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Protein

MAP7 domain-containing protein 3

Gene

MAP7D3

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

Functioni

Promotes the assembly and stability of microtubules.2 Publications

GO - Molecular functioni

  1. microtubule binding Source: UniProtKB
  2. structural molecule activity Source: GO_Central
  3. tubulin binding Source: UniProtKB

GO - Biological processi

  1. microtubule cytoskeleton organization Source: UniProtKB
  2. microtubule polymerization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
MAP7 domain-containing protein 3
Gene namesi
Name:MAP7D3
Synonyms:MDP31 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:25742. MAP7D3.

Subcellular locationi

Cytoplasmcytoskeletonspindle 1 Publication
Note: Localizes to the microtubules throughout mitosis.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. centrosome Source: HPA
  3. cytoplasm Source: HPA
  4. membrane Source: UniProtKB
  5. microtubule Source: InterPro
  6. nucleoplasm Source: HPA
  7. nucleus Source: HPA
  8. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162394972.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 876876MAP7 domain-containing protein 3PRO_0000306812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei322 – 3221Phosphoserine1 Publication
Modified residuei457 – 4571Phosphoserine1 Publication
Modified residuei461 – 4611Phosphoserine1 Publication
Modified residuei524 – 5241Phosphoserine1 Publication
Modified residuei770 – 7701Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8IWC1.
PaxDbiQ8IWC1.
PRIDEiQ8IWC1.

PTM databases

PhosphoSiteiQ8IWC1.

Expressioni

Inductioni

Expression is cell cycle dependent with the highest levels during G1, S, and M phases, and low level in G2 phase.1 Publication

Gene expression databases

BgeeiQ8IWC1.
CleanExiHS_MAP7D3.
GenevestigatoriQ8IWC1.

Organism-specific databases

HPAiHPA035598.

Interactioni

Subunit structurei

Interacts (via N-terminus coiled coil domains) with tubulin and microtubules.2 Publications

Protein-protein interaction databases

BioGridi122777. 8 interactions.
IntActiQ8IWC1. 1 interaction.
MINTiMINT-4990235.
STRINGi9606.ENSP00000318086.

Structurei

3D structure databases

ProteinModelPortaliQ8IWC1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili65 – 14480Sequence AnalysisAdd
BLAST
Coiled coili558 – 64083Sequence AnalysisAdd
BLAST
Coiled coili689 – 72436Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the MAP7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG113680.
GeneTreeiENSGT00660000095160.
HOVERGENiHBG103577.
InParanoidiQ8IWC1.
KOiK16807.
OMAiQQDANKE.
OrthoDBiEOG761BTS.
PhylomeDBiQ8IWC1.
TreeFamiTF332273.

Family and domain databases

InterProiIPR008604. MAP7.
[Graphical view]
PANTHERiPTHR15073. PTHR15073. 1 hit.
PfamiPF05672. MAP7. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IWC1-1) [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
MMADGAAAGA GGSPSLRELR ARMVAAANEI AKERRKQDVV NRVATHSSNI
60 70 80 90 100
RSTFKPVIDG SMLKNDIKQR LARERREEKR RQQDANKETQ LLEKERKTKL
110 120 130 140 150
QYEKQMEERQ RKLKERKEKE EQRRIAAEEK RHQKDEAQKE KFTAILYRTL
160 170 180 190 200
ERRRLADDYQ QKRWSWGGSA MANSESKTAN KRSASTEKLE QGTSALIRQM
210 220 230 240 250
PLSSAGLQNS VAKRKTDKER SSSLNRRDSN LHSSTDKEQA ERKPRVTGVT
260 270 280 290 300
NYVMQYVTVP LRKCTSDELR AVMFPMSTMK IPPQTKVEES PLEKVETPPK
310 320 330 340 350
ASVDAPPQVN VEVFCNTSME ASPKAGVGMA PEVSTDSFPV VSVDVSPVVS
360 370 380 390 400
TYDSEMSMDA SPELSIEALP KVDLETVPKV SIVASPEASL EAPPEVSLEA
410 420 430 440 450
LPEVSVEAAP EGSLEAPPKG SAEVAPKESV KGSPKESMEA SPEAMVKASP
460 470 480 490 500
KTSLEASMEA SPKAKARDAP KKSEMDKQAL IPIAKKRLSS YTECYKWSSS
510 520 530 540 550
PENACGLPSP ISTNRQIQKN CPPSPLPLIS KQSPQTSFPY KIMPIQHTLS
560 570 580 590 600
VQSASSTVKK KKETVSKTTN RCEALSQRHM IYEESGNKST AGIMNAEAAT
610 620 630 640 650
KILTELRRLA REQREKEEEE RQREEMQQRV IKKSKDMAKE AVGGQAEDHL
660 670 680 690 700
KLKDGQQQNE TKKKKGWLDQ EDQEAPLQKG DAKIKAQEEA DKRKKEHERI
710 720 730 740 750
MLQNLQERLE RKKRIEEIMK RTRKTDVNAS KVTETSSHDI YEEAEADNEE
760 770 780 790 800
SDKDSLNEMF PSAILNGTGS PTKFKMPFNN AKKMTHKLVF LEDGTSQVRK
810 820 830 840 850
EPKTYFNGDL KNFRQKSMKD TSIQEVVSRP SSKRMTSHTT KTRKADETNT
860 870
TSRSSAQTKS EGFHDILPKS SDTFRQ
Length:876
Mass (Da):98,429
Last modified:October 2, 2007 - v2
Checksum:iC149899FB0002B39
GO
Isoform 2 (identifier: Q8IWC1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     246-286: Missing.

Note: No experimental confirmation available.

Show »
Length:835
Mass (Da):93,785
Checksum:i636105ADE4362780
GO
Isoform 3 (identifier: Q8IWC1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-214: ANKRSASTEKLEQGTSALIRQMPLSSAGLQNSVAKR → G

Note: No experimental confirmation available.

Show »
Length:841
Mass (Da):94,675
Checksum:i991CB99A9EA667C2
GO
Isoform 4 (identifier: Q8IWC1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MMADGAAAGAGGSPSLRELRARM → MTSPR

Note: No experimental confirmation available.

Show »
Length:858
Mass (Da):96,743
Checksum:i46B3C99CFE457147
GO

Sequence cautioni

The sequence AAH64350.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence CAM21578.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711L → S in BAG62994. (PubMed:14702039)Curated
Sequence conflicti447 – 4471K → R in BAG62994. (PubMed:14702039)Curated
Sequence conflicti448 – 4481A → T in AAH40518. (PubMed:15489334)Curated
Sequence conflicti623 – 6231R → Q in AL832120. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti502 – 5021E → A.1 Publication
Corresponds to variant rs1055497 [ dbSNP | Ensembl ].
VAR_035314
Natural varianti628 – 6281Q → R.1 Publication
Corresponds to variant rs2273221 [ dbSNP | Ensembl ].
VAR_035315

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323MMADG…LRARM → MTSPR in isoform 4. 1 PublicationVSP_045008Add
BLAST
Alternative sequencei179 – 21436ANKRS…SVAKR → G in isoform 3. 1 PublicationVSP_028498Add
BLAST
Alternative sequencei246 – 28641Missing in isoform 2. 1 PublicationVSP_028499Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022711 mRNA. Translation: BAB14195.1.
AK301478 mRNA. Translation: BAG62994.1.
AL832120 mRNA. No translation available.
AL078638 Genomic DNA. Translation: CAI41063.2.
AL078638 Genomic DNA. Translation: CAI41064.2.
AL078638 Genomic DNA. Translation: CAM21578.1. Sequence problems.
CH471150 Genomic DNA. Translation: EAW88475.1.
BC040518 mRNA. Translation: AAH40518.1.
BC064350 mRNA. Translation: AAH64350.1. Sequence problems.
CCDSiCCDS44004.1. [Q8IWC1-1]
CCDS55508.1. [Q8IWC1-3]
CCDS55509.1. [Q8IWC1-4]
RefSeqiNP_001166987.1. NM_001173516.1. [Q8IWC1-4]
NP_001166988.1. NM_001173517.1. [Q8IWC1-3]
NP_078873.2. NM_024597.3. [Q8IWC1-1]
UniGeneiHs.446275.

Genome annotation databases

EnsembliENST00000316077; ENSP00000318086; ENSG00000129680. [Q8IWC1-1]
ENST00000370661; ENSP00000359695; ENSG00000129680. [Q8IWC1-3]
ENST00000370663; ENSP00000359697; ENSG00000129680. [Q8IWC1-4]
GeneIDi79649.
KEGGihsa:79649.
UCSCiuc004ezs.3. human. [Q8IWC1-3]
uc004ezt.3. human. [Q8IWC1-1]
uc010nsa.2. human. [Q8IWC1-2]

Polymorphism databases

DMDMi158705880.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022711 mRNA. Translation: BAB14195.1.
AK301478 mRNA. Translation: BAG62994.1.
AL832120 mRNA. No translation available.
AL078638 Genomic DNA. Translation: CAI41063.2.
AL078638 Genomic DNA. Translation: CAI41064.2.
AL078638 Genomic DNA. Translation: CAM21578.1. Sequence problems.
CH471150 Genomic DNA. Translation: EAW88475.1.
BC040518 mRNA. Translation: AAH40518.1.
BC064350 mRNA. Translation: AAH64350.1. Sequence problems.
CCDSiCCDS44004.1. [Q8IWC1-1]
CCDS55508.1. [Q8IWC1-3]
CCDS55509.1. [Q8IWC1-4]
RefSeqiNP_001166987.1. NM_001173516.1. [Q8IWC1-4]
NP_001166988.1. NM_001173517.1. [Q8IWC1-3]
NP_078873.2. NM_024597.3. [Q8IWC1-1]
UniGeneiHs.446275.

3D structure databases

ProteinModelPortaliQ8IWC1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122777. 8 interactions.
IntActiQ8IWC1. 1 interaction.
MINTiMINT-4990235.
STRINGi9606.ENSP00000318086.

PTM databases

PhosphoSiteiQ8IWC1.

Polymorphism databases

DMDMi158705880.

Proteomic databases

MaxQBiQ8IWC1.
PaxDbiQ8IWC1.
PRIDEiQ8IWC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316077; ENSP00000318086; ENSG00000129680. [Q8IWC1-1]
ENST00000370661; ENSP00000359695; ENSG00000129680. [Q8IWC1-3]
ENST00000370663; ENSP00000359697; ENSG00000129680. [Q8IWC1-4]
GeneIDi79649.
KEGGihsa:79649.
UCSCiuc004ezs.3. human. [Q8IWC1-3]
uc004ezt.3. human. [Q8IWC1-1]
uc010nsa.2. human. [Q8IWC1-2]

Organism-specific databases

CTDi79649.
GeneCardsiGC0XM135295.
H-InvDBHIX0017079.
HGNCiHGNC:25742. MAP7D3.
HPAiHPA035598.
MIMi300930. gene.
neXtProtiNX_Q8IWC1.
PharmGKBiPA162394972.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG113680.
GeneTreeiENSGT00660000095160.
HOVERGENiHBG103577.
InParanoidiQ8IWC1.
KOiK16807.
OMAiQQDANKE.
OrthoDBiEOG761BTS.
PhylomeDBiQ8IWC1.
TreeFamiTF332273.

Miscellaneous databases

ChiTaRSiMAP7D3. human.
GenomeRNAii79649.
NextBioi68800.
PROiQ8IWC1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWC1.
CleanExiHS_MAP7D3.
GenevestigatoriQ8IWC1.

Family and domain databases

InterProiIPR008604. MAP7.
[Graphical view]
PANTHERiPTHR15073. PTHR15073. 1 hit.
PfamiPF05672. MAP7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 701-876 (ISOFORMS 1/2/3).
    Tissue: Synovium and Teratocarcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Cervix.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ALA-502 AND ARG-628.
    Tissue: Brain and Prostate.
  6. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-457; SER-461 AND SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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.
  10. "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-770, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Mdp3 is a novel microtubule-binding protein that regulates microtubule assembly and stability."
    Sun X., Shi X., Liu M., Li D., Zhang L., Liu X., Zhou J.
    Cell Cycle 10:3929-3937(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MICROTUBULES AND TUBULIN, INDUCTION, SUBCELLULAR LOCATION.
  15. "C-terminal region of MAP7 domain containing protein 3 (MAP7D3) promotes microtubule polymerization by binding at the C-terminal tail of tubulin."
    Yadav S., Verma P.J., Panda D.
    PLoS ONE 9:E99539-E99539(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROTUBULES AND TUBULIN, FUNCTION.

Entry informationi

Entry nameiMA7D3_HUMAN
AccessioniPrimary (citable) accession number: Q8IWC1
Secondary accession number(s): A2A2J0
, A6NCZ7, A6NHR4, B4DWD2, H7BY77, Q5JXI5, Q5JXI6, Q6P2S1, Q9H9M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: February 4, 2015
This is version 90 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

Dasty 3

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 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.