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Q9NRL3

- STRN4_HUMAN

UniProt

Q9NRL3 - STRN4_HUMAN

Protein

Striatin-4

Gene

STRN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      Previous versions | rss
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    Functioni

    Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein.

    GO - Molecular functioni

    1. armadillo repeat domain binding Source: UniProtKB
    2. calmodulin binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein complex binding Source: UniProtKB
    5. protein phosphatase 2A binding Source: UniProtKB

    Keywords - Ligandi

    Calmodulin-binding

    Enzyme and pathway databases

    SignaLinkiF8VYA6.
    Q9NRL3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Striatin-4
    Alternative name(s):
    Zinedin
    Gene namesi
    Name:STRN4
    Synonyms:ZIN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:15721. STRN4.

    Subcellular locationi

    Cytoplasm By similarity. Membrane By similarity; Peripheral membrane protein By similarity. Cell projectiondendritic spine By similarity
    Note: CTTNBP2-binding may regulate dendritic spine distribution.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. dendritic spine Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134863218.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 753753Striatin-4PRO_0000051239Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531Phosphoserine2 Publications
    Modified residuei206 – 2061Phosphoserine2 Publications
    Modified residuei276 – 2761Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRL3.
    PaxDbiQ9NRL3.
    PRIDEiQ9NRL3.

    PTM databases

    PhosphoSiteiQ9NRL3.

    Miscellaneous databases

    PMAP-CutDBQ9NRL3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NRL3.
    BgeeiQ9NRL3.
    CleanExiHS_STRN4.
    GenevestigatoriQ9NRL3.

    Organism-specific databases

    HPAiHPA043527.
    HPA056706.

    Interactioni

    Subunit structurei

    Interacts with CTTNBP2; this interaction may regulate dendritic spine distribution of STRN4. Activation of glutamate receptors weakens the interaction with CTTNBP2 By similarity. Interacts with CTTNBP2NL.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    JUNP054123EBI-717245,EBI-852823

    Protein-protein interaction databases

    BioGridi118941. 50 interactions.
    IntActiQ9NRL3. 54 interactions.
    MINTiMINT-1371553.
    STRINGi9606.ENSP00000375777.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRL3.
    SMRiQ9NRL3. Positions 86-130, 409-752.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati436 – 47540WD 1Add
    BLAST
    Repeati489 – 52840WD 2Add
    BLAST
    Repeati542 – 58140WD 3Add
    BLAST
    Repeati587 – 62842WD 4Add
    BLAST
    Repeati635 – 67440WD 5Add
    BLAST
    Repeati677 – 71640WD 6Add
    BLAST
    Repeati723 – 75230WD 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni71 – 799Caveolin-bindingSequence Analysis
    Regioni165 – 18218Calmodulin-bindingSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili69 – 13668Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 149Poly-Ala

    Sequence similaritiesi

    Belongs to the WD repeat striatin family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000236343.
    HOVERGENiHBG007117.
    KOiK17608.
    OMAiYDNYDPG.
    OrthoDBiEOG79KPDR.
    PhylomeDBiQ9NRL3.
    TreeFamiTF313387.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR013258. Striatin_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF08232. Striatin. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRL3-1) [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

    MMEERAAAAV AAAASSCRPL GSGAGPGPTG AAPVSAPAPG PGPAGKGGGG    50
    GGSPGPTAGP EPLSLPGILH FIQHEWARFE AEKARWEAER AELQAQVAFL 100
    QGERKGQENL KTDLVRRIKM LEYALKQERA KYHKLKFGTD LNQGEKKADV 150
    SEQVSNGPVE SVTLENSPLV WKEGRQLLRQ YLEEVGYTDT ILDMRSKRVR 200
    SLLGRSLELN GAVEPSEGAP RAPPGPAGLS GGESLLVKQI EEQIKRNAAG 250
    KDGKERLGGS VLGQIPFLQN CEDEDSDEDD ELDSVQHKKQ RVKLPSKALV 300
    PEMEDEDEED DSEDAINEFD FLGSGEDGEG APDPRRCTVD GSPHELESRR 350
    VKLQGILADL RDVDGLPPKV TGPPPGTPQP RPHEDVFIMD TIGGGEVSLG 400
    DLADLTVTND NDLSCDLSDS KDAFKKTWNP KFTLRSHYDG IRSLAFHHSQ 450
    SALLTASEDG TLKLWNLQKA VTAKKNAALD VEPIHAFRAH RGPVLAVAMG 500
    SNSEYCYSGG ADACIHSWKI PDLSMDPYDG YDPSVLSHVL EGHGDAVWGL 550
    AFSPTSQRLA SCSADGTVRI WDPSSSSPAC LCTFPTASEH GVPTSVAFTS 600
    TEPAHIVASF RSGDTVLYDM EVGSALLTLE SRGSSGPTQI NQVVSHPNQP 650
    LTITAHDDRG IRFLDNRTGK PVHSMVAHLD AVTCLAVDPN GAFLMSGSHD 700
    CSLRLWSLDN KTCVQEITAH RKKHEEAIHA VACHPSKALI ASAGADALAK 750
    VFV 753
    Length:753
    Mass (Da):80,596
    Last modified:July 10, 2007 - v2
    Checksum:i339AC24E26A9CD54
    GO
    Isoform 2 (identifier: Q9NRL3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-119: Missing.
         347-376: ESRRVKLQGILADLRDVDGLPPKVTGPPPG → GPELHSPTEWQGALSVGKASPMPDWVGTAG
         377-753: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:257
    Mass (Da):28,106
    Checksum:iA3898671C11A1A4C
    GO
    Isoform 3 (identifier: Q9NRL3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         384-384: E → EGSFGFSS

    Show »
    Length:760
    Mass (Da):81,266
    Checksum:i653E59DBCD215E42
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti356 – 3561I → V in AAF29527. (PubMed:10748158)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti568 – 5681V → I.
    Corresponds to variant rs10409124 [ dbSNP | Ensembl ].
    VAR_053419

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 119119Missing in isoform 2. 1 PublicationVSP_056170Add
    BLAST
    Alternative sequencei347 – 37630ESRRV…GPPPG → GPELHSPTEWQGALSVGKAS PMPDWVGTAG in isoform 2. 1 PublicationVSP_056171Add
    BLAST
    Alternative sequencei377 – 753377Missing in isoform 2. 1 PublicationVSP_056172Add
    BLAST
    Alternative sequencei384 – 3841E → EGSFGFSS in isoform 3. CuratedVSP_056738

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF212940 mRNA. Translation: AAF29527.1.
    AK298804 mRNA. Translation: BAG60939.1.
    AC008622 Genomic DNA. No translation available.
    AC008635 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57442.1.
    CH471126 Genomic DNA. Translation: EAW57443.1.
    BC004910 mRNA. Translation: AAH04910.2.
    BC034604 mRNA. Translation: AAH34604.1.
    CCDSiCCDS12690.1.
    RefSeqiNP_001034966.1. NM_001039877.1.
    NP_037535.2. NM_013403.2.
    UniGeneiHs.631590.

    Genome annotation databases

    EnsembliENST00000263280; ENSP00000263280; ENSG00000090372.
    ENST00000391910; ENSP00000375777; ENSG00000090372.
    ENST00000435164; ENSP00000473607; ENSG00000090372.
    GeneIDi29888.
    KEGGihsa:29888.
    UCSCiuc002pfl.3. human.
    uc002pfm.3. human.

    Polymorphism databases

    DMDMi152031693.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF212940 mRNA. Translation: AAF29527.1 .
    AK298804 mRNA. Translation: BAG60939.1 .
    AC008622 Genomic DNA. No translation available.
    AC008635 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57442.1 .
    CH471126 Genomic DNA. Translation: EAW57443.1 .
    BC004910 mRNA. Translation: AAH04910.2 .
    BC034604 mRNA. Translation: AAH34604.1 .
    CCDSi CCDS12690.1.
    RefSeqi NP_001034966.1. NM_001039877.1.
    NP_037535.2. NM_013403.2.
    UniGenei Hs.631590.

    3D structure databases

    ProteinModelPortali Q9NRL3.
    SMRi Q9NRL3. Positions 86-130, 409-752.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118941. 50 interactions.
    IntActi Q9NRL3. 54 interactions.
    MINTi MINT-1371553.
    STRINGi 9606.ENSP00000375777.

    PTM databases

    PhosphoSitei Q9NRL3.

    Polymorphism databases

    DMDMi 152031693.

    Proteomic databases

    MaxQBi Q9NRL3.
    PaxDbi Q9NRL3.
    PRIDEi Q9NRL3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263280 ; ENSP00000263280 ; ENSG00000090372 .
    ENST00000391910 ; ENSP00000375777 ; ENSG00000090372 .
    ENST00000435164 ; ENSP00000473607 ; ENSG00000090372 .
    GeneIDi 29888.
    KEGGi hsa:29888.
    UCSCi uc002pfl.3. human.
    uc002pfm.3. human.

    Organism-specific databases

    CTDi 29888.
    GeneCardsi GC19M047222.
    H-InvDB HIX0096898.
    HGNCi HGNC:15721. STRN4.
    HPAi HPA043527.
    HPA056706.
    MIMi 614767. gene.
    neXtProti NX_Q9NRL3.
    PharmGKBi PA134863218.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000236343.
    HOVERGENi HBG007117.
    KOi K17608.
    OMAi YDNYDPG.
    OrthoDBi EOG79KPDR.
    PhylomeDBi Q9NRL3.
    TreeFami TF313387.

    Enzyme and pathway databases

    SignaLinki F8VYA6.
    Q9NRL3.

    Miscellaneous databases

    ChiTaRSi STRN4. human.
    GeneWikii STRN4.
    GenomeRNAii 29888.
    NextBioi 52431.
    PMAP-CutDB Q9NRL3.
    PROi Q9NRL3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRL3.
    Bgeei Q9NRL3.
    CleanExi HS_STRN4.
    Genevestigatori Q9NRL3.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR013258. Striatin_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF08232. Striatin. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain."
      Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G., Monneron A.
      J. Biol. Chem. 275:19970-19977(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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 2).
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 1).
      Tissue: Muscle and Testis.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
      Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
      Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTTNBP2NL.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTRN4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRL3
    Secondary accession number(s): A0A024R0V2
    , B4DQH7, F8VYA6, Q8NE53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 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

    The name 'Zinedin' probably originates from the name of the famous soccer player from Marseille (Zinedine Zidane).

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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