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Q5VYK3

- ECM29_HUMAN

UniProt

Q5VYK3 - ECM29_HUMAN

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Protein
Proteasome-associated protein ECM29 homolog
Gene
ECM29, KIAA0368
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Adapter/scaffolding protein that binds to the 26S proteasome, motor proteins and other compartment specific proteins. May couple the proteasome to different compartments including endosome, endoplasmic reticulum and centrosome. May play a role in ERAD and other enhanced proteolyis.2 Publications

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome-associated protein ECM29 homolog
Short name:
Ecm29
Gene namesi
Name:ECM29
Synonyms:KIAA0368
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:29020. KIAA0368.

Subcellular locationi

Endoplasmic reticulum. Endoplasmic reticulum-Golgi intermediate compartment. Endosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus. Endosomemultivesicular body. Cytoplasmic vesicle 2 Publications

GO - Cellular componenti

  1. ER to Golgi transport vesicle Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytoplasmic membrane-bounded vesicle Source: UniProtKB
  4. early endosome Source: UniProtKB
  5. endocytic vesicle Source: UniProtKB
  6. endoplasmic reticulum Source: UniProtKB
  7. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  8. late endosome Source: UniProtKB
  9. multivesicular body Source: UniProtKB
  10. nucleus Source: UniProtKB
  11. proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endoplasmic reticulum, Endosome, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 18451844Proteasome-associated protein ECM29 homolog
PRO_0000212559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei830 – 8301Phosphoserine1 Publication
Modified residuei836 – 8361Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5VYK3.
PaxDbiQ5VYK3.
PRIDEiQ5VYK3.

PTM databases

PhosphoSiteiQ5VYK3.

Expressioni

Gene expression databases

ArrayExpressiQ5VYK3.
BgeeiQ5VYK3.
CleanExiHS_KIAA0368.
GenevestigatoriQ5VYK3.

Organism-specific databases

HPAiHPA021646.

Interactioni

Subunit structurei

Non-stoichiometric component of the proteasome; associates with the 26S proteasome. Interacts (via N-terminus) with VPS11, VPS26A, VPS36, RAB11FIP4 and RABEP1. Interacts (via C-terminus) with DCTN1, DCTN2, KIF5B, MYH7, MYH10, MYO10 and ARF6.2 Publications

Protein-protein interaction databases

IntActiQ5VYK3. 8 interactions.
MINTiMINT-1146313.
STRINGi9606.ENSP00000259335.

Structurei

3D structure databases

ProteinModelPortaliQ5VYK3.
SMRiQ5VYK3. Positions 396-467, 1165-1304, 1376-1440.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati34 – 7138HEAT 1
Add
BLAST
Repeati113 – 15038HEAT 2
Add
BLAST
Repeati168 – 21144HEAT 3
Add
BLAST
Repeati332 – 36837HEAT 4
Add
BLAST
Repeati393 – 43240HEAT 5
Add
BLAST
Repeati435 – 47238HEAT 6
Add
BLAST
Repeati475 – 51339HEAT 7
Add
BLAST
Repeati689 – 72638HEAT 8
Add
BLAST
Repeati727 – 76539HEAT 9
Add
BLAST
Repeati789 – 82638HEAT 10
Add
BLAST
Repeati835 – 87440HEAT 11
Add
BLAST
Repeati876 – 91338HEAT 12
Add
BLAST
Repeati937 – 97539HEAT 13
Add
BLAST
Repeati981 – 101838HEAT 14
Add
BLAST
Repeati1019 – 105638HEAT 15
Add
BLAST
Repeati1118 – 115538HEAT 16
Add
BLAST
Repeati1158 – 119538HEAT 17
Add
BLAST
Repeati1200 – 123738HEAT 18
Add
BLAST
Repeati1249 – 128739HEAT 19
Add
BLAST
Repeati1291 – 132939HEAT 20
Add
BLAST
Repeati1354 – 139239HEAT 21
Add
BLAST
Repeati1396 – 143338HEAT 22
Add
BLAST
Repeati1523 – 156038HEAT 23
Add
BLAST
Repeati1564 – 160138HEAT 24
Add
BLAST
Repeati1611 – 164838HEAT 25
Add
BLAST
Repeati1652 – 168938HEAT 26
Add
BLAST
Repeati1785 – 182844HEAT 27
Add
BLAST

Sequence similaritiesi

Contains 27 HEAT repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG250280.
HOGENOMiHOG000231642.
HOVERGENiHBG051438.
InParanoidiQ5VYK3.
KOiK11886.
OrthoDBiEOG79SDW5.
PhylomeDBiQ5VYK3.

Family and domain databases

Gene3Di1.25.10.10. 6 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026827. ECM29/GCN1.
IPR024372. Proteasome_stabil_ECM29.
[Graphical view]
PANTHERiPTHR23346. PTHR23346. 1 hit.
PTHR23346:SF19. PTHR23346:SF19. 1 hit.
PfamiPF13001. Ecm29. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 7 hits.

Sequencei

Sequence statusi: Complete.

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

Q5VYK3-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAAASASQ DELNQLERVF LRLGHAETDE QLQNIISKFL PPVLLKLSST     50
QEGVRKKVME LLVHLNKRIK SRPKIQLPVE TLLVQYQDPA AVSFVTNFTI 100
IYVKMGYPRL PVEKQCELAP TLLTAMEGKP QPQQDSLMHL LIPTLFHMKY 150
PVESSKSASP FNLAEKPKTV QLLLDFMLDV LLMPYGYVLN ESQSRQNSSS 200
AQGSSSNSGG GSGIPQPPPG MSFYAAKRVI GDNPWTPEQL EQCKLGIVKF 250
IEAEQVPELE AVLHLVIASS DTRHSVATAA DLELKSKQSL IDWNNPAIIN 300
KMYKVYLGDI PLKTKEGAVL KPELKRDPVS TRVKLKIVPH LLRSRQAAET 350
FPANIQVVYD GLFGTNTNSK LRTLSLQFVH HICITCPEIK IKPLGPMLLN 400
GLTKLINEYK EDPKLLSMAY SAVGKLSSRM PHLFTKDIAL VQQLFEALCK 450
EEPETRLAIQ EALSMMVGAY STLEGAQRTL MEALVASYLI KPEVQVRQVA 500
VKFASTVFPS DHIPSRYLLL LAAGDPREEV HGEAQRVLRC LPGRNRKEST 550
SEQMPSFPEM VYYIQEKASH RMKTPVKYMT GTTVLPFNPA AFGEIVLYLR 600
MCLAHSAGVV PTSQSLADMQ DHAPAIGRYI RTLMSSGQMA PSSSNKSGET 650
NPVQIYIGLL QQLLAGVGGL PVMYCLLEAV SVYPEKLATK FVDKTEWIKS 700
LMNNSKEEMR ELAALFYSVV VSTVSGNELK SMIEQLIKTT KDNHSPEIQH 750
GSLLALGFTV GRYLAKKKMR MSEQQDLERN ADTLPDQEEL IQSATETIGS 800
FLDSTSPLLA IAACTALGEI GRNGPLPIPS EGSGFTKLHL VESLLSRIPS 850
SKETNKMKER AIQTLGYFPV GDGDFPHQKL LLQGLMDSVE AKQIELQFTI 900
GEAITSAAIG TSSVAARDAW QMTEEEYTPP AGAKVNDVVP WVLDVILNKH 950
IISPNPHVRQ AACIWLLSLV RKLSTHKEVK SHLKEIQSAF VSVLSENDEL 1000
SQDVASKGLG LVYELGNEQD QQELVSTLVE TLMTGKRVKH EVSGETVVFQ 1050
GGALGKTPDG QGLSTYKELC SLASDLSQPD LVYKFMNLAN HHAMWNSRKG 1100
AAFGFNVIAT RAGEQLAPFL PQLVPRLYRY QFDPNLGIRQ AMTSIWNALV 1150
TDKSMVDKYL KEILQDLVKN LTSNMWRVRE SSCLALNDLL RGRPLDDIID 1200
KLPEIWETLF RVQDDIKESV RKAAELALKT LSKVCVKMCD PAKGAAGQRT 1250
IAALLPCLLD KGMMSTVTEV RALSINTLVK ISKSAGAMLK PHAPKLIPAL 1300
LESLSVLEPQ VLNYLSLRAT EQEKAAMDSA RLSAAKSSPM METINMCLQY 1350
LDVSVLGELV PRLCELIRSG VGLGTKGGCA SVIVSLTTQC PQDLTPYSGK 1400
LMSALLSGLT DRNSVIQKSC AFAMGHLVRT SRDSSTEKLL QKLNGWYMEK 1450
EEPIYKTSCA LTIHAIGRYS PDVLKNHAKE VLPLAFLGMH EIADEEKSEK 1500
EECNLWTEVW QENVPGSFGG IRLYLQELIT ITQKALQSQS WKMKAQGAIA 1550
MASIAKQTSS LVPPYLGMIL TALLQGLAGR TWAGKEELLK AIACVVTACS 1600
AELEKSVPNQ PSTNEILQAV LKECSKENVK YKIVAISCAA DILKATKEDR 1650
FQEFSNIVIP LIKKNSLESS GVRTTKNEEE NEKEKELQLE YLLGAFESLG 1700
KAWPRNAETQ RCYRQELCKL MCERLKLSTW KVQLGVLQSM NAFFQGLMLL 1750
EEEHADPEAL AEILLETCKS ITYSLENKTY SSVRTEALSV IELLLKKLEE 1800
SKQWECLTSE CRVLLIESLA TMEPDSRPEL QEKAALLKKT LENLE 1845
Length:1,845
Mass (Da):204,291
Last modified:March 15, 2005 - v2
Checksum:i5809A9208F5B4441
GO

Sequence cautioni

The sequence AAH21127.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAH73240.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH73465.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti472 – 4721T → S.
Corresponds to variant rs16916091 [ dbSNP | Ensembl ].
VAR_055702

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011I → N in AI916718. 1 Publication
Sequence conflicti101 – 1011I → N in AK127247. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL354661, AL159168 Genomic DNA. Translation: CAH73240.1. Sequence problems.
AL159168, AL354661 Genomic DNA. Translation: CAH73465.1. Sequence problems.
AI916718 mRNA. No translation available.
AK127247 mRNA. No translation available.
AB002366 mRNA. Translation: BAA20823.1.
BC021127 mRNA. Translation: AAH21127.1. Different initiation.
RefSeqiXP_005251907.1. XM_005251850.2.
UniGeneiHs.368255.

Genome annotation databases

EnsembliENST00000338205; ENSP00000339889; ENSG00000136813.
GeneIDi23392.
KEGGihsa:23392.

Polymorphism databases

DMDMi61212960.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL354661 , AL159168 Genomic DNA. Translation: CAH73240.1 . Sequence problems.
AL159168 , AL354661 Genomic DNA. Translation: CAH73465.1 . Sequence problems.
AI916718 mRNA. No translation available.
AK127247 mRNA. No translation available.
AB002366 mRNA. Translation: BAA20823.1 .
BC021127 mRNA. Translation: AAH21127.1 . Different initiation.
RefSeqi XP_005251907.1. XM_005251850.2.
UniGenei Hs.368255.

3D structure databases

ProteinModelPortali Q5VYK3.
SMRi Q5VYK3. Positions 396-467, 1165-1304, 1376-1440.
ModBasei Search...

Protein-protein interaction databases

IntActi Q5VYK3. 8 interactions.
MINTi MINT-1146313.
STRINGi 9606.ENSP00000259335.

PTM databases

PhosphoSitei Q5VYK3.

Polymorphism databases

DMDMi 61212960.

Proteomic databases

MaxQBi Q5VYK3.
PaxDbi Q5VYK3.
PRIDEi Q5VYK3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338205 ; ENSP00000339889 ; ENSG00000136813 .
GeneIDi 23392.
KEGGi hsa:23392.

Organism-specific databases

CTDi 23392.
GeneCardsi GC09M114122.
H-InvDB HIX0008281.
HGNCi HGNC:29020. KIAA0368.
HPAi HPA021646.
neXtProti NX_Q5VYK3.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250280.
HOGENOMi HOG000231642.
HOVERGENi HBG051438.
InParanoidi Q5VYK3.
KOi K11886.
OrthoDBi EOG79SDW5.
PhylomeDBi Q5VYK3.

Miscellaneous databases

GeneWikii KIAA0368.
GenomeRNAii 23392.
PROi Q5VYK3.

Gene expression databases

ArrayExpressi Q5VYK3.
Bgeei Q5VYK3.
CleanExi HS_KIAA0368.
Genevestigatori Q5VYK3.

Family and domain databases

Gene3Di 1.25.10.10. 6 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026827. ECM29/GCN1.
IPR024372. Proteasome_stabil_ECM29.
[Graphical view ]
PANTHERi PTHR23346. PTHR23346. 1 hit.
PTHR23346:SF19. PTHR23346:SF19. 1 hit.
Pfami PF13001. Ecm29. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 7 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. The MGC Project Team
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-194.
  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] OF 182-1845.
    Tissue: Hippocampus.
  4. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-1845.
    Tissue: Brain.
  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] OF 1301-1845.
    Tissue: B-cell.
  6. "Characterization of mammalian Ecm29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles."
    Gorbea C., Goellner G.M., Teter K., Holmes R.K., Rechsteiner M.
    J. Biol. Chem. 279:54849-54861(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
    Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
    J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS11; VPS26A; VPS36; RAB11FIP4; RABEP1; DCTN1; DCTN2; KIF5B; MYH7; MYH10; MYO10 AND ARF6.
  8. "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-830, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 THR-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiECM29_HUMAN
AccessioniPrimary (citable) accession number: Q5VYK3
Secondary accession number(s): O15074, Q8WU82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 104 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 9
    Human chromosome 9: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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