Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5JRA6

- MIA3_HUMAN

UniProt

Q5JRA6 - MIA3_HUMAN

Protein

Melanoma inhibitory activity protein 3

Gene

MIA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. May participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chondrocyte development Source: Ensembl
    2. collagen fibril organization Source: Ensembl
    3. exocytosis Source: UniProtKB
    4. negative regulation of cell adhesion Source: BHF-UCL
    5. negative regulation of cell migration Source: BHF-UCL
    6. positive regulation of bone mineralization Source: Ensembl
    7. positive regulation of leukocyte migration Source: BHF-UCL
    8. protein transport Source: UniProtKB
    9. wound healing Source: BHF-UCL

    Keywords - Biological processi

    ER-Golgi transport, Exocytosis, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Melanoma inhibitory activity protein 3
    Alternative name(s):
    C219-reactive peptide
    D320
    Transport and Golgi organization protein 1
    Gene namesi
    Name:MIA3
    Synonyms:KIAA0268, TANGO, TANGO1
    ORF Names:UNQ6077/PRO20088
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24008. MIA3.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: Localizes at endoplasmic reticulum exit sites. After loading of COL7A1 into transport carriers, it is not incorporated into COPII carriers and remains in the endoplasmic reticulum membrane.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. integral component of membrane Source: UniProtKB
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485536.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 19071885Melanoma inhibitory activity protein 3PRO_0000288998Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi589 – 5891N-linked (GlcNAc...)1 Publication
    Modified residuei1727 – 17271PhosphoserineBy similarity
    Modified residuei1741 – 17411PhosphoserineBy similarity
    Modified residuei1745 – 17451Phosphoserine1 Publication
    Modified residuei1892 – 18921PhosphoserineBy similarity
    Modified residuei1906 – 19061Phosphoserine1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ5JRA6.
    PaxDbiQ5JRA6.
    PRIDEiQ5JRA6.

    PTM databases

    PhosphoSiteiQ5JRA6.

    Miscellaneous databases

    PMAP-CutDBQ5JRA6.

    Expressioni

    Tissue specificityi

    Broadly expressed, except in bone marrow and peripheral blood mononuclear cells. Down-regulated in melanoma tissue.2 Publications

    Gene expression databases

    ArrayExpressiQ5JRA6.
    BgeeiQ5JRA6.
    CleanExiHS_MIA3.
    GenevestigatoriQ5JRA6.

    Organism-specific databases

    HPAiHPA055922.
    HPA056816.

    Interactioni

    Subunit structurei

    Interacts (via SH3 domain) with COL7A1. Associates with the COPII coat subunits Sec23/Sec24.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COL7A1Q023882EBI-2291868,EBI-724237

    Protein-protein interaction databases

    BioGridi131952. 6 interactions.
    IntActiQ5JRA6. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5JRA6.
    SMRiQ5JRA6. Positions 33-124.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 11441122ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1166 – 117611ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1198 – 1907710CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1145 – 116521Sequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1177 – 119721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 10763SH3Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili471 – 53161Sequence AnalysisAdd
    BLAST
    Coiled coili1214 – 1396183Sequence AnalysisAdd
    BLAST
    Coiled coili1487 – 1639153Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1640 – 1890251Pro-richAdd
    BLAST

    Domaini

    The proline-rich region (PRD) mediates the interaction with COPII coat subunits Sec23/24.1 Publication
    Although 2 transmembrane domains are predicted, PubMed:19269366 showed that it only contains one transmembrane domain. The other predicted transmembrane region is probably a hairpin-type region embedded into the membrane, which does not cross the membrane. It is unclear which of the 2 predicted transmembrane regions is the transmembrane or the hairpin-type region.1 Publication

    Sequence similaritiesi

    Belongs to the MIA/OTOR family. Tango1 subfamily.Curated
    Contains 1 SH3 domain.Curated

    Keywords - Domaini

    Coiled coil, SH3 domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG133684.
    HOVERGENiHBG108133.
    InParanoidiQ5JRA6.
    OMAiDTIFSIV.
    OrthoDBiEOG74TWXQ.
    PhylomeDBiQ5JRA6.
    TreeFamiTF333137.

    Family and domain databases

    InterProiIPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF07653. SH3_2. 1 hit.
    [Graphical view]
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5JRA6-1) [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

    MAAAPGLLVW LLVLRLPWRV PGQLDPSTGR RFSEHKLCAD DECSMLMYRG     50
    EALEDFTGPD CRFVNFKKGD PVYVYYKLAR GWPEVWAGSV GRTFGYFPKD 100
    LIQVVHEYTK EELQVPTDET DFVCFDGGRD DFHNYNVEEL LGFLELYNSA 150
    ATDSEKAVEK TLQDMEKNPE LSKEREPEPE PVEANSEESD SVFSENTEDL 200
    QEQFTTQKHH SHANSQANHA QGEQASFESF EEMLQDKLKV PESENNKTSN 250
    SSQVSNEQDK IDAYKLLKKE MTLDLKTKFG STADALVSDD ETTRLVTSLE 300
    DDFDEELDTE YYAVGKEDEE NQEDFDELPL LTFTDGEDMK TPAKSGVEKY 350
    PTDKEQNSNE EDKVQLTVPP GIKNDDKNIL TTWGDTIFSI VTGGEETRDT 400
    MDLESSSSEE EKEDDDDALV PDSKQGKPQS ATDYSDPDNV DDGLFIVDIP 450
    KTNNDKEVNA EHHIKGKGRG VQESKRGLVQ DKTELEDENQ EGMTVHSSVH 500
    SNNLNSMPAA EKGKDTLKSA YDDTENDLKG AAIHISKGML HEEKPGEQIL 550
    EGGSESESAQ KAAGNQMNDR KIQQESLGSA PLMGDDHPNA SRDSVEGDAL 600
    VNGAKLHTLS VEHQREELKE ELVLKTQNQP RFSSPDEIDL PRELEDEVPI 650
    LGRNLPWQQE RDVAATASKQ MSEKIRLSEG EAKEDSLDEE FFHHKAMQGT 700
    EVGQTDQTDS TGGPAFLSKV EEDDYPSEEL LEDENAINAK RSKEKNPGNQ 750
    GRQFDVNLQV PDRAVLGTIH PDPEIEESKQ ETSMILDSEK TSETAAKGVN 800
    TGGREPNTMV EKERPLADKK AQRPFERSDF SDSIKIQTPE LGEVFQNKDS 850
    DYLKNDNPEE HLKTSGLAGE PEGELSKEDH ENTEKYMGTE SQGSAAAEPE 900
    DDSFHWTPHT SVEPGHSDKR EDLLIISSFF KEQQSLQRFQ KYFNVHELEA 950
    LLQEMSSKLK SAQQESLPYN MEKVLDKVFR ASESQILSIA EKMLDTRVAE 1000
    NRDLGMNENN IFEEAAVLDD IQDLIYFVRY KHSTAEETAT LVMAPPLEEG 1050
    LGGAMEEMQP LHEDNFSREK TAELNVQVPE EPTHLDQRVI GDTHASEVSQ 1100
    KPNTEKDLDP GPVTTEDTPM DAIDANKQPE TAAEEPASVT PLENAILLIY 1150
    SFMFYLTKSL VATLPDDVQP GPDFYGLPWK PVFITAFLGI ASFAIFLWRT 1200
    VLVVKDRVYQ VTEQQISEKL KTIMKENTEL VQKLSNYEQK IKESKKHVQE 1250
    TRKQNMILSD EAIKYKDKIK TLEKNQEILD DTAKNLRVML ESEREQNVKN 1300
    QDLISENKKS IEKLKDVISM NASEFSEVQI ALNEAKLSEE KVKSECHRVQ 1350
    EENARLKKKK EQLQQEIEDW SKLHAELSEQ IKSFEKSQKD LEVALTHKDD 1400
    NINALTNCIT QLNLLECESE SEGQNKGGND SDELANGEVG GDRNEKMKNQ 1450
    IKQMMDVSRT QTAISVVEED LKLLQLKLRA SVSTKCNLED QVKKLEDDRN 1500
    SLQAAKAGLE DECKTLRQKV EILNELYQQK EMALQKKLSQ EEYERQEREH 1550
    RLSAADEKAV SAAEEVKTYK RRIEEMEDEL QKTERSFKNQ IATHEKKAHE 1600
    NWLKARAAER AIAEEKREAA NLRHKLLELT QKMAMLQEEP VIVKPMPGKP 1650
    NTQNPPRRGP LSQNGSFGPS PVSGGECSPP LTVEPPVRPL SATLNRRDMP 1700
    RSEFGSVDGP LPHPRWSAEA SGKPSPSDPG SGTATMMNSS SRGSSPTRVL 1750
    DEGKVNMAPK GPPPFPGVPL MSTPMGGPVP PPIRYGPPPQ LCGPFGPRPL 1800
    PPPFGPGMRP PLGLREFAPG VPPGRRDLPL HPRGFLPGHA PFRPLGSLGP 1850
    REYFIPGTRL PPPTHGPQEY PPPPAVRDLL PSGSRDEPPP ASQSTSQDCS 1900
    QALKQSP 1907
    Length:1,907
    Mass (Da):213,702
    Last modified:February 15, 2005 - v1
    Checksum:iD19C9AF1656F4B1C
    GO
    Isoform 2 (identifier: Q5JRA6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1304-1362: Missing.

    Show »
    Length:1,848
    Mass (Da):206,890
    Checksum:iB793E3992499E137
    GO
    Isoform 3 (identifier: Q5JRA6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         493-500: MTVHSSVH → FKTEPIKL
         501-1907: Missing.

    Show »
    Length:500
    Mass (Da):56,584
    Checksum:iF785E148171092E6
    GO
    Isoform 4 (identifier: Q5JRA6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1122: Missing.
         1123-1159: IDANKQPETAAEEPASVTPLENAILLIYSFMFYLTKS → MDSVPATVPSIAATPGDPELVGPLSVLYAAFIAKLLE

    Show »
    Length:785
    Mass (Da):87,438
    Checksum:i0A3890131D1BA2D5
    GO

    Sequence cautioni

    The sequence BAC04810.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAF83024.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI40474.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461Missing in AAQ89449. (PubMed:12975309)Curated
    Sequence conflicti1032 – 10321H → R in BAC04810. (PubMed:14702039)Curated
    Sequence conflicti1443 – 14431R → Q in AAH47116. (PubMed:15489334)Curated
    Sequence conflicti1754 – 17541K → R in BAH12416. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti482 – 4821K → E.1 Publication
    Corresponds to variant rs2936053 [ dbSNP | Ensembl ].
    VAR_032546
    Natural varianti605 – 6051K → R.
    Corresponds to variant rs2936052 [ dbSNP | Ensembl ].
    VAR_032547
    Natural varianti881 – 8811E → G.1 Publication
    Corresponds to variant rs2936051 [ dbSNP | Ensembl ].
    VAR_032548
    Natural varianti1659 – 16591G → C.1 Publication
    Corresponds to variant rs17857325 [ dbSNP | Ensembl ].
    VAR_032549
    Natural varianti1723 – 17231K → E.1 Publication
    Corresponds to variant rs17854428 [ dbSNP | Ensembl ].
    VAR_032550

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11221122Missing in isoform 4. 1 PublicationVSP_025860Add
    BLAST
    Alternative sequencei493 – 5008MTVHSSVH → FKTEPIKL in isoform 3. 1 PublicationVSP_025861
    Alternative sequencei501 – 19071407Missing in isoform 3. 1 PublicationVSP_025862Add
    BLAST
    Alternative sequencei1123 – 115937IDANK…YLTKS → MDSVPATVPSIAATPGDPEL VGPLSVLYAAFIAKLLE in isoform 4. 1 PublicationVSP_025863Add
    BLAST
    Alternative sequencei1304 – 136259Missing in isoform 2. 1 PublicationVSP_025864Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY359091 mRNA. Translation: AAQ89449.1.
    AK096526 mRNA. Translation: BAC04810.1. Different initiation.
    AK290335 mRNA. Translation: BAF83024.1. Different initiation.
    AK296712 mRNA. Translation: BAH12416.1.
    AL592148 Genomic DNA. Translation: CAI40469.1.
    AL592148 Genomic DNA. Translation: CAI40470.1.
    AL592148 Genomic DNA. Translation: CAI40471.1.
    AL592148 Genomic DNA. Translation: CAI40473.1.
    AL592148 Genomic DNA. Translation: CAI40474.1. Sequence problems.
    D87742 mRNA. Translation: BAA13448.1.
    L34688 mRNA. Translation: AAB00324.1.
    DQ166034 mRNA. Translation: AAZ95512.1.
    BC047116 mRNA. Translation: AAH47116.2.
    CCDSiCCDS41470.1. [Q5JRA6-1]
    RefSeqiNP_940953.2. NM_198551.2. [Q5JRA6-1]
    XP_005273179.1. XM_005273122.2. [Q5JRA6-4]
    UniGeneiHs.118474.

    Genome annotation databases

    EnsembliENST00000340535; ENSP00000345866; ENSG00000154305. [Q5JRA6-4]
    ENST00000344507; ENSP00000341348; ENSG00000154305. [Q5JRA6-3]
    ENST00000344922; ENSP00000340900; ENSG00000154305. [Q5JRA6-1]
    GeneIDi375056.
    KEGGihsa:375056.
    UCSCiuc001hnl.3. human. [Q5JRA6-1]
    uc001hnm.3. human. [Q5JRA6-4]
    uc009xea.1. human. [Q5JRA6-2]

    Polymorphism databases

    DMDMi74741823.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY359091 mRNA. Translation: AAQ89449.1 .
    AK096526 mRNA. Translation: BAC04810.1 . Different initiation.
    AK290335 mRNA. Translation: BAF83024.1 . Different initiation.
    AK296712 mRNA. Translation: BAH12416.1 .
    AL592148 Genomic DNA. Translation: CAI40469.1 .
    AL592148 Genomic DNA. Translation: CAI40470.1 .
    AL592148 Genomic DNA. Translation: CAI40471.1 .
    AL592148 Genomic DNA. Translation: CAI40473.1 .
    AL592148 Genomic DNA. Translation: CAI40474.1 . Sequence problems.
    D87742 mRNA. Translation: BAA13448.1 .
    L34688 mRNA. Translation: AAB00324.1 .
    DQ166034 mRNA. Translation: AAZ95512.1 .
    BC047116 mRNA. Translation: AAH47116.2 .
    CCDSi CCDS41470.1. [Q5JRA6-1 ]
    RefSeqi NP_940953.2. NM_198551.2. [Q5JRA6-1 ]
    XP_005273179.1. XM_005273122.2. [Q5JRA6-4 ]
    UniGenei Hs.118474.

    3D structure databases

    ProteinModelPortali Q5JRA6.
    SMRi Q5JRA6. Positions 33-124.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 131952. 6 interactions.
    IntActi Q5JRA6. 5 interactions.

    PTM databases

    PhosphoSitei Q5JRA6.

    Polymorphism databases

    DMDMi 74741823.

    Proteomic databases

    MaxQBi Q5JRA6.
    PaxDbi Q5JRA6.
    PRIDEi Q5JRA6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340535 ; ENSP00000345866 ; ENSG00000154305 . [Q5JRA6-4 ]
    ENST00000344507 ; ENSP00000341348 ; ENSG00000154305 . [Q5JRA6-3 ]
    ENST00000344922 ; ENSP00000340900 ; ENSG00000154305 . [Q5JRA6-1 ]
    GeneIDi 375056.
    KEGGi hsa:375056.
    UCSCi uc001hnl.3. human. [Q5JRA6-1 ]
    uc001hnm.3. human. [Q5JRA6-4 ]
    uc009xea.1. human. [Q5JRA6-2 ]

    Organism-specific databases

    CTDi 375056.
    GeneCardsi GC01P222791.
    H-InvDB HIX0001613.
    HGNCi HGNC:24008. MIA3.
    HPAi HPA055922.
    HPA056816.
    MIMi 613455. gene.
    neXtProti NX_Q5JRA6.
    PharmGKBi PA143485536.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG133684.
    HOVERGENi HBG108133.
    InParanoidi Q5JRA6.
    OMAi DTIFSIV.
    OrthoDBi EOG74TWXQ.
    PhylomeDBi Q5JRA6.
    TreeFami TF333137.

    Miscellaneous databases

    ChiTaRSi MIA3. human.
    GenomeRNAii 375056.
    NextBioi 100389.
    PMAP-CutDB Q5JRA6.
    PROi Q5JRA6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5JRA6.
    Bgeei Q5JRA6.
    CleanExi HS_MIA3.
    Genevestigatori Q5JRA6.

    Family and domain databases

    InterProi IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF07653. SH3_2. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT GLU-482.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 419-1492 (ISOFORM 2).
      Tissue: Brain and Tongue.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Characterization and expression pattern of the novel MIA homolog TANGO."
      Bosserhoff A.K., Moser M., Buettner R.
      Gene Expr. Patterns 4:473-479(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-125, TISSUE SPECIFICITY.
    5. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-1907 (ISOFORM 1), VARIANT GLY-881.
      Tissue: Bone marrow.
    6. "Analysis of a novel cDNA encoding a C219-reactive peptide isolated from methotrexate-selected multidrug-resistant human leukemic cells."
      Norris M.D., Gilbert J., Madafiglio J., Haber M.
      Gene 156:313-314(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1306-1441.
      Tissue: Leukemia.
    7. "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 1441-1907 (ISOFORM 1), VARIANTS CYS-1659 AND GLU-1723.
      Tissue: Brain.
    8. "TANGO is a tumor suppressor of malignant melanoma."
      Arndt S., Bosserhoff A.K.
      Int. J. Cancer 119:2812-2820(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1906, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites."
      Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D., Polischuk R., Schekman R., Malhotra V.
      Cell 136:891-902(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COL7A1, TOPOLOGY, DOMAIN.
    12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-589.
      Tissue: Liver.
    13. "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.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-1745, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMIA3_HUMAN
    AccessioniPrimary (citable) accession number: Q5JRA6
    Secondary accession number(s): A8K2S0
    , A8MT05, A8MT13, B7Z430, Q14083, Q3S4X3, Q5JRA5, Q5JRB0, Q5JRB1, Q5JRB2, Q6UVY8, Q86Y60, Q8N8M5, Q92580
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 91 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3