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P31948

- STIP1_HUMAN

UniProt

P31948 - STIP1_HUMAN

Protein

Stress-induced-phosphoprotein 1

Gene

STIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. response to stress Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stress-induced-phosphoprotein 1
    Short name:
    STI1
    Alternative name(s):
    Hsc70/Hsp90-organizing protein
    Short name:
    Hop
    Renal carcinoma antigen NY-REN-11
    Transformation-sensitive protein IEF SSP 3521
    Gene namesi
    Name:STIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:11387. STIP1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. Golgi apparatus Source: ProtInc
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36196.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 543543Stress-induced-phosphoprotein 1PRO_0000106372Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei8 – 81N6-acetyllysine1 Publication
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei301 – 3011N6-acetyllysine1 Publication
    Modified residuei312 – 3121N6-acetyllysine1 Publication
    Modified residuei325 – 3251N6-acetyllysine1 Publication
    Modified residuei344 – 3441N6-acetyllysine1 Publication
    Modified residuei354 – 3541Phosphotyrosine1 Publication
    Modified residuei446 – 4461N6-acetyllysine1 Publication
    Modified residuei481 – 4811Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP31948.
    PaxDbiP31948.
    PRIDEiP31948.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00013894.
    UCD-2DPAGEP31948.

    PTM databases

    PhosphoSiteiP31948.

    Expressioni

    Gene expression databases

    ArrayExpressiP31948.
    BgeeiP31948.
    CleanExiHS_STIP1.
    GenevestigatoriP31948.

    Organism-specific databases

    HPAiCAB017448.
    HPA039291.
    HPA044062.

    Interactioni

    Subunit structurei

    Forms a complex with HSC70 and HSPCA/HSP-86 and HSPCB/HSP-84. Interacts with PACRG. Interacts with METTL21B. Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCDC117Q8IWD42EBI-1054052,EBI-3387963
    CDC37L1Q7L3B62EBI-1054052,EBI-2841876
    EGFRP005332EBI-1054052,EBI-297353

    Protein-protein interaction databases

    BioGridi116162. 58 interactions.
    DIPiDIP-41085N.
    IntActiP31948. 77 interactions.
    MINTiMINT-132047.
    STRINGi9606.ENSP00000305958.

    Structurei

    Secondary structure

    1
    543
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi20 – 3314
    Helixi38 – 5114
    Helixi54 – 6714
    Helixi72 – 8413
    Helixi88 – 9912
    Helixi106 – 11712
    Helixi223 – 23715
    Helixi241 – 25414
    Helixi259 – 27214
    Helixi275 – 29117
    Helixi296 – 31217
    Helixi316 – 32914
    Helixi333 – 34816
    Helixi359 – 37214
    Helixi377 – 38711
    Helixi394 – 40411
    Turni405 – 4084
    Helixi410 – 42314
    Helixi428 – 44013
    Helixi444 – 45714
    Helixi459 – 4624
    Helixi463 – 47513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ELRX-ray1.90A223-352[»]
    1ELWX-ray1.60A/B1-118[»]
    2LNINMR-A356-477[»]
    3ESKX-ray2.05A223-350[»]
    3FWVX-ray2.20A/B223-349[»]
    ProteinModelPortaliP31948.
    SMRiP31948. Positions 2-118, 218-477, 479-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31948.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati4 – 3734TPR 1Add
    BLAST
    Repeati38 – 7134TPR 2Add
    BLAST
    Repeati72 – 10534TPR 3Add
    BLAST
    Domaini130 – 16940STI1 1Add
    BLAST
    Repeati225 – 25834TPR 4Add
    BLAST
    Repeati259 – 29234TPR 5Add
    BLAST
    Repeati300 – 33334TPR 6Add
    BLAST
    Repeati360 – 39334TPR 7Add
    BLAST
    Repeati394 – 42734TPR 8Add
    BLAST
    Repeati428 – 46134TPR 9Add
    BLAST
    Domaini492 – 53140STI1 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi222 – 23918Bipartite nuclear localization signalSequence AnalysisAdd
    BLAST

    Domaini

    The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90.

    Sequence similaritiesi

    Contains 2 STI1 domains.Curated
    Contains 9 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000186562.
    HOVERGENiHBG057820.
    KOiK09553.
    OMAiCEKAIDV.
    OrthoDBiEOG7BGHM5.
    PhylomeDBiP31948.
    TreeFamiTF300478.

    Family and domain databases

    Gene3Di1.25.40.10. 3 hits.
    InterProiIPR006636. STI1_HS-bd.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 8 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view]
    SMARTiSM00727. STI1. 2 hits.
    SM00028. TPR. 9 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 9 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P31948-1) [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

    MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK    50
    KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK 100
    HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP 150
    TYRELIEQLR NKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP 200
    PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDK 250
    AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA 300
    KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE 350
    RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR 400
    AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV 450
    YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS 500
    DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR 543
    Length:543
    Mass (Da):62,639
    Last modified:July 1, 1993 - v1
    Checksum:i8E58ECA13825CB0E
    GO
    Isoform 2 (identifier: P31948-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MEQ → MESGSPMGEVEISRTIRTNGRGQRGYDWQCKRPIRVAEVRSSLHSWSLRW

    Show »
    Length:590
    Mass (Da):68,080
    Checksum:i76F4C7A16BFCBCA0
    GO
    Isoform 3 (identifier: P31948-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-97: Missing.

    Show »
    Length:519
    Mass (Da):59,778
    Checksum:i0D7C993B4B4E230E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841F → L in AAH39299. (PubMed:15489334)Curated
    Sequence conflicti364 – 3641K → E in BAG59782. (PubMed:14702039)Curated
    Sequence conflicti533 – 5331K → R in BAG59782. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 33MEQ → MESGSPMGEVEISRTIRTNG RGQRGYDWQCKRPIRVAEVR SSLHSWSLRW in isoform 2. 1 PublicationVSP_055034
    Alternative sequencei74 – 9724Missing in isoform 3. 1 PublicationVSP_055035Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86752 mRNA. Translation: AAA58682.1.
    BT020010 mRNA. Translation: AAV38813.1.
    BT020011 mRNA. Translation: AAV38814.1.
    CR536512 mRNA. Translation: CAG38750.1.
    AK297319 mRNA. Translation: BAG59782.1.
    AP005668 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74196.1.
    CH471076 Genomic DNA. Translation: EAW74197.1.
    BC002987 mRNA. Translation: AAH02987.1.
    BC039299 mRNA. Translation: AAH39299.1.
    CCDSiCCDS60827.1. [P31948-2]
    CCDS60828.1. [P31948-3]
    CCDS8058.1. [P31948-1]
    PIRiA38093.
    RefSeqiNP_001269581.1. NM_001282652.1.
    NP_001269582.1. NM_001282653.1.
    NP_006810.1. NM_006819.2.
    UniGeneiHs.337295.

    Genome annotation databases

    EnsembliENST00000305218; ENSP00000305958; ENSG00000168439. [P31948-1]
    ENST00000358794; ENSP00000351646; ENSG00000168439. [P31948-2]
    ENST00000538945; ENSP00000445957; ENSG00000168439. [P31948-3]
    GeneIDi10963.
    KEGGihsa:10963.
    UCSCiuc001nyk.1. human. [P31948-1]

    Polymorphism databases

    DMDMi400042.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86752 mRNA. Translation: AAA58682.1 .
    BT020010 mRNA. Translation: AAV38813.1 .
    BT020011 mRNA. Translation: AAV38814.1 .
    CR536512 mRNA. Translation: CAG38750.1 .
    AK297319 mRNA. Translation: BAG59782.1 .
    AP005668 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74196.1 .
    CH471076 Genomic DNA. Translation: EAW74197.1 .
    BC002987 mRNA. Translation: AAH02987.1 .
    BC039299 mRNA. Translation: AAH39299.1 .
    CCDSi CCDS60827.1. [P31948-2 ]
    CCDS60828.1. [P31948-3 ]
    CCDS8058.1. [P31948-1 ]
    PIRi A38093.
    RefSeqi NP_001269581.1. NM_001282652.1.
    NP_001269582.1. NM_001282653.1.
    NP_006810.1. NM_006819.2.
    UniGenei Hs.337295.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ELR X-ray 1.90 A 223-352 [» ]
    1ELW X-ray 1.60 A/B 1-118 [» ]
    2LNI NMR - A 356-477 [» ]
    3ESK X-ray 2.05 A 223-350 [» ]
    3FWV X-ray 2.20 A/B 223-349 [» ]
    ProteinModelPortali P31948.
    SMRi P31948. Positions 2-118, 218-477, 479-540.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116162. 58 interactions.
    DIPi DIP-41085N.
    IntActi P31948. 77 interactions.
    MINTi MINT-132047.
    STRINGi 9606.ENSP00000305958.

    PTM databases

    PhosphoSitei P31948.

    Polymorphism databases

    DMDMi 400042.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00013894.
    UCD-2DPAGE P31948.

    Proteomic databases

    MaxQBi P31948.
    PaxDbi P31948.
    PRIDEi P31948.

    Protocols and materials databases

    DNASUi 10963.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305218 ; ENSP00000305958 ; ENSG00000168439 . [P31948-1 ]
    ENST00000358794 ; ENSP00000351646 ; ENSG00000168439 . [P31948-2 ]
    ENST00000538945 ; ENSP00000445957 ; ENSG00000168439 . [P31948-3 ]
    GeneIDi 10963.
    KEGGi hsa:10963.
    UCSCi uc001nyk.1. human. [P31948-1 ]

    Organism-specific databases

    CTDi 10963.
    GeneCardsi GC11P063953.
    HGNCi HGNC:11387. STIP1.
    HPAi CAB017448.
    HPA039291.
    HPA044062.
    MIMi 605063. gene.
    neXtProti NX_P31948.
    PharmGKBi PA36196.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000186562.
    HOVERGENi HBG057820.
    KOi K09553.
    OMAi CEKAIDV.
    OrthoDBi EOG7BGHM5.
    PhylomeDBi P31948.
    TreeFami TF300478.

    Miscellaneous databases

    ChiTaRSi STIP1. human.
    EvolutionaryTracei P31948.
    GeneWikii Hop_(protein).
    GenomeRNAii 10963.
    NextBioi 35473239.
    PROi P31948.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31948.
    Bgeei P31948.
    CleanExi HS_STIP1.
    Genevestigatori P31948.

    Family and domain databases

    Gene3Di 1.25.40.10. 3 hits.
    InterProi IPR006636. STI1_HS-bd.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 8 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view ]
    SMARTi SM00727. STI1. 2 hits.
    SM00028. TPR. 9 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 9 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1."
      Honore B., Leffers H., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.
      J. Biol. Chem. 267:8485-8491(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 3).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Lung and Testis.
    8. Bienvenut W.V.
      Submitted (OCT-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-10; 110-118; 345-364; 382-389; 479-486 AND 534-543, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    9. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-44; 64-73; 79-87; 154-160; 253-272; 306-312; 352-364; 407-429; 454-462; 489-513 AND 534-543, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 101-109; 352-364 AND 374-381.
      Tissue: Keratinocyte.
    11. "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
      Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
      J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSP90AA1.
    12. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    13. "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
      Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
      J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PACRG.
    14. "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-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 MET-1; LYS-8; LYS-301; LYS-312; LYS-325; LYS-344 AND LYS-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
      Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
      PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH METTL21B.
    23. "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine."
      Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I.
      Cell 101:199-210(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 223-349.

    Entry informationi

    Entry nameiSTIP1_HUMAN
    AccessioniPrimary (citable) accession number: P31948
    Secondary accession number(s): B4DM70
    , F5H0T1, G3XAD8, Q3ZCU9, Q5TZU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 158 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3