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Q6NUQ1

- RINT1_HUMAN

UniProt

Q6NUQ1 - RINT1_HUMAN

Protein

RAD50-interacting protein 1

Gene

RINT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum. May play a role in cell cycle checkpoint control. Essential for telomere length control.3 Publications

    GO - Molecular functioni

    1. protein binding Source: HGNC

    GO - Biological processi

    1. G2 DNA damage checkpoint Source: HGNC
    2. protein transport Source: UniProtKB-KW
    3. vesicle-mediated transport Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, ER-Golgi transport, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RAD50-interacting protein 1
    Alternative name(s):
    RAD50 interactor 1
    Short name:
    HsRINT-1
    Short name:
    RINT-1
    Gene namesi
    Name:RINT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:21876. RINT1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HGNC
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485595.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 792792RAD50-interacting protein 1PRO_0000097349Add
    BLAST

    Proteomic databases

    MaxQBiQ6NUQ1.
    PaxDbiQ6NUQ1.
    PRIDEiQ6NUQ1.

    PTM databases

    PhosphoSiteiQ6NUQ1.

    Expressioni

    Developmental stagei

    Expressed throughout the cell cycle.1 Publication

    Gene expression databases

    ArrayExpressiQ6NUQ1.
    BgeeiQ6NUQ1.
    CleanExiHS_RINT1.
    GenevestigatoriQ6NUQ1.

    Organism-specific databases

    HPAiHPA019875.
    HPA031646.

    Interactioni

    Subunit structurei

    Associated with a SNARE complex consisting of STX18, USE1L, BNIP1/SEC20L, and SEC22B. Interacts directly with BNIP1/SEC20L and ZW10. Interacts with RAD50 during late S and G2/M phases. Interacts with RBL2, preferentially with the active, hypophosphorylated form.4 Publications

    Protein-protein interaction databases

    BioGridi121942. 10 interactions.
    DIPiDIP-36477N.
    IntActiQ6NUQ1. 8 interactions.
    MINTiMINT-1393029.
    STRINGi9606.ENSP00000257700.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NUQ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini220 – 792573RINT1/TIP20PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili103 – 12422Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RINT1 family.Curated
    Contains 1 RINT1/TIP20 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG244420.
    HOGENOMiHOG000118368.
    HOVERGENiHBG057727.
    InParanoidiQ6NUQ1.
    OMAiQESSCSH.
    OrthoDBiEOG70GMFF.
    PhylomeDBiQ6NUQ1.
    TreeFamiTF324274.

    Family and domain databases

    InterProiIPR007528. RINT1_TIP1.
    [Graphical view]
    PfamiPF04437. RINT1_TIP1. 1 hit.
    [Graphical view]
    PROSITEiPS51386. RINT1_TIP20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6NUQ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPAGEIGAS PAAPCCSESG DERKNLEEKS DINVTVLIGS KQVSEGTDNG    50
    DLPSYVSAFI EKEVGNDLKS LKKLDKLIEQ RTVSKMQLEE QVLTISSEIP 100
    KRIRSALKNA EESKQFLNQF LEQETHLFSA INSHLLTAQP WMDDLGTMIS 150
    QIEEIERHLA YLKWISQIEE LSDNIQQYLM TNNVPEAAST LVSMAELDIK 200
    LQESSCTHLL GFMRATVKFW HKILKDKLTS DFEEILAQLH WPFIAPPQSQ 250
    TVGLSRPASA PEIYSYLETL FCQLLKLQTS DELLTEPKQL PEKYSLPASP 300
    SVILPIQVML TPLQKRFRYH FRGNRQTNVL SKPEWYLAQV LMWIGNHTEF 350
    LDEKIQPILD KVGSLVNARL EFSRGLMMLV LEKLATDIPC LLYDDNLFCH 400
    LVDEVLLFER ELHSVHGYPG TFASCMHILS EETCFQRWLT VERKFALQKM 450
    DSMLSSEAAW VSQYKDITDV DEMKVPDCAE TFMTLLLVIT DRYKNLPTAS 500
    RKLQFLELQK DLVDDFRIRL TQVMKEETRA SLGFRYCAIL NAVNYISTVL 550
    ADWADNVFFL QLQQAALEVF AENNTLSKLQ LGQLASMESS VFDDMINLLE 600
    RLKHDMLTRQ VDHVFREVKD AAKLYKKERW LSLPSQSEQA VMSLSSSACP 650
    LLLTLRDHLL QLEQQLCFSL FKIFWQMLVE KLDVYIYQEI ILANHFNEGG 700
    AAQLQFDMTR NLFPLFSHYC KRPENYFKHI KEACIVLNLN VGSALLLKDV 750
    LQSASGQLPA TAALNEVGIY KLAQQDVEIL LNLRTNWPNT GK 792
    Length:792
    Mass (Da):90,632
    Last modified:July 5, 2004 - v1
    Checksum:i6671066FCC5E74D6
    GO

    Sequence cautioni

    The sequence AAG42101.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB13910.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAQ96849.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAQ96850.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti758 – 7581L → P(PubMed:14702039)Curated
    Sequence conflicti759 – 7602PA → ST in AAG42101. (PubMed:11096100)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401S → C.
    Corresponds to variant rs11556986 [ dbSNP | Ensembl ].
    VAR_051322
    Natural varianti668 – 6681F → S.
    Corresponds to variant rs35971380 [ dbSNP | Ensembl ].
    VAR_034418
    Natural varianti759 – 7591P → L.
    Corresponds to variant rs34310648 [ dbSNP | Ensembl ].
    VAR_034419

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF317622 mRNA. Translation: AAG42101.1. Different initiation.
    AC073073 Genomic DNA. Translation: AAQ96849.1. Sequence problems.
    AC073073 Genomic DNA. Translation: AAQ96850.1. Sequence problems.
    BC007120 mRNA. Translation: AAH07120.2.
    BC068483 mRNA. Translation: AAH68483.1.
    AK021847 mRNA. Translation: BAB13910.1. Different initiation.
    CCDSiCCDS34726.1.
    RefSeqiNP_068749.3. NM_021930.4.
    UniGeneiHs.531388.

    Genome annotation databases

    EnsembliENST00000257700; ENSP00000257700; ENSG00000135249.
    GeneIDi60561.
    KEGGihsa:60561.
    UCSCiuc003vda.1. human.

    Polymorphism databases

    DMDMi71152944.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF317622 mRNA. Translation: AAG42101.1 . Different initiation.
    AC073073 Genomic DNA. Translation: AAQ96849.1 . Sequence problems.
    AC073073 Genomic DNA. Translation: AAQ96850.1 . Sequence problems.
    BC007120 mRNA. Translation: AAH07120.2 .
    BC068483 mRNA. Translation: AAH68483.1 .
    AK021847 mRNA. Translation: BAB13910.1 . Different initiation.
    CCDSi CCDS34726.1.
    RefSeqi NP_068749.3. NM_021930.4.
    UniGenei Hs.531388.

    3D structure databases

    ProteinModelPortali Q6NUQ1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121942. 10 interactions.
    DIPi DIP-36477N.
    IntActi Q6NUQ1. 8 interactions.
    MINTi MINT-1393029.
    STRINGi 9606.ENSP00000257700.

    PTM databases

    PhosphoSitei Q6NUQ1.

    Polymorphism databases

    DMDMi 71152944.

    Proteomic databases

    MaxQBi Q6NUQ1.
    PaxDbi Q6NUQ1.
    PRIDEi Q6NUQ1.

    Protocols and materials databases

    DNASUi 60561.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257700 ; ENSP00000257700 ; ENSG00000135249 .
    GeneIDi 60561.
    KEGGi hsa:60561.
    UCSCi uc003vda.1. human.

    Organism-specific databases

    CTDi 60561.
    GeneCardsi GC07P105172.
    H-InvDB HIX0033650.
    HGNCi HGNC:21876. RINT1.
    HPAi HPA019875.
    HPA031646.
    MIMi 610089. gene.
    neXtProti NX_Q6NUQ1.
    PharmGKBi PA143485595.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244420.
    HOGENOMi HOG000118368.
    HOVERGENi HBG057727.
    InParanoidi Q6NUQ1.
    OMAi QESSCSH.
    OrthoDBi EOG70GMFF.
    PhylomeDBi Q6NUQ1.
    TreeFami TF324274.

    Miscellaneous databases

    GeneWikii RINT1.
    GenomeRNAii 60561.
    NextBioi 65449.
    PROi Q6NUQ1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6NUQ1.
    Bgeei Q6NUQ1.
    CleanExi HS_RINT1.
    Genevestigatori Q6NUQ1.

    Family and domain databases

    InterProi IPR007528. RINT1_TIP1.
    [Graphical view ]
    Pfami PF04437. RINT1_TIP1. 1 hit.
    [Graphical view ]
    PROSITEi PS51386. RINT1_TIP20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G2/M checkpoint control."
      Xiao J., Liu C.-C., Chen P.-L., Lee W.-H.
      J. Biol. Chem. 276:6105-6111(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH RAD50.
      Tissue: B-cell.
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Brain and Testis.
    4. "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 367-792.
      Tissue: Embryo.
    5. "Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi."
      Hirose H., Arasaki K., Dohmae N., Takio K., Hatsuzawa K., Nagahama M., Tani K., Yamamoto A., Tohyama M., Tagaya M.
      EMBO J. 23:1267-1278(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH SEC22B; STX18; USE1L AND ZW10.
    6. "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion."
      Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K., Nagahama M., Tani K., Yamamoto A., Tagaya M.
      EMBO J. 23:3216-3226(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BNIP1.
    7. "The Rb-related p130 protein controls telomere lengthening through an interaction with a Rad50-interacting protein, RINT-1."
      Kong L.-J., Meloni A.R., Nevins J.R.
      Mol. Cell 22:63-71(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RBL2.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRINT1_HUMAN
    AccessioniPrimary (citable) accession number: Q6NUQ1
    Secondary accession number(s): Q75MG9
    , Q75MH0, Q96IW8, Q9H229, Q9HAD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 92 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

    Miscellaneous

    According to PubMed:11096100, a longer form, which may be due to the differential initiation of translation using a non-AUG codon, may exist. However, the existence of such form has not been clearly demonstrated.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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