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Protein

Microtubule-associated protein 9

Gene

MAP9

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

Functioni

Involved in organization of the bipolar mitotic spindle. Required for bipolar spindle assembly, mitosis progression and cytokinesis. May act by stabilizing interphase microtubules.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

SIGNORiQ49MG5.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 9
Alternative name(s):
Aster-associated protein
Gene namesi
Name:MAP9
Synonyms:ASAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:26118. MAP9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148442.

Polymorphism and mutation databases

BioMutaiMAP9.
DMDMi116242626.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 647646Microtubule-associated protein 9PRO_0000247753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei12 – 121PhosphotyrosineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ49MG5.
MaxQBiQ49MG5.
PaxDbiQ49MG5.
PeptideAtlasiQ49MG5.
PRIDEiQ49MG5.

PTM databases

iPTMnetiQ49MG5.
PhosphoSiteiQ49MG5.

Expressioni

Developmental stagei

Constitutively expressed during the cell cycle.1 Publication

Gene expression databases

BgeeiQ49MG5.
CleanExiHS_MAP9.
ExpressionAtlasiQ49MG5. baseline and differential.
GenevisibleiQ49MG5. HS.

Organism-specific databases

HPAiHPA037864.

Interactioni

Subunit structurei

Binds to purified microtubules via its C-terminus.

Protein-protein interaction databases

BioGridi122969. 7 interactions.
IntActiQ49MG5. 3 interactions.
STRINGi9606.ENSP00000310593.

Structurei

3D structure databases

ProteinModelPortaliQ49MG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili184 – 21027Sequence analysisAdd
BLAST
Coiled coili298 – 32831Sequence analysisAdd
BLAST
Coiled coili443 – 628186Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGGW. Eukaryota.
ENOG4111X21. LUCA.
GeneTreeiENSGT00730000111184.
HOGENOMiHOG000113480.
HOVERGENiHBG081953.
InParanoidiQ49MG5.
KOiK10434.
OMAiKEAFFKQ.
OrthoDBiEOG7RRF7V.
PhylomeDBiQ49MG5.
TreeFamiTF328794.

Family and domain databases

InterProiIPR026106. MAP9.
[Graphical view]
PANTHERiPTHR14739. PTHR14739. 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. AlignAdd to basket

Isoform 1 (identifier: Q49MG5-1) [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
MSDEVFSTTL AYTKSPKVTK RTTFQDELIR AITARSARQR SSEYSDDFDS
60 70 80 90 100
DEIVSLGDFS DTSADENSVN KKMNDFHISD DEEKNPSKLL FLKTNKSNGN
110 120 130 140 150
ITKDEPVCAI KNEEEMAPDG CEDIVVKSFS ESQNKDEEFE KDKIKMKPKP
160 170 180 190 200
RILSIKSTSS AENNSLDTDD HFKPSPRPRS MLKKKSHMEE KDGLEDKETA
210 220 230 240 250
LSEELELHSA PSSLPTPNGI QLEAEKKAFS ENLDPEDSCL TSLASSSLKQ
260 270 280 290 300
ILGDSFSPGS EGNASGKDPN EEITENHNSL KSDENKENSF SADHVTTAVE
310 320 330 340 350
KSKESQVTAD DLEEEKAKAE LIMDDDRTVD PLLSKSQSIL ISTSATASSK
360 370 380 390 400
KTIEDRNIKN KKSTNNRASS ASARLMTSEF LKKSSSKRRT PSTTTSSHYL
410 420 430 440 450
GTLKVLDQKP SQKQSIEPDR ADNIRAAVYQ EWLEKKNVYL HEMHRIKRIE
460 470 480 490 500
SENLRIQNEQ KKAAKREEAL ASFEAWKAMK EKEAKKIAAK KRLEEKNKKK
510 520 530 540 550
TEEENAARKG EALQAFEKWK EKKMEYLKEK NRKEREYERA KKQKEEETVA
560 570 580 590 600
EKKKDNLTAV EKWNEKKEAF FKQKEKEKIN EKRKEELKRA EKKDKDKQAI
610 620 630 640
NEYEKWLENK EKQERIERKQ KKRHSFLESE ALPPWSPPSR TVFAKVF
Length:647
Mass (Da):74,234
Last modified:October 17, 2006 - v3
Checksum:i1F0BDE2986845B39
GO
Isoform 2 (identifier: Q49MG5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     374-377: RLMT → ARSG
     378-647: Missing.

Note: No experimental confirmation available.
Show »
Length:377
Mass (Da):41,582
Checksum:iB76E5EBED1224B79
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161M → L in BAB14978 (PubMed:14702039).Curated
Sequence conflicti450 – 4501E → G in BAB14978 (PubMed:14702039).Curated
Sequence conflicti575 – 5751E → K in AAW02921 (PubMed:16049101).Curated
Sequence conflicti631 – 6311A → T in CAH18129 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461M → V.
Corresponds to variant rs34082815 [ dbSNP | Ensembl ].
VAR_051152
Natural varianti177 – 1771R → W.2 Publications
Corresponds to variant rs3733391 [ dbSNP | Ensembl ].
VAR_027151
Natural varianti499 – 4991K → R.
Corresponds to variant rs1058992 [ dbSNP | Ensembl ].
VAR_051153
Natural varianti601 – 6011N → D.1 Publication
Corresponds to variant rs2305050 [ dbSNP | Ensembl ].
VAR_051154

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei374 – 3774RLMT → ARSG in isoform 2. 1 PublicationVSP_020037
Alternative sequencei378 – 647270Missing in isoform 2. 1 PublicationVSP_020038Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY690636 mRNA. Translation: AAW02921.1.
AK024730 mRNA. Translation: BAB14978.1. Sequence problems.
AK024812 mRNA. Translation: BAB15017.1.
AC097467 Genomic DNA. Translation: AAY40981.1.
CR749274 mRNA. Translation: CAH18129.1.
CCDSiCCDS35493.1. [Q49MG5-1]
RefSeqiNP_001034669.1. NM_001039580.1. [Q49MG5-1]
XP_011530555.1. XM_011532253.1. [Q49MG5-1]
XP_011530556.1. XM_011532254.1. [Q49MG5-1]
UniGeneiHs.61271.

Genome annotation databases

EnsembliENST00000311277; ENSP00000310593; ENSG00000164114. [Q49MG5-1]
GeneIDi79884.
KEGGihsa:79884.
UCSCiuc003ios.4. human. [Q49MG5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY690636 mRNA. Translation: AAW02921.1.
AK024730 mRNA. Translation: BAB14978.1. Sequence problems.
AK024812 mRNA. Translation: BAB15017.1.
AC097467 Genomic DNA. Translation: AAY40981.1.
CR749274 mRNA. Translation: CAH18129.1.
CCDSiCCDS35493.1. [Q49MG5-1]
RefSeqiNP_001034669.1. NM_001039580.1. [Q49MG5-1]
XP_011530555.1. XM_011532253.1. [Q49MG5-1]
XP_011530556.1. XM_011532254.1. [Q49MG5-1]
UniGeneiHs.61271.

3D structure databases

ProteinModelPortaliQ49MG5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122969. 7 interactions.
IntActiQ49MG5. 3 interactions.
STRINGi9606.ENSP00000310593.

PTM databases

iPTMnetiQ49MG5.
PhosphoSiteiQ49MG5.

Polymorphism and mutation databases

BioMutaiMAP9.
DMDMi116242626.

Proteomic databases

EPDiQ49MG5.
MaxQBiQ49MG5.
PaxDbiQ49MG5.
PeptideAtlasiQ49MG5.
PRIDEiQ49MG5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311277; ENSP00000310593; ENSG00000164114. [Q49MG5-1]
GeneIDi79884.
KEGGihsa:79884.
UCSCiuc003ios.4. human. [Q49MG5-1]

Organism-specific databases

CTDi79884.
GeneCardsiMAP9.
H-InvDBHIX0004589.
HGNCiHGNC:26118. MAP9.
HPAiHPA037864.
MIMi610070. gene.
neXtProtiNX_Q49MG5.
PharmGKBiPA145148442.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGGW. Eukaryota.
ENOG4111X21. LUCA.
GeneTreeiENSGT00730000111184.
HOGENOMiHOG000113480.
HOVERGENiHBG081953.
InParanoidiQ49MG5.
KOiK10434.
OMAiKEAFFKQ.
OrthoDBiEOG7RRF7V.
PhylomeDBiQ49MG5.
TreeFamiTF328794.

Enzyme and pathway databases

SIGNORiQ49MG5.

Miscellaneous databases

ChiTaRSiMAP9. human.
GenomeRNAii79884.
PROiQ49MG5.
SOURCEiSearch...

Gene expression databases

BgeeiQ49MG5.
CleanExiHS_MAP9.
ExpressionAtlasiQ49MG5. baseline and differential.
GenevisibleiQ49MG5. HS.

Family and domain databases

InterProiIPR026106. MAP9.
[Graphical view]
PANTHERiPTHR14739. PTHR14739. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ASAP, a human microtubule-associated protein required for bipolar spindle assembly and cytokinesis."
    Saffin J.-M., Venoux M., Prigent C., Espeut J., Poulat F., Giorgi D., Abrieu A., Rouquier S.
    Proc. Natl. Acad. Sci. U.S.A. 102:11302-11307(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, VARIANT TRP-177.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-574 (ISOFORM 1), VARIANT TRP-177.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 456-647, VARIANT ASP-601.
    Tissue: Amygdala.
  5. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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 TYR-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiMAP9_HUMAN
AccessioniPrimary (citable) accession number: Q49MG5
Secondary accession number(s): Q4W5I7
, Q68DU1, Q9H781, Q9H7B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 17, 2006
Last modified: July 6, 2016
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.