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Q9BPW8

- NIPS1_HUMAN

UniProt

Q9BPW8 - NIPS1_HUMAN

Protein

Protein NipSnap homolog 1

Gene

NIPSNAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. neurotransmitter binding Source: Ensembl

    GO - Biological processi

    1. sensory perception of pain Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein NipSnap homolog 1
    Short name:
    NipSnap1
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7827. NIPSNAP1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrion Source: UniProtKB
    3. synaptic membrane Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31634.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284Protein NipSnap homolog 1PRO_0000221146Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651N6-acetyllysineBy similarity
    Modified residuei66 – 661N6-acetyllysineBy similarity
    Modified residuei73 – 731N6-acetyllysineBy similarity
    Modified residuei80 – 801N6-acetyllysineBy similarity
    Modified residuei143 – 1431N6-acetyllysineBy similarity
    Modified residuei146 – 1461N6-acetyllysine; alternate1 Publication
    Modified residuei146 – 1461N6-succinyllysine; alternateBy similarity
    Modified residuei191 – 1911N6-acetyllysineBy similarity
    Modified residuei193 – 1931N6-acetyllysine; alternateBy similarity
    Modified residuei193 – 1931N6-succinyllysine; alternateBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BPW8.
    PaxDbiQ9BPW8.
    PeptideAtlasiQ9BPW8.
    PRIDEiQ9BPW8.

    2D gel databases

    UCD-2DPAGEQ9BPW8.

    PTM databases

    PhosphoSiteiQ9BPW8.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest expression in liver.

    Gene expression databases

    ArrayExpressiQ9BPW8.
    BgeeiQ9BPW8.
    CleanExiHS_NIPSNAP1.
    GenevestigatoriQ9BPW8.

    Organism-specific databases

    HPAiHPA059227.

    Interactioni

    Protein-protein interaction databases

    BioGridi114080. 19 interactions.
    IntActiQ9BPW8. 17 interactions.
    MINTiMINT-1405060.
    STRINGi9606.ENSP00000216121.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BPW8.
    SMRiQ9BPW8. Positions 185-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NipSnap family.Curated

    Phylogenomic databases

    eggNOGiNOG09022.
    HOGENOMiHOG000194298.
    HOVERGENiHBG052627.
    InParanoidiQ9BPW8.
    OMAiAFSYWPQ.
    OrthoDBiEOG769ZM2.
    PhylomeDBiQ9BPW8.
    TreeFamiTF314501.

    Family and domain databases

    InterProiIPR011008. Dimeric_a/b-barrel.
    IPR012577. NIPSNAP.
    [Graphical view]
    PfamiPF07978. NIPSNAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF54909. SSF54909. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9BPW8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPRLCSISV TARRLLGGPG PRAGDVASAA AARFYSKDNE GSWFRSLFVH    50
    KVDPRKDAHS TLLSKKETSN LYKIQFHNVK PEYLDAYNSL TEAVLPKLHL 100
    DEDYPCSLVG NWNTWYGEQD QAVHLWRFSG GYPALMDCMN KLKNNKEYLE 150
    FRRERSQMLL SRRNQLLLEF SFWNEPQPRM GPNIYELRTY KLKPGTMIEW 200
    GNNWARAIKY RQENQEAVGG FFSQIGELYV VHHLWAYKDL QSREETRNAA 250
    WRKRGWDENV YYTVPLVRHM ESRIMIPLKI SPLQ 284
    Length:284
    Mass (Da):33,310
    Last modified:June 1, 2001 - v1
    Checksum:iE0B3E60082C2CACA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti156 – 1561S → T in CAA04632. (PubMed:9661659)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti245 – 2451E → K.
    Corresponds to variant rs1058646 [ dbSNP | Ensembl ].
    VAR_011630

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001258 mRNA. Translation: CAA04632.1.
    AK314407 mRNA. Translation: BAG37030.1.
    CH471095 Genomic DNA. Translation: EAW59813.1.
    BC006473 mRNA. Translation: AAH06473.1.
    BC002371 mRNA. Translation: AAH02371.1.
    CCDSiCCDS13860.1.
    RefSeqiNP_001189431.1. NM_001202502.1.
    NP_003625.2. NM_003634.3.
    UniGeneiHs.173878.

    Genome annotation databases

    EnsembliENST00000216121; ENSP00000216121; ENSG00000184117.
    GeneIDi8508.
    KEGGihsa:8508.
    UCSCiuc003afx.4. human.

    Polymorphism databases

    DMDMi17380144.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001258 mRNA. Translation: CAA04632.1 .
    AK314407 mRNA. Translation: BAG37030.1 .
    CH471095 Genomic DNA. Translation: EAW59813.1 .
    BC006473 mRNA. Translation: AAH06473.1 .
    BC002371 mRNA. Translation: AAH02371.1 .
    CCDSi CCDS13860.1.
    RefSeqi NP_001189431.1. NM_001202502.1.
    NP_003625.2. NM_003634.3.
    UniGenei Hs.173878.

    3D structure databases

    ProteinModelPortali Q9BPW8.
    SMRi Q9BPW8. Positions 185-283.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114080. 19 interactions.
    IntActi Q9BPW8. 17 interactions.
    MINTi MINT-1405060.
    STRINGi 9606.ENSP00000216121.

    PTM databases

    PhosphoSitei Q9BPW8.

    Polymorphism databases

    DMDMi 17380144.

    2D gel databases

    UCD-2DPAGE Q9BPW8.

    Proteomic databases

    MaxQBi Q9BPW8.
    PaxDbi Q9BPW8.
    PeptideAtlasi Q9BPW8.
    PRIDEi Q9BPW8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216121 ; ENSP00000216121 ; ENSG00000184117 .
    GeneIDi 8508.
    KEGGi hsa:8508.
    UCSCi uc003afx.4. human.

    Organism-specific databases

    CTDi 8508.
    GeneCardsi GC22M029952.
    HGNCi HGNC:7827. NIPSNAP1.
    HPAi HPA059227.
    MIMi 603249. gene.
    neXtProti NX_Q9BPW8.
    PharmGKBi PA31634.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG09022.
    HOGENOMi HOG000194298.
    HOVERGENi HBG052627.
    InParanoidi Q9BPW8.
    OMAi AFSYWPQ.
    OrthoDBi EOG769ZM2.
    PhylomeDBi Q9BPW8.
    TreeFami TF314501.

    Miscellaneous databases

    ChiTaRSi NIPSNAP1. human.
    GenomeRNAii 8508.
    NextBioi 31843.
    PROi Q9BPW8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BPW8.
    Bgeei Q9BPW8.
    CleanExi HS_NIPSNAP1.
    Genevestigatori Q9BPW8.

    Family and domain databases

    InterProi IPR011008. Dimeric_a/b-barrel.
    IPR012577. NIPSNAP.
    [Graphical view ]
    Pfami PF07978. NIPSNAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54909. SSF54909. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the human NIPSNAP1 gene from 22q12: a member of a novel gene family."
      Seroussi E., Pan H.Q., Kedra D., Roe B.A., Dumanski J.P.
      Gene 212:13-20(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Colon.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Lung.
    5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNIPS1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BPW8
    Secondary accession number(s): B2RAY3, O43800
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 116 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 22
      Human chromosome 22: 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