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Q96QV1

- HHIP_HUMAN

UniProt

Q96QV1 - HHIP_HUMAN

Protein

Hedgehog-interacting protein

Gene

HHIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    Modulates hedgehog signaling in several cell types including brain and lung through direct interaction with members of the hedgehog family.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi383 – 3831Zinc; shared with SHH

    GO - Molecular functioni

    1. hedgehog family protein binding Source: BHF-UCL
    2. oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor Source: InterPro
    3. protein binding Source: UniProtKB
    4. quinone binding Source: InterPro
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. dorsal/ventral pattern formation Source: Ensembl
    3. epithelial tube branching involved in lung morphogenesis Source: Ensembl
    4. negative regulation of signal transduction Source: UniProtKB
    5. negative regulation of smoothened signaling pathway Source: BHF-UCL
    6. neuroblast proliferation Source: Ensembl
    7. regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
    8. skeletal system morphogenesis Source: BHF-UCL
    9. smoothened signaling pathway Source: Ensembl

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ96QV1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hedgehog-interacting protein
    Short name:
    HHIP
    Short name:
    HIP
    Gene namesi
    Name:HHIP
    Synonyms:HIP
    ORF Names:UNQ5825/PRO19644
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:14866. HHIP.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Secreted By similarity
    Note: The last 22 C-terminal amino acids may participate in cell membrane attachment.

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. cytoplasm Source: UniProtKB-SubCell
    3. extracellular region Source: UniProtKB-SubCell
    4. integral component of plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi380 – 3801E → A: Abolishes SHH binding. 1 Publication
    Mutagenesisi382 – 3821M → A: Abolishes SHH binding. 1 Publication
    Mutagenesisi383 – 3831D → A or R: Abolishes SHH binding. 2 Publications
    Mutagenesisi387 – 3871D → A: Abolishes SHH binding. 1 Publication

    Organism-specific databases

    MIMi612226. phenotype.
    PharmGKBiPA29276.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 700683Hedgehog-interacting proteinPRO_0000007623Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi216 ↔ 536
    Disulfide bondi218 ↔ 543
    Disulfide bondi402 ↔ 624
    Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi435 ↔ 452
    Glycosylationi447 – 4471N-linked (GlcNAc...)1 Publication
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi500 ↔ 594
    Disulfide bondi608 ↔ 617
    Disulfide bondi612 ↔ 623
    Disulfide bondi625 ↔ 634
    Disulfide bondi639 ↔ 649
    Disulfide bondi643 ↔ 655
    Disulfide bondi657 ↔ 666

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ96QV1.
    PaxDbiQ96QV1.
    PRIDEiQ96QV1.

    PTM databases

    PhosphoSiteiQ96QV1.

    Expressioni

    Tissue specificityi

    Widely expressed in fetal and adult tissues. Highest expression in adult heart, liver and pancreas, and in fetal kidney.2 Publications

    Gene expression databases

    BgeeiQ96QV1.
    CleanExiHS_HHIP.
    GenevestigatoriQ96QV1.

    Organism-specific databases

    HPAiHPA012616.

    Interactioni

    Subunit structurei

    Interacts with all three hedgehog family members, SHH, IHH and DHH.3 Publications

    Protein-protein interaction databases

    BioGridi122156. 1 interaction.
    DIPiDIP-48536N.
    IntActiQ96QV1. 1 interaction.
    STRINGi9606.ENSP00000296575.

    Structurei

    Secondary structure

    1
    700
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi217 – 23317
    Beta strandi236 – 2394
    Beta strandi242 – 2465
    Turni247 – 2493
    Beta strandi250 – 2545
    Beta strandi256 – 2583
    Beta strandi265 – 2673
    Turni269 – 2713
    Beta strandi277 – 2793
    Beta strandi283 – 2897
    Helixi293 – 2964
    Beta strandi298 – 3058
    Beta strandi312 – 3154
    Beta strandi317 – 32610
    Helixi336 – 3383
    Beta strandi340 – 35213
    Beta strandi354 – 3596
    Helixi361 – 3633
    Beta strandi365 – 3695
    Helixi376 – 3816
    Beta strandi391 – 3966
    Beta strandi402 – 4054
    Turni413 – 4164
    Beta strandi418 – 4203
    Beta strandi424 – 4274
    Beta strandi430 – 4323
    Beta strandi434 – 4407
    Beta strandi442 – 4454
    Beta strandi447 – 4537
    Beta strandi457 – 4593
    Beta strandi463 – 4686
    Beta strandi481 – 4833
    Beta strandi491 – 4966
    Turni503 – 5075
    Beta strandi509 – 5135
    Beta strandi514 – 5163
    Beta strandi518 – 5225
    Turni525 – 5273
    Beta strandi531 – 5355
    Beta strandi537 – 5393
    Beta strandi543 – 5453
    Beta strandi549 – 5568
    Beta strandi558 – 5603
    Beta strandi562 – 5698
    Helixi571 – 5733
    Beta strandi575 – 5839
    Beta strandi587 – 5904
    Helixi592 – 5943
    Helixi607 – 6115
    Beta strandi614 – 6174
    Beta strandi623 – 6253
    Beta strandi629 – 6313
    Beta strandi644 – 6463
    Beta strandi648 – 6514
    Beta strandi654 – 6563
    Beta strandi661 – 6633

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WFTX-ray2.80A/B214-671[»]
    2WFXX-ray3.20B214-670[»]
    2WG3X-ray2.60C/D214-670[»]
    2WG4X-ray3.15B214-670[»]
    3HO3X-ray2.90A193-667[»]
    3HO4X-ray3.10A/B193-667[»]
    3HO5X-ray3.01A/B193-667[»]
    ProteinModelPortaliQ96QV1.
    SMRiQ96QV1. Positions 214-668.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96QV1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini607 – 63428EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini635 – 66733EGF-like 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni376 – 38813Interaction with SHH zinc binding siteAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi35 – 5420Arg-richAdd
    BLAST

    Domaini

    A flexible loop interacts with the SHH zinc binding site and contributes to zinc binding.

    Sequence similaritiesi

    Belongs to the HHIP family.Curated
    Contains 2 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2133.
    HOGENOMiHOG000008644.
    HOVERGENiHBG051901.
    InParanoidiQ96QV1.
    KOiK06231.
    OMAiFGDRNGN.
    OrthoDBiEOG7CZK54.
    PhylomeDBiQ96QV1.
    TreeFamiTF329059.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR018143. Folate_rcpt-like.
    IPR012938. Glc/Sorbosone_DH.
    IPR011041. Quinoprot_gluc/sorb_DH.
    [Graphical view]
    PfamiPF03024. Folate_rec. 1 hit.
    PF07995. GSDH. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 2 hits.
    [Graphical view]
    SUPFAMiSSF50952. SSF50952. 1 hit.
    PROSITEiPS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96QV1-1) [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

    MLKMLSFKLL LLAVALGFFE GDAKFGERNE GSGARRRRCL NGNPPKRLKR    50
    RDRRMMSQLE LLSGGEMLCG GFYPRLSCCL RSDSPGLGRL ENKIFSVTNN 100
    TECGKLLEEI KCALCSPHSQ SLFHSPEREV LERDLVLPLL CKDYCKEFFY 150
    TCRGHIPGFL QTTADEFCFY YARKDGGLCF PDFPRKQVRG PASNYLDQME 200
    EYDKVEEISR KHKHNCFCIQ EVVSGLRQPV GALHSGDGSQ RLFILEKEGY 250
    VKILTPEGEI FKEPYLDIHK LVQSGIKGGD ERGLLSLAFH PNYKKNGKLY 300
    VSYTTNQERW AIGPHDHILR VVEYTVSRKN PHQVDLRTAR VFLEVAELHR 350
    KHLGGQLLFG PDGFLYIILG DGMITLDDME EMDGLSDFTG SVLRLDVDTD 400
    MCNVPYSIPR SNPHFNSTNQ PPEVFAHGLH DPGRCAVDRH PTDININLTI 450
    LCSDSNGKNR SSARILQIIK GKDYESEPSL LEFKPFSNGP LVGGFVYRGC 500
    QSERLYGSYV FGDRNGNFLT LQQSPVTKQW QEKPLCLGTS GSCRGYFSGH 550
    ILGFGEDELG EVYILSSSKS MTQTHNGKLY KIVDPKRPLM PEECRATVQP 600
    AQTLTSECSR LCRNGYCTPT GKCCCSPGWE GDFCRTAKCE PACRHGGVCV 650
    RPNKCLCKKG YLGPQCEQVD RNIRRVTRAG ILDQIIDMTS YLLDLTSYIV 700
    Length:700
    Mass (Da):78,851
    Last modified:November 28, 2006 - v3
    Checksum:iCC1CB3435E29303A
    GO
    Isoform 2 (identifier: Q96QV1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         278-320: GGDERGLLSL...AIGPHDHILR → VGFLNFIYFC...NLAGENKGAT
         321-700: Missing.

    Note: Potentially soluble form.

    Show »
    Length:320
    Mass (Da):36,373
    Checksum:i3AF86509A46A7676
    GO

    Sequence cautioni

    The sequence BAB14945.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti126 – 1261P → L in BAC11154. (PubMed:14702039)Curated
    Sequence conflicti135 – 1351L → I in AAG34731. 1 PublicationCurated
    Sequence conflicti173 – 1731R → G in BAC11154. (PubMed:14702039)Curated

    Polymorphismi

    Genetic variations in HHIP define the stature quantitative trait locus 12 (STQTL12) [MIMi:612226]. Adult height is an easily observable and highly heritable complex continuous trait. Because of this, it is a model trait for studying genetic influence on quantitative traits.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti341 – 3411V → I.2 Publications
    VAR_021518

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei278 – 32043GGDER…DHILR → VGFLNFIYFCAGYVNFILVL PSSLKVFLCNKRKNLAGENK GAT in isoform 2. 2 PublicationsVSP_013192Add
    BLAST
    Alternative sequencei321 – 700380Missing in isoform 2. 2 PublicationsVSP_013193Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY009951 mRNA. Translation: AAG34731.1.
    AF326471
    , AF326459, AF326460, AF326462, AF326464, AF326466, AF326468, AF326470, AF326469, AF326467, AF326465, AF326463, AF326461 Genomic DNA. Translation: AAK18182.1.
    AY009317 mRNA. Translation: AAG35411.1.
    AY358747 mRNA. Translation: AAQ89107.1.
    AK024645 mRNA. Translation: BAB14945.1. Different initiation.
    AK074711 mRNA. Translation: BAC11154.1.
    AC098588 Genomic DNA. No translation available.
    BC009298 mRNA. Translation: AAH09298.1.
    BC025311 mRNA. Translation: AAH25311.1.
    CCDSiCCDS3762.1. [Q96QV1-1]
    RefSeqiNP_071920.1. NM_022475.2. [Q96QV1-1]
    UniGeneiHs.507991.

    Genome annotation databases

    EnsembliENST00000296575; ENSP00000296575; ENSG00000164161. [Q96QV1-1]
    ENST00000434550; ENSP00000408587; ENSG00000164161. [Q96QV1-2]
    GeneIDi64399.
    KEGGihsa:64399.
    UCSCiuc003ijr.2. human. [Q96QV1-2]
    uc003ijs.2. human. [Q96QV1-1]

    Polymorphism databases

    DMDMi118572655.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY009951 mRNA. Translation: AAG34731.1 .
    AF326471
    , AF326459 , AF326460 , AF326462 , AF326464 , AF326466 , AF326468 , AF326470 , AF326469 , AF326467 , AF326465 , AF326463 , AF326461 Genomic DNA. Translation: AAK18182.1 .
    AY009317 mRNA. Translation: AAG35411.1 .
    AY358747 mRNA. Translation: AAQ89107.1 .
    AK024645 mRNA. Translation: BAB14945.1 . Different initiation.
    AK074711 mRNA. Translation: BAC11154.1 .
    AC098588 Genomic DNA. No translation available.
    BC009298 mRNA. Translation: AAH09298.1 .
    BC025311 mRNA. Translation: AAH25311.1 .
    CCDSi CCDS3762.1. [Q96QV1-1 ]
    RefSeqi NP_071920.1. NM_022475.2. [Q96QV1-1 ]
    UniGenei Hs.507991.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WFT X-ray 2.80 A/B 214-671 [» ]
    2WFX X-ray 3.20 B 214-670 [» ]
    2WG3 X-ray 2.60 C/D 214-670 [» ]
    2WG4 X-ray 3.15 B 214-670 [» ]
    3HO3 X-ray 2.90 A 193-667 [» ]
    3HO4 X-ray 3.10 A/B 193-667 [» ]
    3HO5 X-ray 3.01 A/B 193-667 [» ]
    ProteinModelPortali Q96QV1.
    SMRi Q96QV1. Positions 214-668.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122156. 1 interaction.
    DIPi DIP-48536N.
    IntActi Q96QV1. 1 interaction.
    STRINGi 9606.ENSP00000296575.

    PTM databases

    PhosphoSitei Q96QV1.

    Polymorphism databases

    DMDMi 118572655.

    Proteomic databases

    MaxQBi Q96QV1.
    PaxDbi Q96QV1.
    PRIDEi Q96QV1.

    Protocols and materials databases

    DNASUi 64399.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296575 ; ENSP00000296575 ; ENSG00000164161 . [Q96QV1-1 ]
    ENST00000434550 ; ENSP00000408587 ; ENSG00000164161 . [Q96QV1-2 ]
    GeneIDi 64399.
    KEGGi hsa:64399.
    UCSCi uc003ijr.2. human. [Q96QV1-2 ]
    uc003ijs.2. human. [Q96QV1-1 ]

    Organism-specific databases

    CTDi 64399.
    GeneCardsi GC04P145567.
    HGNCi HGNC:14866. HHIP.
    HPAi HPA012616.
    MIMi 606178. gene.
    612226. phenotype.
    neXtProti NX_Q96QV1.
    PharmGKBi PA29276.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2133.
    HOGENOMi HOG000008644.
    HOVERGENi HBG051901.
    InParanoidi Q96QV1.
    KOi K06231.
    OMAi FGDRNGN.
    OrthoDBi EOG7CZK54.
    PhylomeDBi Q96QV1.
    TreeFami TF329059.

    Enzyme and pathway databases

    SignaLinki Q96QV1.

    Miscellaneous databases

    ChiTaRSi HHIP. human.
    EvolutionaryTracei Q96QV1.
    GeneWikii HHIP.
    GenomeRNAii 64399.
    NextBioi 66342.
    PROi Q96QV1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96QV1.
    CleanExi HS_HHIP.
    Genevestigatori Q96QV1.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR018143. Folate_rcpt-like.
    IPR012938. Glc/Sorbosone_DH.
    IPR011041. Quinoprot_gluc/sorb_DH.
    [Graphical view ]
    Pfami PF03024. Folate_rec. 1 hit.
    PF07995. GSDH. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50952. SSF50952. 1 hit.
    PROSITEi PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Determination of the chromosomal location and genomic structure of the Hedgehog-interacting protein gene, and analysis of its role in holoprosencephaly."
      Huo L., Roessler E., Dutra A., Chuang P.-T., McMahon A.P., Muenke M.
      Gene Funct. Dis. 1:119-127(2000)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT ILE-341, TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    2. "The human hedgehog-interacting protein gene: structure and chromosome mapping to 4q31.21-->q31.3."
      Bak M., Hansen C., Friis Henriksen K., Tommerup N.
      Cytogenet. Cell Genet. 92:300-303(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Testis.
    3. 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] (ISOFORMS 1 AND 2), VARIANT ILE-341.
      Tissue: Coronary arterial endothelium and Teratocarcinoma.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Muscle.
    7. Cited for: FUNCTION, SUBUNIT.
    8. "The structure of SHH in complex with HHIP reveals a recognition role for the Shh pseudo active site in signaling."
      Bosanac I., Maun H.R., Scales S.J., Wen X., Lingel A., Bazan J.F., de Sauvage F.J., Hymowitz S.G., Lazarus R.A.
      Nat. Struct. Mol. Biol. 16:691-697(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 193-667 IN COMPLEX WITH SHH, INTERACTION WITH SHH, FUNCTION, MUTAGENESIS OF GLU-380; MET-382; ASP-383 AND ASP-387, DISULFIDE BONDS.
    9. "Structural insights into hedgehog ligand sequestration by the human hedgehog-interacting protein HHIP."
      Bishop B., Aricescu A.R., Harlos K., O'Callaghan C.A., Jones E.Y., Siebold C.
      Nat. Struct. Mol. Biol. 16:698-703(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 214-670 IN COMPLEX WITH SHH, INTERACTION WITH SHH AND DHH, DISULFIDE BONDS, MUTAGENESIS OF ASP-383, GLYCOSYLATION AT ASN-447.

    Entry informationi

    Entry nameiHHIP_HUMAN
    AccessioniPrimary (citable) accession number: Q96QV1
    Secondary accession number(s): Q6PK09
    , Q8NCI7, Q9BXK3, Q9H1J4, Q9H7E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 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 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3