Q96QV1 (HHIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hedgehog-interacting protein
Short name=HHIP
Short name=HIP

Gene names

Name:	HHIP
Synonyms:	HIP
ORF Names:	UNQ5825/PRO19644

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Modulates hedgehog signaling in several cell types including brain and lung through direct interaction with members of the hedgehog family. Ref.7 Ref.8
Subunit structure	Interacts with all three hedgehog family members, SHH, IHH and DHH. Ref.7 Ref.8 Ref.9
Subcellular location	Cell membrane; Peripheral membrane protein By similarity. Secreted By similarity. Note: The last 22 C-terminal amino acids may participate in cell membrane attachment. Isoform 2: Cytoplasm Probable.
Tissue specificity	Widely expressed in fetal and adult tissues. Highest expression in adult heart, liver and pancreas, and in fetal kidney. Ref.1 Ref.2
Domain	A flexible loop interacts with the SHH zinc binding site and contributes to zinc binding.
Polymorphism	Genetic variations in HHIP define the stature quantitative trait locus 12 (STQTL12) [MIM: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.
Sequence similarities	Belongs to the HHIP family. Contains 2 EGF-like domains.
Sequence caution	The sequence BAB14945.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Repeat Signal
Ligand	Metal-binding Zinc
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro dorsal/ventral pattern formation Inferred from electronic annotation. Source: Compara epithelial tube branching involved in lung morphogenesis Inferred from electronic annotation. Source: Compara negative regulation of smoothened signaling pathway Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL neuroblast proliferation Inferred from electronic annotation. Source: Compara regulation of fibroblast growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara skeletal system morphogenesis Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL smoothened signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL
Molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor Inferred from electronic annotation. Source: InterPro quinone binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96QV1-1)

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.

Isoform 2 (identifier: Q96QV1-2)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Chain

18 – 700

683

Hedgehog-interacting protein

PRO_0000007623

Regions

Domain

607 – 634

28

EGF-like 1

Domain

635 – 667

33

EGF-like 2

Region

376 – 388

13

Interaction with SHH zinc binding site

Compositional bias

35 – 54

20

Arg-rich

Sites

Metal binding

383

1

Zinc; shared with SHH

Amino acid modifications

Glycosylation

99

1

N-linked (GlcNAc...) Potential

Glycosylation

416

1

N-linked (GlcNAc...) Potential

Glycosylation

447

1

N-linked (GlcNAc...) Potential

Glycosylation

459

1

N-linked (GlcNAc...) Potential

Disulfide bond

216 ↔ 536

Ref.8 Ref.9

Disulfide bond

218 ↔ 543

Ref.8 Ref.9

Disulfide bond

402 ↔ 624

Ref.8 Ref.9

Disulfide bond

435 ↔ 452

Ref.8 Ref.9

Disulfide bond

500 ↔ 594

Ref.8 Ref.9

Disulfide bond

608 ↔ 617

Ref.8 Ref.9

Disulfide bond

612 ↔ 623

Ref.8 Ref.9

Disulfide bond

625 ↔ 634

Ref.8 Ref.9

Disulfide bond

639 ↔ 649

Ref.8 Ref.9

Disulfide bond

643 ↔ 655

Ref.8 Ref.9

Disulfide bond

657 ↔ 666

Ref.8 Ref.9

Natural variations

Alternative sequence

278 – 320

43

GGDER…DHILR → VGFLNFIYFCAGYVNFILVL PSSLKVFLCNKRKNLAGENK GAT in isoform 2.

VSP_013192

Alternative sequence

321 – 700

380

Missing in isoform 2.

VSP_013193

Natural variant

341

1

V → I. Ref.1 Ref.4

VAR_021518

Experimental info

Mutagenesis

380

1

E → A: Abolishes SHH binding. Ref.8

Mutagenesis

382

1

M → A: Abolishes SHH binding. Ref.8

Mutagenesis

383

1

D → A or R: Abolishes SHH binding. Ref.8

Mutagenesis

387

1

D → A: Abolishes SHH binding. Ref.8

Sequence conflict

126

1

P → L in BAC11154. Ref.4

Sequence conflict

135

1

L → I in AAG34731. Ref.1

Sequence conflict

173

1

R → G in BAC11154. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

700

Helix Strand Turn

Details...

Beta strand

217 – 233

17

Beta strand

236 – 239

4

Beta strand

242 – 246

5

Turn

247 – 249

3

Beta strand

250 – 254

5

Beta strand

256 – 258

3

Beta strand

265 – 267

3

Turn

269 – 271

3

Beta strand

277 – 279

3

Beta strand

283 – 289

7

Helix

293 – 296

4

Beta strand

298 – 305

8

Beta strand

312 – 315

4

Beta strand

317 – 326

10

Helix

336 – 338

3

Beta strand

340 – 352

13

Beta strand

354 – 359

6

Helix

361 – 363

3

Beta strand

365 – 369

5

Helix

376 – 381

6

Beta strand

391 – 396

6

Beta strand

402 – 405

4

Turn

413 – 416

4

Beta strand

418 – 420

3

Beta strand

424 – 427

4

Beta strand

430 – 432

3

Beta strand

434 – 440

7

Beta strand

442 – 445

4

Beta strand

447 – 453

7

Beta strand

457 – 459

3

Beta strand

463 – 468

6

Beta strand

481 – 483

3

Beta strand

491 – 496

6

Turn

503 – 507

5

Beta strand

509 – 513

5

Beta strand

514 – 516

3

Beta strand

518 – 522

5

Turn

525 – 527

3

Beta strand

531 – 535

5

Beta strand

537 – 539

3

Beta strand

543 – 545

3

Beta strand

549 – 556

8

Beta strand

558 – 560

3

Beta strand

562 – 569

8

Helix

571 – 573

3

Beta strand

575 – 583

9

Beta strand

587 – 590

4

Helix

592 – 594

3

Helix

607 – 611

5

Beta strand

614 – 617

4

Beta strand

623 – 625

3

Beta strand

629 – 631

3

Beta strand

644 – 646

3

Beta strand

648 – 651

4

Beta strand

654 – 656

3

Beta strand

661 – 663

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 3. Checksum: CC1CB3435E29303A	FASTA	700	78,851
	10 20 30 40 50 60 MLKMLSFKLL LLAVALGFFE GDAKFGERNE GSGARRRRCL NGNPPKRLKR RDRRMMSQLE 70 80 90 100 110 120 LLSGGEMLCG GFYPRLSCCL RSDSPGLGRL ENKIFSVTNN TECGKLLEEI KCALCSPHSQ 130 140 150 160 170 180 SLFHSPEREV LERDLVLPLL CKDYCKEFFY TCRGHIPGFL QTTADEFCFY YARKDGGLCF 190 200 210 220 230 240 PDFPRKQVRG PASNYLDQME EYDKVEEISR KHKHNCFCIQ EVVSGLRQPV GALHSGDGSQ 250 260 270 280 290 300 RLFILEKEGY VKILTPEGEI FKEPYLDIHK LVQSGIKGGD ERGLLSLAFH PNYKKNGKLY 310 320 330 340 350 360 VSYTTNQERW AIGPHDHILR VVEYTVSRKN PHQVDLRTAR VFLEVAELHR KHLGGQLLFG 370 380 390 400 410 420 PDGFLYIILG DGMITLDDME EMDGLSDFTG SVLRLDVDTD MCNVPYSIPR SNPHFNSTNQ 430 440 450 460 470 480 PPEVFAHGLH DPGRCAVDRH PTDININLTI LCSDSNGKNR SSARILQIIK GKDYESEPSL 490 500 510 520 530 540 LEFKPFSNGP LVGGFVYRGC QSERLYGSYV FGDRNGNFLT LQQSPVTKQW QEKPLCLGTS 550 560 570 580 590 600 GSCRGYFSGH ILGFGEDELG EVYILSSSKS MTQTHNGKLY KIVDPKRPLM PEECRATVQP 610 620 630 640 650 660 AQTLTSECSR LCRNGYCTPT GKCCCSPGWE GDFCRTAKCE PACRHGGVCV RPNKCLCKKG 670 680 690 700 YLGPQCEQVD RNIRRVTRAG ILDQIIDMTS YLLDLTSYIV
	Isoform 2 [UniParc]. Checksum: 3AF86509A46A7676	FASTA	320	36,373
	10 20 30 40 50 60 MLKMLSFKLL LLAVALGFFE GDAKFGERNE GSGARRRRCL NGNPPKRLKR RDRRMMSQLE 70 80 90 100 110 120 LLSGGEMLCG GFYPRLSCCL RSDSPGLGRL ENKIFSVTNN TECGKLLEEI KCALCSPHSQ 130 140 150 160 170 180 SLFHSPEREV LERDLVLPLL CKDYCKEFFY TCRGHIPGFL QTTADEFCFY YARKDGGLCF 190 200 210 220 230 240 PDFPRKQVRG PASNYLDQME EYDKVEEISR KHKHNCFCIQ EVVSGLRQPV GALHSGDGSQ 250 260 270 280 290 300 RLFILEKEGY VKILTPEGEI FKEPYLDIHK LVQSGIKVGF LNFIYFCAGY VNFILVLPSS 310 320 LKVFLCNKRK NLAGENKGAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Comparative biological responses to human Sonic, Indian, and Desert hedgehog." Pathi S., Pagan-Westphal S., Baker D.P., Garber E.A., Rayhorn P., Bumcrot D., Tabin C.J., Blake Pepinsky R., Williams K.P. Mech. Dev. 106:107-117(2001) [PubMed] [Europe PMC] [Abstract] 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, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00045106.
IPI00556597.

RefSeq

NP_071920.1. NM_022475.2.

UniGene

Hs.507991.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q96QV1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48536N.

STRING

9606.ENSP00000296575.

PTM databases

PhosphoSite

Q96QV1.

Polymorphism databases

DMDM

118572655.

Proteomic databases

PaxDb

Q96QV1.

PRIDE

Q96QV1.

Protocols and materials databases

DNASU

64399.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296575; ENSP00000296575; ENSG00000164161.
ENST00000434550; ENSP00000408587; ENSG00000164161.

GeneID

64399.

KEGG

hsa:64399.

UCSC

uc003ijr.2. human.
uc003ijs.2. human.

Organism-specific databases

CTD

64399.

GeneCards

GC04P145567.

HGNC

HGNC:14866. HHIP.

HPA

HPA012616.

MIM

606178. gene.
612226. phenotype.

neXtProt

NX_Q96QV1.

PharmGKB

PA29276.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2133.

HOGENOM

HOG000008644.

HOVERGEN

HBG051901.

InParanoid

Q96QV1.

KO

K06231.

OMA

NGNFLTL.

OrthoDB

EOG483D41.

PhylomeDB

Q96QV1.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_2pathway. Signaling events mediated by the Hedgehog family.

Gene expression databases

Bgee

Q96QV1.

CleanEx

HS_HHIP.

Genevestigator

Q96QV1.

GermOnline

ENSG00000164161. Homo sapiens.

Family and domain databases

Gene3D

2.120.10.30. 1 hit.

InterPro

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]

Pfam

PF03024. Folate_rec. 1 hit.
PF07995. GSDH. 1 hit.
[Graphical view]

SMART

SM00181. EGF. 2 hits.
[Graphical view]

SUPFAM

SSF50952. Quino_gluc_DH. 1 hit.

PROSITE

PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HHIP. human.

EvolutionaryTrace

Q96QV1.

GenomeRNAi

64399.

NextBio

66342.

SOURCE

Search...

Entry information

Entry name

HHIP_HUMAN

Accession

Primary (citable) accession number: Q96QV1
Secondary accession number(s): Q6PK09 , Q8NCI7, Q9BXK3, Q9H1J4, Q9H7E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	November 28, 2006
Last modified:	May 1, 2013
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.