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Protein

Microtubule-associated protein RP/EB family member 2

Gene

MAPRE2

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

Functioni

May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).By similarity

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • mitotic nuclear division Source: UniProtKB-KW
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein RP/EB family member 2
Alternative name(s):
APC-binding protein EB2
End-binding protein 2
Short name:
EB2
Gene namesi
Name:MAPRE2
Synonyms:RP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:6891. MAPRE2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • microtubule cytoskeleton Source: LIFEdb
  • microtubule plus-end Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30635.

Protein family/group databases

Allergomei8363. Hom s RP1.

Polymorphism and mutation databases

BioMutaiMAPRE2.
DMDMi60390165.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Microtubule-associated protein RP/EB family member 2PRO_0000213424Add
BLAST
Isoform 5 (identifier: Q15555-5)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei167 – 1671PhosphotyrosineCombined sources
Modified residuei219 – 2191PhosphoserineCombined sources
Isoform 5 (identifier: Q15555-5)
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15555.
MaxQBiQ15555.
PaxDbiQ15555.
PeptideAtlasiQ15555.
PRIDEiQ15555.

2D gel databases

OGPiQ15555.

PTM databases

iPTMnetiQ15555.
PhosphoSiteiQ15555.

Expressioni

Tissue specificityi

Expressed in different tumor cell lines. Up-regulated in activated B- and T-lymphocytes.1 Publication

Gene expression databases

BgeeiQ15555.
CleanExiHS_MAPRE2.
HS_RP1.
ExpressionAtlasiQ15555. baseline and differential.
GenevisibleiQ15555. HS.

Organism-specific databases

HPAiHPA016738.
HPA016739.

Interactioni

Subunit structurei

Interacts with DCTN1. Binds to the C-terminal domain of APC. Binds monomeric and polymerized tubulin.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRTAC1Q9NQ793EBI-739717,EBI-10205543
LMO2P257914EBI-739717,EBI-739696
MAPRE1Q156913EBI-739717,EBI-1004115
PAXIP1Q6ZW49-23EBI-739717,EBI-10236271
TRAF1Q130773EBI-739717,EBI-359224
TRAIPQ9BWF23EBI-739717,EBI-1756205
TXN2Q997573EBI-739717,EBI-2932492

Protein-protein interaction databases

BioGridi116178. 34 interactions.
IntActiQ15555. 18 interactions.
MINTiMINT-1458854.
STRINGi9606.ENSP00000300249.

Structurei

3D structure databases

ProteinModelPortaliQ15555.
SMRiQ15555. Positions 44-173, 263-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 159103CHPROSITE-ProRule annotationAdd
BLAST
Domaini236 – 30671EB1 C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 327141DCTN1-bindingAdd
BLAST
Regioni259 – 30244APC-bindingAdd
BLAST

Domaini

Composed of two functionally independent domains. The N-terminal domain forms a hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1.

Sequence similaritiesi

Belongs to the MAPRE family.Curated
Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 EB1 C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3000. Eukaryota.
COG5217. LUCA.
GeneTreeiENSGT00490000043329.
HOGENOMiHOG000198048.
HOVERGENiHBG052410.
InParanoidiQ15555.
KOiK10436.
OMAiHESHTEE.
PhylomeDBiQ15555.
TreeFamiTF313620.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027328. MAPRE.
IPR027735. RP1/EB2_vertebrate.
[Graphical view]
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF7. PTHR10623:SF7. 1 hit.
PfamiPF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
[Graphical view]
SUPFAMiSSF140612. SSF140612. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS51230. EB1_C. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15555-1) [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
MPGPTQTLSP NGENNNDIIQ DNNGTIIPFR KHTVRGERSY SWGMAVNVYS
60 70 80 90 100
TSITQETMSR HDIIAWVNDI VSLNYTKVEQ LCSGAAYCQF MDMLFPGCIS
110 120 130 140 150
LKKVKFQAKL EHEYIHNFKL LQASFKRMNV DKVIPVEKLV KGRFQDNLDF
160 170 180 190 200
IQWFKKFYDA NYDGKEYDPV EARQGQDAIP PPDPGEQIFN LPKKSHHANS
210 220 230 240 250
PTAGAAKSSP AAKPGSTPSR PSSAKRASSS GSASKSDKDL ETQVIQLNEQ
260 270 280 290 300
VHSLKLALEG VEKERDFYFG KLREIELLCQ EHGQENDDLV QRLMDILYAS
310 320
EEHEGHTEEP EAEEQAHEQQ PPQQEEY
Length:327
Mass (Da):37,031
Last modified:November 1, 1996 - v1
Checksum:i2BE99E9F9EFA83C3
GO
Isoform 2 (identifier: Q15555-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     252-259: HSLKLALE → MHQLWPRL
     260-327: Missing.

Show »
Length:259
Mass (Da):29,091
Checksum:i37088FEA106B1EA1
GO
Isoform 3 (identifier: Q15555-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSY → MKQNRDQKCPVSQRNSSFQQPGRKPGCS

Note: No experimental confirmation available.
Show »
Length:315
Mass (Da):35,741
Checksum:i7E948A0018C5C8D1
GO
Isoform 5 (identifier: Q15555-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:284
Mass (Da):32,236
Checksum:i028548689D6B82D0
GO
Isoform 4 (identifier: Q15555-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: MPGPTQTLSP...NYTKVEQLCS → MARTTTTSSRIITGPSFLSGSTQCAGSVPT

Note: No experimental confirmation available.
Show »
Length:274
Mass (Da):30,691
Checksum:i793DB6E775EBF28B
GO

Sequence cautioni

The sequence BAA83375.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651A → G in BAA83375 (PubMed:15489334).Curated
Sequence conflicti100 – 1001S → N in BAG58966 (PubMed:14702039).Curated
Sequence conflicti128 – 1281M → K in BAG58966 (PubMed:14702039).Curated
Sequence conflicti209 – 2091S → G in BAG52251 (PubMed:14702039).Curated
Sequence conflicti235 – 2351K → I in BAH11899 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti162 – 1621Y → C.
Corresponds to variant rs11538993 [ dbSNP | Ensembl ].
VAR_050018

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8383MPGPT…EQLCS → MARTTTTSSRIITGPSFLSG STQCAGSVPT in isoform 4. 1 PublicationVSP_046041Add
BLAST
Alternative sequencei1 – 4343Missing in isoform 5. 1 PublicationVSP_055671Add
BLAST
Alternative sequencei1 – 4040MPGPT…GERSY → MKQNRDQKCPVSQRNSSFQQ PGRKPGCS in isoform 3. 1 PublicationVSP_045710Add
BLAST
Alternative sequencei252 – 2598HSLKLALE → MHQLWPRL in isoform 2. 1 PublicationVSP_012944
Alternative sequencei260 – 32768Missing in isoform 2. 1 PublicationVSP_012945Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94232 mRNA. Translation: CAA63923.1.
AB016823 mRNA. Translation: BAA83375.1. Different initiation.
CR536545 mRNA. Translation: CAG38782.1.
BT020086 mRNA. Translation: AAV38889.1.
AK090945 mRNA. Translation: BAG52251.1.
AK296251 mRNA. Translation: BAG58966.1.
AK294833 mRNA. Translation: BAH11899.1.
AK315766 mRNA. Translation: BAG38118.1.
AC009277 Genomic DNA. No translation available.
AC015967 Genomic DNA. No translation available.
CH471088 Genomic DNA. Translation: EAX01336.1.
CH471088 Genomic DNA. Translation: EAX01338.1.
BC007318 mRNA. Translation: AAH07318.1.
CCDSiCCDS11910.1. [Q15555-1]
CCDS45850.1. [Q15555-3]
CCDS45851.1. [Q15555-5]
CCDS58619.1. [Q15555-4]
PIRiG01037.
RefSeqiNP_001137298.1. NM_001143826.2. [Q15555-5]
NP_001137299.1. NM_001143827.2. [Q15555-3]
NP_001243349.1. NM_001256420.1. [Q15555-4]
NP_055083.1. NM_014268.3. [Q15555-1]
XP_011524097.1. XM_011525795.1. [Q15555-5]
UniGeneiHs.532824.

Genome annotation databases

EnsembliENST00000300249; ENSP00000300249; ENSG00000166974. [Q15555-1]
ENST00000413393; ENSP00000396074; ENSG00000166974. [Q15555-5]
ENST00000436190; ENSP00000407723; ENSG00000166974. [Q15555-3]
ENST00000538170; ENSP00000446343; ENSG00000166974. [Q15555-4]
ENST00000588910; ENSP00000468588; ENSG00000166974. [Q15555-2]
ENST00000589699; ENSP00000464921; ENSG00000166974. [Q15555-5]
GeneIDi10982.
KEGGihsa:10982.
UCSCiuc002kyf.3. human. [Q15555-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94232 mRNA. Translation: CAA63923.1.
AB016823 mRNA. Translation: BAA83375.1. Different initiation.
CR536545 mRNA. Translation: CAG38782.1.
BT020086 mRNA. Translation: AAV38889.1.
AK090945 mRNA. Translation: BAG52251.1.
AK296251 mRNA. Translation: BAG58966.1.
AK294833 mRNA. Translation: BAH11899.1.
AK315766 mRNA. Translation: BAG38118.1.
AC009277 Genomic DNA. No translation available.
AC015967 Genomic DNA. No translation available.
CH471088 Genomic DNA. Translation: EAX01336.1.
CH471088 Genomic DNA. Translation: EAX01338.1.
BC007318 mRNA. Translation: AAH07318.1.
CCDSiCCDS11910.1. [Q15555-1]
CCDS45850.1. [Q15555-3]
CCDS45851.1. [Q15555-5]
CCDS58619.1. [Q15555-4]
PIRiG01037.
RefSeqiNP_001137298.1. NM_001143826.2. [Q15555-5]
NP_001137299.1. NM_001143827.2. [Q15555-3]
NP_001243349.1. NM_001256420.1. [Q15555-4]
NP_055083.1. NM_014268.3. [Q15555-1]
XP_011524097.1. XM_011525795.1. [Q15555-5]
UniGeneiHs.532824.

3D structure databases

ProteinModelPortaliQ15555.
SMRiQ15555. Positions 44-173, 263-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116178. 34 interactions.
IntActiQ15555. 18 interactions.
MINTiMINT-1458854.
STRINGi9606.ENSP00000300249.

Protein family/group databases

Allergomei8363. Hom s RP1.

PTM databases

iPTMnetiQ15555.
PhosphoSiteiQ15555.

Polymorphism and mutation databases

BioMutaiMAPRE2.
DMDMi60390165.

2D gel databases

OGPiQ15555.

Proteomic databases

EPDiQ15555.
MaxQBiQ15555.
PaxDbiQ15555.
PeptideAtlasiQ15555.
PRIDEiQ15555.

Protocols and materials databases

DNASUi10982.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300249; ENSP00000300249; ENSG00000166974. [Q15555-1]
ENST00000413393; ENSP00000396074; ENSG00000166974. [Q15555-5]
ENST00000436190; ENSP00000407723; ENSG00000166974. [Q15555-3]
ENST00000538170; ENSP00000446343; ENSG00000166974. [Q15555-4]
ENST00000588910; ENSP00000468588; ENSG00000166974. [Q15555-2]
ENST00000589699; ENSP00000464921; ENSG00000166974. [Q15555-5]
GeneIDi10982.
KEGGihsa:10982.
UCSCiuc002kyf.3. human. [Q15555-1]

Organism-specific databases

CTDi10982.
GeneCardsiMAPRE2.
HGNCiHGNC:6891. MAPRE2.
HPAiHPA016738.
HPA016739.
MIMi605789. gene.
neXtProtiNX_Q15555.
PharmGKBiPA30635.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3000. Eukaryota.
COG5217. LUCA.
GeneTreeiENSGT00490000043329.
HOGENOMiHOG000198048.
HOVERGENiHBG052410.
InParanoidiQ15555.
KOiK10436.
OMAiHESHTEE.
PhylomeDBiQ15555.
TreeFamiTF313620.

Miscellaneous databases

ChiTaRSiMAPRE2. human.
GeneWikiiMAPRE2.
GenomeRNAii10982.
PROiQ15555.
SOURCEiSearch...

Gene expression databases

BgeeiQ15555.
CleanExiHS_MAPRE2.
HS_RP1.
ExpressionAtlasiQ15555. baseline and differential.
GenevisibleiQ15555. HS.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027328. MAPRE.
IPR027735. RP1/EB2_vertebrate.
[Graphical view]
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF7. PTHR10623:SF7. 1 hit.
PfamiPF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
[Graphical view]
SUPFAMiSSF140612. SSF140612. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS51230. EB1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene family, is differentially expressed in activated T cells."
    Renner C., Pfitzenmeier J.-P., Gerlach K., Held G., Ohnesorge S., Sahin U., Bauer S., Pfreundschuh M.
    J. Immunol. 159:1276-1283(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY, INTERACTION WITH APC.
  2. "RP1, a member of the APC-binding EB1 family, alternative form."
    Oishi N.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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; 3; 4 AND 5).
    Tissue: Amygdala, Brain and Trachea.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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).
    Tissue: Lymph.
  9. Cited for: INTERACTION WITH TUBULIN, SUBCELLULAR LOCATION.
  10. "Characterization of functional domains of human EB1 family proteins."
    Bu W., Su L.-K.
    J. Biol. Chem. 278:49721-49731(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH TUBULIN; APC AND DCTN1.
  11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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].
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 5), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMARE2_HUMAN
AccessioniPrimary (citable) accession number: Q15555
Secondary accession number(s): B2RE21
, B3KR39, B4DJV4, B7Z2L3, E9PHR3, F5H1V8, G5E9I6, Q9UQ33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 144 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 18
    Human chromosome 18: 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.