
, Q27QB1, Q6NXF1, Q8N3L8, Q8N3W5, Q8NI88, Q96H94, Q96IT4, Q96SP8, Q9BRC6, Q9H928, Q9NVK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: November 26, 2014
This is version 96 of the entry and version 2 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

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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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