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Protein

Ensconsin

Gene

MAP7

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

Functioni

Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments.3 Publications

GO - Molecular functioni

  • receptor binding Source: BHF-UCL
  • structural molecule activity Source: ProtInc

GO - Biological processi

  • establishment or maintenance of cell polarity Source: ProtInc
  • microtubule cytoskeleton organization Source: ProtInc
  • protein localization to plasma membrane Source: BHF-UCL
  • response to osmotic stress Source: BHF-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ensconsin
Alternative name(s):
Epithelial microtubule-associated protein of 115 kDa
Short name:
E-MAP-115
Microtubule-associated protein 7
Short name:
MAP-7
Gene namesi
Name:MAP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6869. MAP7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30615.

Polymorphism and mutation databases

BioMutaiMAP7.
DMDMi74739817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 749748EnsconsinPRO_0000255949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei183 – 1831PhosphoserineCombined sources
Modified residuei202 – 2021PhosphoserineBy similarity
Modified residuei209 – 2091PhosphoserineCombined sources
Modified residuei219 – 2191PhosphoserineCombined sources
Modified residuei231 – 2311PhosphothreonineCombined sources
Modified residuei235 – 2351PhosphoserineCombined sources
Modified residuei254 – 2541PhosphoserineCombined sources
Modified residuei277 – 2771PhosphothreonineCombined sources
Modified residuei365 – 3651PhosphoserineCombined sources
Cross-linki406 – 406Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei673 – 6731PhosphothreonineCombined sources

Post-translational modificationi

The association with microtubules is regulated by phosphorylation during the cell cycle. During interphase only phosphorylated on serine. Phosphorylated on threonine in mitosis.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14244.
MaxQBiQ14244.
PaxDbiQ14244.
PRIDEiQ14244.

PTM databases

iPTMnetiQ14244.
PhosphoSiteiQ14244.

Expressioni

Tissue specificityi

Expressed in the skin and cells of epithelial origin. Predominantly expressed in the suprabasal layers of the normal epidermis and relatively abundant in squamous cell carcinomas but barely detectable in basal cell carcinomas.2 Publications

Inductioni

Up-regulated upon terminal differentiation of primary keratinocytes.

Gene expression databases

BgeeiQ14244.
CleanExiHS_MAP7.
ExpressionAtlasiQ14244. baseline and differential.
GenevisibleiQ14244. HS.

Organism-specific databases

HPAiHPA029712.
HPA029713.

Interactioni

Subunit structurei

Interacts with TRPV4.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114515. 37 interactions.
IntActiQ14244. 16 interactions.
MINTiMINT-4532905.
STRINGi9606.ENSP00000414712.

Structurei

3D structure databases

ProteinModelPortaliQ14244.
SMRiQ14244. Positions 477-631.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili89 – 15264Sequence analysisAdd
BLAST
Coiled coili477 – 612136Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi316 – 451136Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the MAP7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIRT. Eukaryota.
ENOG410XS5W. LUCA.
GeneTreeiENSGT00660000095160.
HOGENOMiHOG000231569.
HOVERGENiHBG081952.
InParanoidiQ14244.
KOiK10433.
OrthoDBiEOG77DJ5Q.
PhylomeDBiQ14244.
TreeFamiTF332273.

Family and domain databases

InterProiIPR030707. MAP7.
IPR008604. MAP7_fam.
[Graphical view]
PANTHERiPTHR15073. PTHR15073. 1 hit.
PTHR15073:SF4. PTHR15073:SF4. 1 hit.
PfamiPF05672. MAP7. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14244-1) [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
MAELGAGGDG HRGGDGAVRS ETAPDSYKVQ DKKNASSRPA SAISGQNNNH
60 70 80 90 100
SGNKPDPPPV LRVDDRQRLA RERREEREKQ LAAREIVWLE REERARQHYE
110 120 130 140 150
KHLEERKKRL EEQRQKEERR RAAVEEKRRQ RLEEDKERHE AVVRRTMERS
160 170 180 190 200
QKPKQKHNRW SWGGSLHGSP SIHSADPDRR SVSTMNLSKY VDPVISKRLS
210 220 230 240 250
SSSATLLNSP DRARRLQLSP WESSVVNRLL TPTHSFLARS KSTAALSGEA
260 270 280 290 300
ASCSPIIMPY KAAHSRNSMD RPKLFVTPPE GSSRRRIIHG TASYKKERER
310 320 330 340 350
ENVLFLTSGT RRAVSPSNPK ARQPARSRLW LPSKSLPHLP GTPRPTSSLP
360 370 380 390 400
PGSVKAAPAQ VRPPSPGNIR PVKREVKVEP EKKDPEKEPQ KVANEPSLKG
410 420 430 440 450
RAPLVKVEEA TVEERTPAEP EVGPAAPAMA PAPASAPAPA SAPAPAPVPT
460 470 480 490 500
PAMVSAPSST VNASASVKTS AGTTDPEEAT RLLAEKRRLA REQREKEERE
510 520 530 540 550
RREQEELERQ KREELAQRVA EERTTRREEE SRRLEAEQAR EKEEQLQRQA
560 570 580 590 600
EERALREREE AERAQRQKEE EARVREEAER VRQEREKHFQ REEQERLERK
610 620 630 640 650
KRLEEIMKRT RRTEATDKKT SDQRNGDIAK GALTGGTEVS ALPCTTNAPG
660 670 680 690 700
NGKPVGSPHV VTSHQSKVTV ESTPDLEKQP NENGVSVQNE NFEEIINLPI
710 720 730 740
GSKPSRLDVT NSESPEIPLN PILAFDDEGT LGPLPQVDGV QTQQTAEVI
Length:749
Mass (Da):84,052
Last modified:November 1, 1996 - v1
Checksum:iCB69BDE25C9540E3
GO
Isoform 2 (identifier: Q14244-2) [UniParc]FASTAAdd to basket

Also known as: E-MAP-115-105

The sequence of this isoform differs from the canonical sequence as follows:
     176-212: Missing.

Show »
Length:712
Mass (Da):79,976
Checksum:iECAA14610C717550
GO
Isoform 3 (identifier: Q14244-3) [UniParc]FASTAAdd to basket

Also known as: E-MAP-115-95

The sequence of this isoform differs from the canonical sequence as follows:
     82-175: Missing.

Show »
Length:655
Mass (Da):72,414
Checksum:i5DB5677DDD254C2E
GO
Isoform 4 (identifier: Q14244-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MAELGAGGDGHRGGDGAVRSET → MPGSATALRHERLKKTNARPIPLGLFTINEEDEQQKNGNSRRPK
     176-212: Missing.

Note: No experimental confirmation available.
Show »
Length:734
Mass (Da):82,877
Checksum:iECC44D5E7D550F48
GO
Isoform 5 (identifier: Q14244-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.

Note: No experimental confirmation available.
Show »
Length:603
Mass (Da):66,938
Checksum:i276DC81A68500D90
GO
Isoform 6 (identifier: Q14244-6) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:734
Mass (Da):82,867
Checksum:i442B7844C6097C72
GO
Isoform 7 (identifier: Q14244-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MAELGAGGDGHRGGDGAVRSET → MPGSATALRHERLKKTNARPIPLGLFTINEEDEQQKNGNSRRPK

Note: No experimental confirmation available.
Show »
Length:771
Mass (Da):86,952
Checksum:iF91E6CBDDD0DB6D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti318 – 3181N → D in BAH13013 (PubMed:14702039).Curated
Sequence conflicti583 – 5831Q → R in BAH12386 (PubMed:14702039).Curated
Sequence conflicti725 – 7251F → S in BAH13013 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti361 – 3611V → I.
Corresponds to variant rs35350783 [ dbSNP | Ensembl ].
VAR_034091
Natural varianti526 – 5261R → P.
Corresponds to variant rs35107962 [ dbSNP | Ensembl ].
VAR_034092
Natural varianti558 – 5581R → W.2 Publications
Corresponds to variant rs2076190 [ dbSNP | Ensembl ].
VAR_028880

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 146146Missing in isoform 5. 1 PublicationVSP_043335Add
BLAST
Alternative sequencei1 – 2323MAELG…RSETA → MEDTKLYS in isoform 6. 1 PublicationVSP_046758Add
BLAST
Alternative sequencei1 – 2222MAELG…VRSET → MPGSATALRHERLKKTNARP IPLGLFTINEEDEQQKNGNS RRPK in isoform 4 and isoform 7. 1 PublicationVSP_043336Add
BLAST
Alternative sequencei82 – 17594Missing in isoform 3. 1 PublicationVSP_021316Add
BLAST
Alternative sequencei176 – 21237Missing in isoform 2 and isoform 4. 2 PublicationsVSP_021317Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73882 mRNA. Translation: CAA52086.1.
AJ242501 mRNA. Translation: CAB88030.1.
AJ242502 mRNA. Translation: CAB88031.1.
AK294461 mRNA. Translation: BAH11776.1.
AK296556 mRNA. Translation: BAH12386.1.
AK299355 mRNA. Translation: BAH13013.1.
AK316062 mRNA. Translation: BAH14433.1.
AL024508, AL023284 Genomic DNA. Translation: CAD92557.2.
AL023284, AL024508 Genomic DNA. Translation: CAI20475.1.
AL133511 Genomic DNA. No translation available.
BC025777 mRNA. Translation: AAH25777.1.
CCDSiCCDS5178.1. [Q14244-1]
CCDS56452.1. [Q14244-5]
CCDS56453.1. [Q14244-6]
CCDS56454.1. [Q14244-4]
CCDS56455.1. [Q14244-7]
CCDS75528.1. [Q14244-3]
CCDS75529.1. [Q14244-2]
PIRiI37356.
RefSeqiNP_001185537.1. NM_001198608.1. [Q14244-7]
NP_001185538.1. NM_001198609.1.
NP_001185540.1. NM_001198611.1. [Q14244-4]
NP_001185543.1. NM_001198614.1. [Q14244-7]
NP_001185544.1. NM_001198615.1. [Q14244-6]
NP_001185545.1. NM_001198616.1. [Q14244-2]
NP_001185546.1. NM_001198617.1. [Q14244-3]
NP_001185547.1. NM_001198618.1. [Q14244-5]
NP_001185548.1. NM_001198619.1. [Q14244-5]
NP_003971.1. NM_003980.4. [Q14244-1]
XP_006715663.1. XM_006715600.1. [Q14244-7]
UniGeneiHs.486548.

Genome annotation databases

EnsembliENST00000354570; ENSP00000346581; ENSG00000135525. [Q14244-1]
ENST00000432797; ENSP00000414879; ENSG00000135525. [Q14244-5]
ENST00000438100; ENSP00000400790; ENSG00000135525. [Q14244-4]
ENST00000454590; ENSP00000414712; ENSG00000135525. [Q14244-7]
ENST00000544465; ENSP00000445737; ENSG00000135525. [Q14244-6]
ENST00000611373; ENSP00000482998; ENSG00000135525. [Q14244-5]
ENST00000616617; ENSP00000483511; ENSG00000135525. [Q14244-3]
ENST00000618822; ENSP00000482356; ENSG00000135525. [Q14244-2]
GeneIDi9053.
KEGGihsa:9053.
UCSCiuc003qgz.4. human. [Q14244-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73882 mRNA. Translation: CAA52086.1.
AJ242501 mRNA. Translation: CAB88030.1.
AJ242502 mRNA. Translation: CAB88031.1.
AK294461 mRNA. Translation: BAH11776.1.
AK296556 mRNA. Translation: BAH12386.1.
AK299355 mRNA. Translation: BAH13013.1.
AK316062 mRNA. Translation: BAH14433.1.
AL024508, AL023284 Genomic DNA. Translation: CAD92557.2.
AL023284, AL024508 Genomic DNA. Translation: CAI20475.1.
AL133511 Genomic DNA. No translation available.
BC025777 mRNA. Translation: AAH25777.1.
CCDSiCCDS5178.1. [Q14244-1]
CCDS56452.1. [Q14244-5]
CCDS56453.1. [Q14244-6]
CCDS56454.1. [Q14244-4]
CCDS56455.1. [Q14244-7]
CCDS75528.1. [Q14244-3]
CCDS75529.1. [Q14244-2]
PIRiI37356.
RefSeqiNP_001185537.1. NM_001198608.1. [Q14244-7]
NP_001185538.1. NM_001198609.1.
NP_001185540.1. NM_001198611.1. [Q14244-4]
NP_001185543.1. NM_001198614.1. [Q14244-7]
NP_001185544.1. NM_001198615.1. [Q14244-6]
NP_001185545.1. NM_001198616.1. [Q14244-2]
NP_001185546.1. NM_001198617.1. [Q14244-3]
NP_001185547.1. NM_001198618.1. [Q14244-5]
NP_001185548.1. NM_001198619.1. [Q14244-5]
NP_003971.1. NM_003980.4. [Q14244-1]
XP_006715663.1. XM_006715600.1. [Q14244-7]
UniGeneiHs.486548.

3D structure databases

ProteinModelPortaliQ14244.
SMRiQ14244. Positions 477-631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114515. 37 interactions.
IntActiQ14244. 16 interactions.
MINTiMINT-4532905.
STRINGi9606.ENSP00000414712.

PTM databases

iPTMnetiQ14244.
PhosphoSiteiQ14244.

Polymorphism and mutation databases

BioMutaiMAP7.
DMDMi74739817.

Proteomic databases

EPDiQ14244.
MaxQBiQ14244.
PaxDbiQ14244.
PRIDEiQ14244.

Protocols and materials databases

DNASUi9053.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354570; ENSP00000346581; ENSG00000135525. [Q14244-1]
ENST00000432797; ENSP00000414879; ENSG00000135525. [Q14244-5]
ENST00000438100; ENSP00000400790; ENSG00000135525. [Q14244-4]
ENST00000454590; ENSP00000414712; ENSG00000135525. [Q14244-7]
ENST00000544465; ENSP00000445737; ENSG00000135525. [Q14244-6]
ENST00000611373; ENSP00000482998; ENSG00000135525. [Q14244-5]
ENST00000616617; ENSP00000483511; ENSG00000135525. [Q14244-3]
ENST00000618822; ENSP00000482356; ENSG00000135525. [Q14244-2]
GeneIDi9053.
KEGGihsa:9053.
UCSCiuc003qgz.4. human. [Q14244-1]

Organism-specific databases

CTDi9053.
GeneCardsiMAP7.
HGNCiHGNC:6869. MAP7.
HPAiHPA029712.
HPA029713.
MIMi604108. gene.
neXtProtiNX_Q14244.
PharmGKBiPA30615.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIRT. Eukaryota.
ENOG410XS5W. LUCA.
GeneTreeiENSGT00660000095160.
HOGENOMiHOG000231569.
HOVERGENiHBG081952.
InParanoidiQ14244.
KOiK10433.
OrthoDBiEOG77DJ5Q.
PhylomeDBiQ14244.
TreeFamiTF332273.

Miscellaneous databases

ChiTaRSiMAP7. human.
GeneWikiiMAP7.
GenomeRNAii9053.
NextBioi33919.
PROiQ14244.
SOURCEiSearch...

Gene expression databases

BgeeiQ14244.
CleanExiHS_MAP7.
ExpressionAtlasiQ14244. baseline and differential.
GenevisibleiQ14244. HS.

Family and domain databases

InterProiIPR030707. MAP7.
IPR008604. MAP7_fam.
[Graphical view]
PANTHERiPTHR15073. PTHR15073. 1 hit.
PTHR15073:SF4. PTHR15073:SF4. 1 hit.
PfamiPF05672. MAP7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and molecular characterization of E-MAP-115, a novel microtubule-associated protein predominantly expressed in epithelial cells."
    Masson D., Kreis T.E.
    J. Cell Biol. 123:357-371(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. "Novel features of E-MAP-115 revealed by the characterization of its variants E-MAP-115/105 and E-MAP-115/95."
    Fabre-Jonca N., Masson D.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
  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 4; 5; 6 AND 7), VARIANT TRP-558.
    Tissue: Amygdala, Hippocampus and Thalamus.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1), VARIANT TRP-558.
    Tissue: Pancreas.
  6. "Binding of E-MAP-115 to microtubules is regulated by cell cycle-dependent phosphorylation."
    Masson D., Kreis T.E.
    J. Cell Biol. 131:1015-1024(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  7. "Upregulation and redistribution of E-MAP-115 (epithelial microtubule-associated protein of 115 kDa) in terminally differentiating keratinocytes is coincident with the formation of intercellular contacts."
    Fabre-Jonca N., Viard I., French L.E., Masson D.
    J. Invest. Dermatol. 112:216-225(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Rapid dynamics of the microtubule binding of ensconsin in vivo."
    Bulinski J.C., Odde D.J., Howell B.J., Salmon T.D., Waterman-Storer C.M.
    J. Cell Sci. 114:3885-3897(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-219; SER-254 AND THR-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-209 AND SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-219; THR-231; SER-254 AND THR-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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 ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-209; SER-219; THR-277 AND THR-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP7_HUMAN
AccessioniPrimary (citable) accession number: Q14244
Secondary accession number(s): B7Z290
, B7Z400, B7Z5S7, B7Z9U7, C9JPS0, E9PCP3, F5H1E2, Q7Z6S0, Q8TAU5, Q9NY82, Q9NY83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 130 of the entry and version 1 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 6
    Human chromosome 6: 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

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.