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P53990

- IST1_HUMAN

UniProt

P53990 - IST1_HUMAN

Protein

IST1 homolog

Gene

IST1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Proposed to be involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells.2 Publications

    GO - Molecular functioni

    1. MIT domain binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein complex binding Source: UniProtKB
    4. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. abscission Source: UniProtKB
    2. cell division Source: UniProtKB
    3. cytokinesis Source: UniProtKB
    4. establishment of protein localization Source: UniProt
    5. positive regulation of collateral sprouting Source: Ensembl
    6. positive regulation of proteolysis Source: UniProtKB
    7. protein localization Source: UniProtKB
    8. viral capsid secondary envelopment Source: UniProtKB
    9. viral release from host cell Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    IST1 homolog
    Short name:
    hIST1
    Alternative name(s):
    Putative MAPK-activating protein PM28
    Gene namesi
    Name:IST1
    Synonyms:KIAA0174
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:28977. IST1.

    Subcellular locationi

    Cytoplasmic vesicle 2 Publications
    Note: Localizes to the midbody of dividing cells.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. Flemming body Source: UniProtKB
    7. midbody Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasmic vesicle

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi323 – 3231L → D: Diminishes interaction with VPS4A. 2 Publications
    Mutagenesisi323 – 3231L → D: Greatly diminishes interaction with VPS4A; when associated with A-353. 2 Publications
    Mutagenesisi326 – 3261L → D: Diminishes interaction with VPS4A. 2 Publications
    Mutagenesisi326 – 3261L → D: Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with A-353. 2 Publications
    Mutagenesisi326 – 3261L → D: Greatly diminishes interaction with VPS4A; when associated with A-360. 2 Publications
    Mutagenesisi353 – 3531L → A: Diminishes interaction with VPS4A. 2 Publications
    Mutagenesisi353 – 3531L → A: Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with D-326. 2 Publications
    Mutagenesisi353 – 3531L → A: Greatly diminishes interaction with VPS4A; when associated with D-323. 2 Publications
    Mutagenesisi360 – 3612LK → AA: Abolishes interaction with VTA1, MITD1 and USP8; diminishes interaction with VPS4A. 2 Publications
    Mutagenesisi360 – 3601L → A: Diminishes interaction with VPS4A. 2 Publications
    Mutagenesisi360 – 3601L → A: Greatly diminishes interaction with VPS4A; when associated with D-326. 2 Publications

    Organism-specific databases

    PharmGKBiPA142671633.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 364364IST1 homologPRO_0000050727Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53990.
    PaxDbiP53990.
    PRIDEiP53990.

    PTM databases

    PhosphoSiteiP53990.

    Miscellaneous databases

    PMAP-CutDBP53990.

    Expressioni

    Gene expression databases

    ArrayExpressiP53990.
    BgeeiP53990.
    CleanExiHS_KIAA0174.
    GenevestigatoriP53990.

    Organism-specific databases

    HPAiHPA041802.
    HPA054532.

    Interactioni

    Subunit structurei

    Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts with SPAST, STAMBP, and USP8. May interact with VPS37B. May associate with the ESCRT-I complex. Interacts with MITD1, in competition with VSP4.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542532EBI-945994,EBI-930964
    CAPN7Q9Y6W36EBI-945994,EBI-1765641

    Protein-protein interaction databases

    BioGridi115141. 17 interactions.
    DIPiDIP-42546N.
    IntActiP53990. 6 interactions.
    MINTiMINT-1461091.
    STRINGi9606.ENSP00000330408.

    Structurei

    Secondary structure

    1
    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 4538
    Helixi49 – 8133
    Helixi83 – 875
    Helixi94 – 963
    Helixi97 – 11014
    Turni111 – 1133
    Helixi115 – 12814
    Helixi130 – 1378
    Turni138 – 1414
    Helixi146 – 1516
    Helixi159 – 17315
    Helixi181 – 1855

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FRRX-ray1.80A1-189[»]
    3FRSX-ray2.61A5-189[»]
    ProteinModelPortaliP53990.
    SMRiP53990. Positions 2-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53990.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 168168Interaction with CHMP1A and CHMP1BAdd
    BLAST
    Regioni64 – 279216Interaction with VPS37BAdd
    BLAST
    Regioni190 – 364175Interaction with VTA1Add
    BLAST
    Regioni348 – 36417Interaction with VPS4A, VTA1, MITD1 STAMBP and USP8Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi321 – 33212Type-2 MIT-interacting motifAdd
    BLAST
    Motifi351 – 36111MIT-interacting motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the IST1 family.Curated

    Phylogenomic databases

    eggNOGiNOG273475.
    HOGENOMiHOG000205346.
    InParanoidiP53990.
    OMAiPTYESID.
    PhylomeDBiP53990.
    TreeFamiTF314258.

    Family and domain databases

    InterProiIPR005061. DUF292_euk.
    [Graphical view]
    PfamiPF03398. Ist1. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P53990-1) [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

    MLGSGFKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE    50
    RARIRVEHII REDYLVEAME ILELYCDLLL ARFGLIQSMK ELDSGLAESV 100
    STLIWAAPRL QSEVAELKIV ADQLCAKYSK EYGKLCRTNQ IGTVNDRLMH 150
    KLSVEAPPKI LVERYLIEIA KNYNVPYEPD SVVMAEAPPG VETDLIDVGF 200
    TDDVKKGGPG RGGSGGFTAP VGGPDGTVPM PMPMPMPSAN TPFSYPLPKG 250
    PSDFNGLPMG TYQAFPNIHP PQIPATPPSY ESVDDINADK NISSAQIVGP 300
    GPKPEASAKL PSRPADNYDN FVLPELPSVP DTLPTASAGA STSASEDIDF 350
    DDLSRRFEEL KKKT 364
    Length:364
    Mass (Da):39,751
    Last modified:October 1, 1996 - v1
    Checksum:i0DD3C186A52A4380
    GO
    Isoform 2 (identifier: P53990-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         228-228: V → VPM
         252-282: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:335
    Mass (Da):36,622
    Checksum:i7D0714269380E835
    GO
    Isoform 5 (identifier: P53990-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVFKLKTKEEQHSM
         237-237: P → PMP

    Show »
    Length:379
    Mass (Da):41,566
    Checksum:i37E0FEF4BB93C054
    GO
    Isoform 4 (identifier: P53990-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         228-228: V → VPM

    Show »
    Length:366
    Mass (Da):39,979
    Checksum:iE25DE7D7A5693AF8
    GO
    Isoform 3 (identifier: P53990-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         228-228: V → VPM
         283-364: VDDINADKNI...RRFEELKKKT → MTLMLIRISL...LMIFPGGLKS

    Note: No experimental confirmation available.

    Show »
    Length:360
    Mass (Da):39,928
    Checksum:i5D0DDB4113DAA2BC
    GO
    Isoform 6 (identifier: P53990-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-148: Missing.
         228-228: V → VPM

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:218
    Mass (Da):23,089
    Checksum:iB0405956455B9777
    GO

    Sequence cautioni

    The sequence BAA11491.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 148148Missing in isoform 6. CuratedVSP_055118Add
    BLAST
    Alternative sequencei1 – 11M → MVFKLKTKEEQHSM in isoform 5. 1 PublicationVSP_047075
    Alternative sequencei228 – 2281V → VPM in isoform 2, isoform 3, isoform 4 and isoform 6. 2 PublicationsVSP_017118
    Alternative sequencei237 – 2371P → PMP in isoform 5. 1 PublicationVSP_047076
    Alternative sequencei252 – 28231Missing in isoform 2. 1 PublicationVSP_017119Add
    BLAST
    Alternative sequencei283 – 36482VDDIN…LKKKT → MTLMLIRISLLHRLLVLDPS QKPLQSFLPDLQITMTTLSY QSCHLCQTHYQLHLLVPAPQ HLKTLTLMIFPGGLKS in isoform 3. 1 PublicationVSP_017120Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB097052 mRNA. Translation: BAC77405.1.
    D79996 mRNA. Translation: BAA11491.2. Different initiation.
    AK057258 mRNA. Translation: BAG51894.1.
    AK293022 mRNA. Translation: BAF85711.1.
    AK293040 mRNA. Translation: BAF85729.1.
    AC009127 Genomic DNA. No translation available.
    AC010653 Genomic DNA. No translation available.
    BC000116 mRNA. Translation: AAH00116.1.
    BC000430 mRNA. Translation: AAH00430.1.
    BC004359 mRNA. Translation: AAH04359.1.
    BC103745 mRNA. Translation: AAI03746.1.
    CCDSiCCDS10905.1. [P53990-3]
    CCDS59271.1. [P53990-5]
    CCDS59272.1. [P53990-4]
    CCDS59273.1. [P53990-2]
    CCDS59274.1. [P53990-6]
    RefSeqiNP_001257904.1. NM_001270975.1. [P53990-4]
    NP_001257905.1. NM_001270976.1. [P53990-5]
    NP_001257906.1. NM_001270977.1. [P53990-2]
    NP_001257907.1. NM_001270978.1.
    NP_055576.2. NM_014761.3. [P53990-3]
    UniGeneiHs.232194.

    Genome annotation databases

    EnsembliENST00000329908; ENSP00000330408; ENSG00000182149. [P53990-3]
    ENST00000378798; ENSP00000368075; ENSG00000182149. [P53990-2]
    ENST00000378799; ENSP00000368076; ENSG00000182149. [P53990-4]
    ENST00000535424; ENSP00000438399; ENSG00000182149. [P53990-5]
    ENST00000538850; ENSP00000463711; ENSG00000182149. [P53990-6]
    ENST00000541571; ENSP00000455860; ENSG00000182149. [P53990-4]
    ENST00000544564; ENSP00000457844; ENSG00000182149. [P53990-4]
    ENST00000606369; ENSP00000475853; ENSG00000182149. [P53990-6]
    GeneIDi9798.
    KEGGihsa:9798.
    UCSCiuc002fbk.2. human. [P53990-3]
    uc002fbl.2. human. [P53990-2]
    uc002fbm.2. human. [P53990-4]
    uc010cgh.2. human.

    Polymorphism databases

    DMDMi1723119.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB097052 mRNA. Translation: BAC77405.1 .
    D79996 mRNA. Translation: BAA11491.2 . Different initiation.
    AK057258 mRNA. Translation: BAG51894.1 .
    AK293022 mRNA. Translation: BAF85711.1 .
    AK293040 mRNA. Translation: BAF85729.1 .
    AC009127 Genomic DNA. No translation available.
    AC010653 Genomic DNA. No translation available.
    BC000116 mRNA. Translation: AAH00116.1 .
    BC000430 mRNA. Translation: AAH00430.1 .
    BC004359 mRNA. Translation: AAH04359.1 .
    BC103745 mRNA. Translation: AAI03746.1 .
    CCDSi CCDS10905.1. [P53990-3 ]
    CCDS59271.1. [P53990-5 ]
    CCDS59272.1. [P53990-4 ]
    CCDS59273.1. [P53990-2 ]
    CCDS59274.1. [P53990-6 ]
    RefSeqi NP_001257904.1. NM_001270975.1. [P53990-4 ]
    NP_001257905.1. NM_001270976.1. [P53990-5 ]
    NP_001257906.1. NM_001270977.1. [P53990-2 ]
    NP_001257907.1. NM_001270978.1.
    NP_055576.2. NM_014761.3. [P53990-3 ]
    UniGenei Hs.232194.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FRR X-ray 1.80 A 1-189 [» ]
    3FRS X-ray 2.61 A 5-189 [» ]
    ProteinModelPortali P53990.
    SMRi P53990. Positions 2-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115141. 17 interactions.
    DIPi DIP-42546N.
    IntActi P53990. 6 interactions.
    MINTi MINT-1461091.
    STRINGi 9606.ENSP00000330408.

    PTM databases

    PhosphoSitei P53990.

    Polymorphism databases

    DMDMi 1723119.

    Proteomic databases

    MaxQBi P53990.
    PaxDbi P53990.
    PRIDEi P53990.

    Protocols and materials databases

    DNASUi 9798.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329908 ; ENSP00000330408 ; ENSG00000182149 . [P53990-3 ]
    ENST00000378798 ; ENSP00000368075 ; ENSG00000182149 . [P53990-2 ]
    ENST00000378799 ; ENSP00000368076 ; ENSG00000182149 . [P53990-4 ]
    ENST00000535424 ; ENSP00000438399 ; ENSG00000182149 . [P53990-5 ]
    ENST00000538850 ; ENSP00000463711 ; ENSG00000182149 . [P53990-6 ]
    ENST00000541571 ; ENSP00000455860 ; ENSG00000182149 . [P53990-4 ]
    ENST00000544564 ; ENSP00000457844 ; ENSG00000182149 . [P53990-4 ]
    ENST00000606369 ; ENSP00000475853 ; ENSG00000182149 . [P53990-6 ]
    GeneIDi 9798.
    KEGGi hsa:9798.
    UCSCi uc002fbk.2. human. [P53990-3 ]
    uc002fbl.2. human. [P53990-2 ]
    uc002fbm.2. human. [P53990-4 ]
    uc010cgh.2. human.

    Organism-specific databases

    CTDi 9798.
    GeneCardsi GC16P071930.
    HGNCi HGNC:28977. IST1.
    HPAi HPA041802.
    HPA054532.
    neXtProti NX_P53990.
    PharmGKBi PA142671633.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG273475.
    HOGENOMi HOG000205346.
    InParanoidi P53990.
    OMAi PTYESID.
    PhylomeDBi P53990.
    TreeFami TF314258.

    Miscellaneous databases

    ChiTaRSi IST1. human.
    EvolutionaryTracei P53990.
    GenomeRNAii 9798.
    NextBioi 35464749.
    PMAP-CutDB P53990.
    PROi P53990.

    Gene expression databases

    ArrayExpressi P53990.
    Bgeei P53990.
    CleanExi HS_KIAA0174.
    Genevestigatori P53990.

    Family and domain databases

    InterProi IPR005061. DUF292_euk.
    [Graphical view ]
    Pfami PF03398. Ist1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
      Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
      Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung fibroblast.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
      Tissue: Testis and Uterus.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
      Tissue: Eye and Lung.
    6. "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-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CHMP1A; CHMP1B; VPS4A; VTA1; MITD1; STAMBP; SPAST AND USP8, MUTAGENESIS OF 360-LEU-LYS-361.
    8. "Biochemical analyses of human IST1 and its function in cytokinesis."
      Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
      Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH VPS37B; VTA1; CHMP1A; CHMP1B; VPS4A AND VPS4B, INTERACTION WITH THE ESCRT-1 COMPLEX, MUTAGENESIS OF LEU-323; LEU-326; LEU-353 AND LEU-360.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "MITD1 is recruited to midbodies by ESCRT-III and participates in cytokinesis."
      Lee S., Chang J., Renvoise B., Tipirneni A., Yang S., Blackstone C.
      Mol. Biol. Cell 23:4347-4361(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MITD1.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIST1_HUMAN
    AccessioniPrimary (citable) accession number: P53990
    Secondary accession number(s): A8KAH5
    , J3QLU7, Q3SYM4, Q9BQ81, Q9BWN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3