Full text data of ECM29
ECM29
(KIAA0368)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Proteasome-associated protein ECM29 homolog; Ecm29
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome-associated protein ECM29 homolog; Ecm29
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q5VYK3
ID ECM29_HUMAN Reviewed; 1845 AA.
AC Q5VYK3; O15074; Q8WU82;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Proteasome-associated protein ECM29 homolog;
DE Short=Ecm29;
GN Name=ECM29; Synonyms=KIAA0368;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-194.
RG The MGC Project Team;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-1845.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-1845.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1301-1845.
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15496406; DOI=10.1074/jbc.M410444200;
RA Gorbea C., Goellner G.M., Teter K., Holmes R.K., Rechsteiner M.;
RT "Characterization of mammalian Ecm29, a 26 S proteasome-associated
RT protein that localizes to the nucleus and membrane vesicles.";
RL J. Biol. Chem. 279:54849-54861(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS11; VPS26A;
RP VPS36; RAB11FIP4; RABEP1; DCTN1; DCTN2; KIF5B; MYH7; MYH10; MYO10 AND
RP ARF6.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Adapter/scaffolding protein that binds to the 26S
CC proteasome, motor proteins and other compartment specific
CC proteins. May couple the proteasome to different compartments
CC including endosome, endoplasmic reticulum and centrosome. May play
CC a role in ERAD and other enhanced proteolyis.
CC -!- SUBUNIT: Non-stoichiometric component of the proteasome;
CC associates with the 26S proteasome. Interacts (via N-terminus)
CC with VPS11, VPS26A, VPS36, RAB11FIP4 and RABEP1. Interacts (via C-
CC terminus) with DCTN1, DCTN2, KIF5B, MYH7, MYH10, MYO10 and ARF6.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Endoplasmic
CC reticulum-Golgi intermediate compartment. Endosome. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome. Nucleus.
CC Endosome, multivesicular body. Cytoplasmic vesicle.
CC -!- SIMILARITY: Contains 27 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21127.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAH73240.1; Type=Erroneous gene model prediction;
CC Sequence=CAH73465.1; Type=Erroneous gene model prediction;
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DR EMBL; AL354661; CAH73240.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL159168; CAH73240.1; JOINED; Genomic_DNA.
DR EMBL; AL159168; CAH73465.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL354661; CAH73465.1; JOINED; Genomic_DNA.
DR EMBL; AI916718; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK127247; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB002366; BAA20823.1; -; mRNA.
DR EMBL; BC021127; AAH21127.1; ALT_INIT; mRNA.
DR RefSeq; XP_005251907.1; XM_005251850.1.
DR UniGene; Hs.368255; -.
DR ProteinModelPortal; Q5VYK3; -.
DR SMR; Q5VYK3; 396-467, 1165-1304, 1376-1440.
DR IntAct; Q5VYK3; 8.
DR MINT; MINT-1146313; -.
DR STRING; 9606.ENSP00000259335; -.
DR PhosphoSite; Q5VYK3; -.
DR DMDM; 61212960; -.
DR PaxDb; Q5VYK3; -.
DR PRIDE; Q5VYK3; -.
DR Ensembl; ENST00000338205; ENSP00000339889; ENSG00000136813.
DR GeneID; 23392; -.
DR GeneCards; GC09M114122; -.
DR H-InvDB; HIX0008281; -.
DR HGNC; HGNC:29020; KIAA0368.
DR HPA; HPA021646; -.
DR neXtProt; NX_Q5VYK3; -.
DR eggNOG; NOG250280; -.
DR HOGENOM; HOG000231642; -.
DR HOVERGEN; HBG051438; -.
DR InParanoid; Q5VYK3; -.
DR OrthoDB; EOG79SDW5; -.
DR GeneWiki; KIAA0368; -.
DR PRO; PR:Q5VYK3; -.
DR ArrayExpress; Q5VYK3; -.
DR Bgee; Q5VYK3; -.
DR CleanEx; HS_KIAA0368; -.
DR Genevestigator; Q5VYK3; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0030134; C:ER to Golgi transport vesicle; IDA:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 6.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026827; ECM29/GCN1.
DR InterPro; IPR026826; ECM29_metazoa.
DR InterPro; IPR024372; Proteasome_stabil_ECM29.
DR PANTHER; PTHR23346; PTHR23346; 1.
DR PANTHER; PTHR23346:SF13; PTHR23346:SF13; 1.
DR Pfam; PF13001; Ecm29; 1.
DR SUPFAM; SSF48371; SSF48371; 7.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endoplasmic reticulum; Endosome; Nucleus;
KW Phosphoprotein; Polymorphism; Proteasome; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1845 Proteasome-associated protein ECM29
FT homolog.
FT /FTId=PRO_0000212559.
FT REPEAT 34 71 HEAT 1.
FT REPEAT 113 150 HEAT 2.
FT REPEAT 168 211 HEAT 3.
FT REPEAT 332 368 HEAT 4.
FT REPEAT 393 432 HEAT 5.
FT REPEAT 435 472 HEAT 6.
FT REPEAT 475 513 HEAT 7.
FT REPEAT 689 726 HEAT 8.
FT REPEAT 727 765 HEAT 9.
FT REPEAT 789 826 HEAT 10.
FT REPEAT 835 874 HEAT 11.
FT REPEAT 876 913 HEAT 12.
FT REPEAT 937 975 HEAT 13.
FT REPEAT 981 1018 HEAT 14.
FT REPEAT 1019 1056 HEAT 15.
FT REPEAT 1118 1155 HEAT 16.
FT REPEAT 1158 1195 HEAT 17.
FT REPEAT 1200 1237 HEAT 18.
FT REPEAT 1249 1287 HEAT 19.
FT REPEAT 1291 1329 HEAT 20.
FT REPEAT 1354 1392 HEAT 21.
FT REPEAT 1396 1433 HEAT 22.
FT REPEAT 1523 1560 HEAT 23.
FT REPEAT 1564 1601 HEAT 24.
FT REPEAT 1611 1648 HEAT 25.
FT REPEAT 1652 1689 HEAT 26.
FT REPEAT 1785 1828 HEAT 27.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 830 830 Phosphoserine.
FT MOD_RES 836 836 Phosphothreonine.
FT VARIANT 472 472 T -> S (in dbSNP:rs16916091).
FT /FTId=VAR_055702.
FT CONFLICT 101 101 I -> N (in Ref. 2; AI916718/AK127247).
SQ SEQUENCE 1845 AA; 204291 MW; 5809A9208F5B4441 CRC64;
MAAAAASASQ DELNQLERVF LRLGHAETDE QLQNIISKFL PPVLLKLSST QEGVRKKVME
LLVHLNKRIK SRPKIQLPVE TLLVQYQDPA AVSFVTNFTI IYVKMGYPRL PVEKQCELAP
TLLTAMEGKP QPQQDSLMHL LIPTLFHMKY PVESSKSASP FNLAEKPKTV QLLLDFMLDV
LLMPYGYVLN ESQSRQNSSS AQGSSSNSGG GSGIPQPPPG MSFYAAKRVI GDNPWTPEQL
EQCKLGIVKF IEAEQVPELE AVLHLVIASS DTRHSVATAA DLELKSKQSL IDWNNPAIIN
KMYKVYLGDI PLKTKEGAVL KPELKRDPVS TRVKLKIVPH LLRSRQAAET FPANIQVVYD
GLFGTNTNSK LRTLSLQFVH HICITCPEIK IKPLGPMLLN GLTKLINEYK EDPKLLSMAY
SAVGKLSSRM PHLFTKDIAL VQQLFEALCK EEPETRLAIQ EALSMMVGAY STLEGAQRTL
MEALVASYLI KPEVQVRQVA VKFASTVFPS DHIPSRYLLL LAAGDPREEV HGEAQRVLRC
LPGRNRKEST SEQMPSFPEM VYYIQEKASH RMKTPVKYMT GTTVLPFNPA AFGEIVLYLR
MCLAHSAGVV PTSQSLADMQ DHAPAIGRYI RTLMSSGQMA PSSSNKSGET NPVQIYIGLL
QQLLAGVGGL PVMYCLLEAV SVYPEKLATK FVDKTEWIKS LMNNSKEEMR ELAALFYSVV
VSTVSGNELK SMIEQLIKTT KDNHSPEIQH GSLLALGFTV GRYLAKKKMR MSEQQDLERN
ADTLPDQEEL IQSATETIGS FLDSTSPLLA IAACTALGEI GRNGPLPIPS EGSGFTKLHL
VESLLSRIPS SKETNKMKER AIQTLGYFPV GDGDFPHQKL LLQGLMDSVE AKQIELQFTI
GEAITSAAIG TSSVAARDAW QMTEEEYTPP AGAKVNDVVP WVLDVILNKH IISPNPHVRQ
AACIWLLSLV RKLSTHKEVK SHLKEIQSAF VSVLSENDEL SQDVASKGLG LVYELGNEQD
QQELVSTLVE TLMTGKRVKH EVSGETVVFQ GGALGKTPDG QGLSTYKELC SLASDLSQPD
LVYKFMNLAN HHAMWNSRKG AAFGFNVIAT RAGEQLAPFL PQLVPRLYRY QFDPNLGIRQ
AMTSIWNALV TDKSMVDKYL KEILQDLVKN LTSNMWRVRE SSCLALNDLL RGRPLDDIID
KLPEIWETLF RVQDDIKESV RKAAELALKT LSKVCVKMCD PAKGAAGQRT IAALLPCLLD
KGMMSTVTEV RALSINTLVK ISKSAGAMLK PHAPKLIPAL LESLSVLEPQ VLNYLSLRAT
EQEKAAMDSA RLSAAKSSPM METINMCLQY LDVSVLGELV PRLCELIRSG VGLGTKGGCA
SVIVSLTTQC PQDLTPYSGK LMSALLSGLT DRNSVIQKSC AFAMGHLVRT SRDSSTEKLL
QKLNGWYMEK EEPIYKTSCA LTIHAIGRYS PDVLKNHAKE VLPLAFLGMH EIADEEKSEK
EECNLWTEVW QENVPGSFGG IRLYLQELIT ITQKALQSQS WKMKAQGAIA MASIAKQTSS
LVPPYLGMIL TALLQGLAGR TWAGKEELLK AIACVVTACS AELEKSVPNQ PSTNEILQAV
LKECSKENVK YKIVAISCAA DILKATKEDR FQEFSNIVIP LIKKNSLESS GVRTTKNEEE
NEKEKELQLE YLLGAFESLG KAWPRNAETQ RCYRQELCKL MCERLKLSTW KVQLGVLQSM
NAFFQGLMLL EEEHADPEAL AEILLETCKS ITYSLENKTY SSVRTEALSV IELLLKKLEE
SKQWECLTSE CRVLLIESLA TMEPDSRPEL QEKAALLKKT LENLE
//
ID ECM29_HUMAN Reviewed; 1845 AA.
AC Q5VYK3; O15074; Q8WU82;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Proteasome-associated protein ECM29 homolog;
DE Short=Ecm29;
GN Name=ECM29; Synonyms=KIAA0368;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-194.
RG The MGC Project Team;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-1845.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-1845.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1301-1845.
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15496406; DOI=10.1074/jbc.M410444200;
RA Gorbea C., Goellner G.M., Teter K., Holmes R.K., Rechsteiner M.;
RT "Characterization of mammalian Ecm29, a 26 S proteasome-associated
RT protein that localizes to the nucleus and membrane vesicles.";
RL J. Biol. Chem. 279:54849-54861(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS11; VPS26A;
RP VPS36; RAB11FIP4; RABEP1; DCTN1; DCTN2; KIF5B; MYH7; MYH10; MYO10 AND
RP ARF6.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Adapter/scaffolding protein that binds to the 26S
CC proteasome, motor proteins and other compartment specific
CC proteins. May couple the proteasome to different compartments
CC including endosome, endoplasmic reticulum and centrosome. May play
CC a role in ERAD and other enhanced proteolyis.
CC -!- SUBUNIT: Non-stoichiometric component of the proteasome;
CC associates with the 26S proteasome. Interacts (via N-terminus)
CC with VPS11, VPS26A, VPS36, RAB11FIP4 and RABEP1. Interacts (via C-
CC terminus) with DCTN1, DCTN2, KIF5B, MYH7, MYH10, MYO10 and ARF6.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Endoplasmic
CC reticulum-Golgi intermediate compartment. Endosome. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome. Nucleus.
CC Endosome, multivesicular body. Cytoplasmic vesicle.
CC -!- SIMILARITY: Contains 27 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21127.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAH73240.1; Type=Erroneous gene model prediction;
CC Sequence=CAH73465.1; Type=Erroneous gene model prediction;
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DR EMBL; AL354661; CAH73240.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL159168; CAH73240.1; JOINED; Genomic_DNA.
DR EMBL; AL159168; CAH73465.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL354661; CAH73465.1; JOINED; Genomic_DNA.
DR EMBL; AI916718; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK127247; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB002366; BAA20823.1; -; mRNA.
DR EMBL; BC021127; AAH21127.1; ALT_INIT; mRNA.
DR RefSeq; XP_005251907.1; XM_005251850.1.
DR UniGene; Hs.368255; -.
DR ProteinModelPortal; Q5VYK3; -.
DR SMR; Q5VYK3; 396-467, 1165-1304, 1376-1440.
DR IntAct; Q5VYK3; 8.
DR MINT; MINT-1146313; -.
DR STRING; 9606.ENSP00000259335; -.
DR PhosphoSite; Q5VYK3; -.
DR DMDM; 61212960; -.
DR PaxDb; Q5VYK3; -.
DR PRIDE; Q5VYK3; -.
DR Ensembl; ENST00000338205; ENSP00000339889; ENSG00000136813.
DR GeneID; 23392; -.
DR GeneCards; GC09M114122; -.
DR H-InvDB; HIX0008281; -.
DR HGNC; HGNC:29020; KIAA0368.
DR HPA; HPA021646; -.
DR neXtProt; NX_Q5VYK3; -.
DR eggNOG; NOG250280; -.
DR HOGENOM; HOG000231642; -.
DR HOVERGEN; HBG051438; -.
DR InParanoid; Q5VYK3; -.
DR OrthoDB; EOG79SDW5; -.
DR GeneWiki; KIAA0368; -.
DR PRO; PR:Q5VYK3; -.
DR ArrayExpress; Q5VYK3; -.
DR Bgee; Q5VYK3; -.
DR CleanEx; HS_KIAA0368; -.
DR Genevestigator; Q5VYK3; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0030134; C:ER to Golgi transport vesicle; IDA:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 6.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026827; ECM29/GCN1.
DR InterPro; IPR026826; ECM29_metazoa.
DR InterPro; IPR024372; Proteasome_stabil_ECM29.
DR PANTHER; PTHR23346; PTHR23346; 1.
DR PANTHER; PTHR23346:SF13; PTHR23346:SF13; 1.
DR Pfam; PF13001; Ecm29; 1.
DR SUPFAM; SSF48371; SSF48371; 7.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endoplasmic reticulum; Endosome; Nucleus;
KW Phosphoprotein; Polymorphism; Proteasome; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1845 Proteasome-associated protein ECM29
FT homolog.
FT /FTId=PRO_0000212559.
FT REPEAT 34 71 HEAT 1.
FT REPEAT 113 150 HEAT 2.
FT REPEAT 168 211 HEAT 3.
FT REPEAT 332 368 HEAT 4.
FT REPEAT 393 432 HEAT 5.
FT REPEAT 435 472 HEAT 6.
FT REPEAT 475 513 HEAT 7.
FT REPEAT 689 726 HEAT 8.
FT REPEAT 727 765 HEAT 9.
FT REPEAT 789 826 HEAT 10.
FT REPEAT 835 874 HEAT 11.
FT REPEAT 876 913 HEAT 12.
FT REPEAT 937 975 HEAT 13.
FT REPEAT 981 1018 HEAT 14.
FT REPEAT 1019 1056 HEAT 15.
FT REPEAT 1118 1155 HEAT 16.
FT REPEAT 1158 1195 HEAT 17.
FT REPEAT 1200 1237 HEAT 18.
FT REPEAT 1249 1287 HEAT 19.
FT REPEAT 1291 1329 HEAT 20.
FT REPEAT 1354 1392 HEAT 21.
FT REPEAT 1396 1433 HEAT 22.
FT REPEAT 1523 1560 HEAT 23.
FT REPEAT 1564 1601 HEAT 24.
FT REPEAT 1611 1648 HEAT 25.
FT REPEAT 1652 1689 HEAT 26.
FT REPEAT 1785 1828 HEAT 27.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 830 830 Phosphoserine.
FT MOD_RES 836 836 Phosphothreonine.
FT VARIANT 472 472 T -> S (in dbSNP:rs16916091).
FT /FTId=VAR_055702.
FT CONFLICT 101 101 I -> N (in Ref. 2; AI916718/AK127247).
SQ SEQUENCE 1845 AA; 204291 MW; 5809A9208F5B4441 CRC64;
MAAAAASASQ DELNQLERVF LRLGHAETDE QLQNIISKFL PPVLLKLSST QEGVRKKVME
LLVHLNKRIK SRPKIQLPVE TLLVQYQDPA AVSFVTNFTI IYVKMGYPRL PVEKQCELAP
TLLTAMEGKP QPQQDSLMHL LIPTLFHMKY PVESSKSASP FNLAEKPKTV QLLLDFMLDV
LLMPYGYVLN ESQSRQNSSS AQGSSSNSGG GSGIPQPPPG MSFYAAKRVI GDNPWTPEQL
EQCKLGIVKF IEAEQVPELE AVLHLVIASS DTRHSVATAA DLELKSKQSL IDWNNPAIIN
KMYKVYLGDI PLKTKEGAVL KPELKRDPVS TRVKLKIVPH LLRSRQAAET FPANIQVVYD
GLFGTNTNSK LRTLSLQFVH HICITCPEIK IKPLGPMLLN GLTKLINEYK EDPKLLSMAY
SAVGKLSSRM PHLFTKDIAL VQQLFEALCK EEPETRLAIQ EALSMMVGAY STLEGAQRTL
MEALVASYLI KPEVQVRQVA VKFASTVFPS DHIPSRYLLL LAAGDPREEV HGEAQRVLRC
LPGRNRKEST SEQMPSFPEM VYYIQEKASH RMKTPVKYMT GTTVLPFNPA AFGEIVLYLR
MCLAHSAGVV PTSQSLADMQ DHAPAIGRYI RTLMSSGQMA PSSSNKSGET NPVQIYIGLL
QQLLAGVGGL PVMYCLLEAV SVYPEKLATK FVDKTEWIKS LMNNSKEEMR ELAALFYSVV
VSTVSGNELK SMIEQLIKTT KDNHSPEIQH GSLLALGFTV GRYLAKKKMR MSEQQDLERN
ADTLPDQEEL IQSATETIGS FLDSTSPLLA IAACTALGEI GRNGPLPIPS EGSGFTKLHL
VESLLSRIPS SKETNKMKER AIQTLGYFPV GDGDFPHQKL LLQGLMDSVE AKQIELQFTI
GEAITSAAIG TSSVAARDAW QMTEEEYTPP AGAKVNDVVP WVLDVILNKH IISPNPHVRQ
AACIWLLSLV RKLSTHKEVK SHLKEIQSAF VSVLSENDEL SQDVASKGLG LVYELGNEQD
QQELVSTLVE TLMTGKRVKH EVSGETVVFQ GGALGKTPDG QGLSTYKELC SLASDLSQPD
LVYKFMNLAN HHAMWNSRKG AAFGFNVIAT RAGEQLAPFL PQLVPRLYRY QFDPNLGIRQ
AMTSIWNALV TDKSMVDKYL KEILQDLVKN LTSNMWRVRE SSCLALNDLL RGRPLDDIID
KLPEIWETLF RVQDDIKESV RKAAELALKT LSKVCVKMCD PAKGAAGQRT IAALLPCLLD
KGMMSTVTEV RALSINTLVK ISKSAGAMLK PHAPKLIPAL LESLSVLEPQ VLNYLSLRAT
EQEKAAMDSA RLSAAKSSPM METINMCLQY LDVSVLGELV PRLCELIRSG VGLGTKGGCA
SVIVSLTTQC PQDLTPYSGK LMSALLSGLT DRNSVIQKSC AFAMGHLVRT SRDSSTEKLL
QKLNGWYMEK EEPIYKTSCA LTIHAIGRYS PDVLKNHAKE VLPLAFLGMH EIADEEKSEK
EECNLWTEVW QENVPGSFGG IRLYLQELIT ITQKALQSQS WKMKAQGAIA MASIAKQTSS
LVPPYLGMIL TALLQGLAGR TWAGKEELLK AIACVVTACS AELEKSVPNQ PSTNEILQAV
LKECSKENVK YKIVAISCAA DILKATKEDR FQEFSNIVIP LIKKNSLESS GVRTTKNEEE
NEKEKELQLE YLLGAFESLG KAWPRNAETQ RCYRQELCKL MCERLKLSTW KVQLGVLQSM
NAFFQGLMLL EEEHADPEAL AEILLETCKS ITYSLENKTY SSVRTEALSV IELLLKKLEE
SKQWECLTSE CRVLLIESLA TMEPDSRPEL QEKAALLKKT LENLE
//