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Q96QV1

- HHIP_HUMAN

UniProt

Q96QV1 - HHIP_HUMAN

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Protein

Hedgehog-interacting protein

Gene

HHIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. quinone binding Source: InterPro
  4. 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
Complete GO annotation...

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-KW
  3. extracellular region Source: UniProtKB-KW
  4. integral component of plasma membrane Source: BHF-UCL
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063250.
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

        10         20         30         40         50
MLKMLSFKLL LLAVALGFFE GDAKFGERNE GSGARRRRCL NGNPPKRLKR
60 70 80 90 100
RDRRMMSQLE LLSGGEMLCG GFYPRLSCCL RSDSPGLGRL ENKIFSVTNN
110 120 130 140 150
TECGKLLEEI KCALCSPHSQ SLFHSPEREV LERDLVLPLL CKDYCKEFFY
160 170 180 190 200
TCRGHIPGFL QTTADEFCFY YARKDGGLCF PDFPRKQVRG PASNYLDQME
210 220 230 240 250
EYDKVEEISR KHKHNCFCIQ EVVSGLRQPV GALHSGDGSQ RLFILEKEGY
260 270 280 290 300
VKILTPEGEI FKEPYLDIHK LVQSGIKGGD ERGLLSLAFH PNYKKNGKLY
310 320 330 340 350
VSYTTNQERW AIGPHDHILR VVEYTVSRKN PHQVDLRTAR VFLEVAELHR
360 370 380 390 400
KHLGGQLLFG PDGFLYIILG DGMITLDDME EMDGLSDFTG SVLRLDVDTD
410 420 430 440 450
MCNVPYSIPR SNPHFNSTNQ PPEVFAHGLH DPGRCAVDRH PTDININLTI
460 470 480 490 500
LCSDSNGKNR SSARILQIIK GKDYESEPSL LEFKPFSNGP LVGGFVYRGC
510 520 530 540 550
QSERLYGSYV FGDRNGNFLT LQQSPVTKQW QEKPLCLGTS GSCRGYFSGH
560 570 580 590 600
ILGFGEDELG EVYILSSSKS MTQTHNGKLY KIVDPKRPLM PEECRATVQP
610 620 630 640 650
AQTLTSECSR LCRNGYCTPT GKCCCSPGWE GDFCRTAKCE PACRHGGVCV
660 670 680 690 700
RPNKCLCKKG YLGPQCEQVD RNIRRVTRAG ILDQIIDMTS YLLDLTSYIV
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00530000063250.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 112 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