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Protein

Huntingtin-interacting protein 1

Gene

HIP1

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

Functioni

Plays a role in clathrin-mediated endocytosis and trafficking. Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. Enhances androgen receptor (AR)-mediated transcription. May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. May play a functional role in the cell filament networks. May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors.8 Publications

GO - Molecular functioni

  1. clathrin binding Source: MGI
  2. phosphatidylinositol binding Source: UniProtKB
  3. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  3. apoptotic process Source: MGI
  4. apoptotic signaling pathway Source: UniProtKB
  5. cell differentiation Source: UniProtKB-KW
  6. clathrin coat assembly Source: UniProtKB
  7. endocytosis Source: UniProtKB-KW
  8. positive regulation of receptor-mediated endocytosis Source: UniProtKB
  9. regulation of apoptotic process Source: MGI
  10. regulation of transcription, DNA-templated Source: UniProtKB-KW
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Differentiation, Endocytosis, Transcription, Transcription regulation

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Huntingtin-interacting protein 1
Short name:
HIP-1
Alternative name(s):
Huntingtin-interacting protein I
Short name:
HIP-I
Gene namesi
Name:HIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:4913. HIP1.

Subcellular locationi

  1. Cytoplasm
  2. Nucleus
  3. Endomembrane system
  4. Cytoplasmic vesicleclathrin-coated vesicle membrane

  5. Note: Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR.

GO - Cellular componenti

  1. clathrin-coated vesicle Source: UniProtKB
  2. clathrin-coated vesicle membrane Source: UniProtKB-SubCell
  3. cytoplasm Source: MGI
  4. cytoskeleton Source: ProtInc
  5. Golgi apparatus Source: MGI
  6. intracellular membrane-bounded organelle Source: HPA
  7. membrane Source: ProtInc
  8. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving HIP1 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;7)(q33;q11.2) with PDGFRB. The chimeric HIP1-PDGFRB transcript results from an in-frame fusion of the two genes. The reciprocal PDGFRB-HIP1 transcript is not expressed.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561K → E: Abolishes 3-phosphoinositide-binding; when associated with E-58. 1 Publication
Mutagenesisi58 – 581K → E: Abolishes 3-phosphoinositide-binding; when associated with E-56. 1 Publication
Mutagenesisi432 – 4321F → G: Abolishes HIP1-induced cell death. 1 Publication
Mutagenesisi1005 – 10051R → E: Reduces AR-induced nuclear translocation. 1 Publication

Keywords - Diseasei

Neurodegeneration

Organism-specific databases

PharmGKBiPA29289.

Polymorphism and mutation databases

BioMutaiHIP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10371037Huntingtin-interacting protein 1PRO_0000083986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei338 – 3381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00291.
PaxDbiO00291.
PRIDEiO00291.

PTM databases

PhosphoSiteiO00291.

Expressioni

Tissue specificityi

Ubiquitously expressed with the highest level in brain. Expression is up-regulated in prostate and colon cancer.3 Publications

Gene expression databases

BgeeiO00291.
CleanExiHS_HIP1.
ExpressionAtlasiO00291. baseline and differential.
GenevestigatoriO00291.

Organism-specific databases

HPAiCAB015334.
CAB016402.
HPA013606.
HPA017964.

Interactioni

Subunit structurei

Homodimer. Binds actin. Binds HTT (via N-terminus). This interaction is restricted to the brain. Binds to IFT57. In normal conditions, it poorly interacts with IFT57, HIP1 being strongly associated with HTT. However, in mutant HTT proteins with a long poly-Gln region, interaction between HTT and HIP1 is inhibited, promoting the interaction between HIP1 and IFT57. Interacts with CLTB (via N-terminus). Interacts (via coiled coil domain) with AR. Interacts with AP2A1, AP2A2, CLTC and HIP1R. Interacts with GRIA1, GRIN2A AND GRIN2B.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Apaf1Q9EPV52EBI-473886,EBI-6978501From a different organism.
DAZAP2Q150383EBI-473886,EBI-724310
HTTP428584EBI-473886,EBI-466029
Necap1Q9CR953EBI-473886,EBI-7592476From a different organism.
RELQ048643EBI-473886,EBI-307352

Protein-protein interaction databases

BioGridi109339. 19 interactions.
DIPiDIP-17041N.
IntActiO00291. 18 interactions.
MINTiMINT-208214.
STRINGi9606.ENSP00000336747.

Structurei

Secondary structure

1
1037
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi373 – 44169Combined sources
Turni459 – 4613Combined sources
Helixi462 – 4654Combined sources
Helixi482 – 58099Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NO2X-ray2.80A482-586[»]
2QA7X-ray2.80A/B/C/D370-481[»]
3I00X-ray2.30A/B361-480[»]
ProteinModelPortaliO00291.
SMRiO00291. Positions 371-472, 481-581, 773-966.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00291.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 160129ENTHPROSITE-ProRule annotationAdd
BLAST
Domaini771 – 1012242I/LWEQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni410 – 49182pDEDAdd
BLAST
Regioni867 – 92458Important for actin bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili368 – 644277Sequence AnalysisAdd
BLAST

Domaini

The pseudo DED region (pDED) mediates the interaction with IFT57.1 Publication
Binds F-actin via the talin-like I/LWEQ domain.1 Publication

Sequence similaritiesi

Belongs to the SLA2 family.Curated
Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation
Contains 1 I/LWEQ domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG280957.
GeneTreeiENSGT00550000074542.
HOGENOMiHOG000020612.
HOVERGENiHBG005968.
InParanoidiO00291.
KOiK04559.
OMAiVQGRGKF.
PhylomeDBiO00291.
TreeFamiTF316860.

Family and domain databases

Gene3Di1.20.1410.10. 1 hit.
1.25.40.90. 1 hit.
InterProiIPR011417. ANTH_dom.
IPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR030554. HIP1.
IPR002558. ILWEQ_dom.
IPR030224. Sla2_fam.
[Graphical view]
PANTHERiPTHR10407. PTHR10407. 1 hit.
PTHR10407:SF14. PTHR10407:SF14. 1 hit.
PfamiPF07651. ANTH. 1 hit.
PF01608. I_LWEQ. 1 hit.
[Graphical view]
ProDomiPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00273. ENTH. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMiSSF109885. SSF109885. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform HIP1-1 (identifier: O00291-1) [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
MDRMASSMKQ VPNPLPKVLS RRGVGAGLEA AERESFERTQ TVSINKAINT
60 70 80 90 100
QEVAVKEKHA RTCILGTHHE KGAQTFWSVV NRLPLSSNAV LCWKFCHVFH
110 120 130 140 150
KLLRDGHPNV LKDSLRYRNE LSDMSRMWGH LSEGYGQLCS IYLKLLRTKM
160 170 180 190 200
EYHTKNPRFP GNLQMSDRQL DEAGESDVNN FFQLTVEMFD YLECELNLFQ
210 220 230 240 250
TVFNSLDMSR SVSVTAAGQC RLAPLIQVIL DCSHLYDYTV KLLFKLHSCL
260 270 280 290 300
PADTLQGHRD RFMEQFTKLK DLFYRSSNLQ YFKRLIQIPQ LPENPPNFLR
310 320 330 340 350
ASALSEHISP VVVIPAEASS PDSEPVLEKD DLMDMDASQQ NLFDNKFDDI
360 370 380 390 400
FGSSFSSDPF NFNSQNGVNK DEKDHLIERL YREISGLKAQ LENMKTESQR
410 420 430 440 450
VVLQLKGHVS ELEADLAEQQ HLRQQAADDC EFLRAELDEL RRQREDTEKA
460 470 480 490 500
QRSLSEIERK AQANEQRYSK LKEKYSELVQ NHADLLRKNA EVTKQVSMAR
510 520 530 540 550
QAQVDLEREK KELEDSLERI SDQGQRKTQE QLEVLESLKQ ELATSQRELQ
560 570 580 590 600
VLQGSLETSA QSEANWAAEF AELEKERDSL VSGAAHREEE LSALRKELQD
610 620 630 640 650
TQLKLASTEE SMCQLAKDQR KMLLVGSRKA AEQVIQDALN QLEEPPLISC
660 670 680 690 700
AGSADHLLST VTSISSCIEQ LEKSWSQYLA CPEDISGLLH SITLLAHLTS
710 720 730 740 750
DAIAHGATTC LRAPPEPADS LTEACKQYGR ETLAYLASLE EEGSLENADS
760 770 780 790 800
TAMRNCLSKI KAIGEELLPR GLDIKQEELG DLVDKEMAAT SAAIETATAR
810 820 830 840 850
IEEMLSKSRA GDTGVKLEVN ERILGCCTSL MQAIQVLIVA SKDLQREIVE
860 870 880 890 900
SGRGTASPKE FYAKNSRWTE GLISASKAVG WGATVMVDAA DLVVQGRGKF
910 920 930 940 950
EELMVCSHEI AASTAQLVAA SKVKADKDSP NLAQLQQASR GVNQATAGVV
960 970 980 990 1000
ASTISGKSQI EETDNMDFSS MTLTQIKRQE MDSQVRVLEL ENELQKERQK
1010 1020 1030
LGELRKKHYE LAGVAEGWEE GTEASPPTLQ EVVTEKE
Length:1,037
Mass (Da):116,221
Last modified:September 23, 2008 - v5
Checksum:iF8C0369DBF0A836F
GO
Isoform HIP1-2 (identifier: O00291-2)

Sequence is not available
Length:
Mass (Da):
Isoform 3 (identifier: O00291-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     803-853: Missing.

Note: No experimental confirmation available.

Show »
Length:986
Mass (Da):110,663
Checksum:iC09BAD680242941A
GO
Isoform 4 (identifier: O00291-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MDRMASSMKQVPNPLPKVLSRRGVGAGLEAAERESFERTQ → MMFPNPEPPPE

Show »
Length:1,008
Mass (Da):113,076
Checksum:i37DDE891F2F15C00
GO

Sequence cautioni

The sequence AAC51257.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891A → P in AAC33564 (PubMed:11788820).Curated
Sequence conflicti245 – 2517KLHSCLP → EFAAAST in CAA70574 (PubMed:9147654).Curated
Sequence conflicti357 – 3571S → R in BAG65499 (PubMed:14702039).Curated
Sequence conflicti639 – 6446LNQLEE → STRPRI in CAA70574 (PubMed:9147654).Curated
Sequence conflicti688 – 6881L → F in AAL87037 (PubMed:11788820).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti263 – 2631M → K.
Corresponds to variant rs17149023 [ dbSNP | Ensembl ].
VAR_051032

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4040MDRMA…FERTQ → MMFPNPEPPPE in isoform 4. 1 PublicationVSP_057400Add
BLAST
Alternative sequencei803 – 85351Missing in isoform 3. 1 PublicationVSP_044736Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF437291 mRNA. Translation: AHA56631.1.
AK304738 mRNA. Translation: BAG65499.1.
AC004491 Genomic DNA. No translation available.
AC018720 Genomic DNA. No translation available.
AC211429 Genomic DNA. No translation available.
KF495977 Genomic DNA. No translation available.
BC110545 mRNA. Translation: AAI10546.1.
AF365404 mRNA. Translation: AAL87037.1.
AH006397 Genomic DNA. Translation: AAC33564.1.
U79734 mRNA. Translation: AAC51257.1. Different initiation.
Y09420 mRNA. Translation: CAA70574.1.
CCDSiCCDS34669.1. [O00291-1]
CCDS59060.1. [O00291-3]
RefSeqiNP_001230127.1. NM_001243198.2. [O00291-3]
NP_005329.3. NM_005338.6. [O00291-1]
XP_005250361.1. XM_005250304.2. [O00291-4]
UniGeneiHs.329266.
Hs.619089.
Hs.674397.

Genome annotation databases

EnsembliENST00000336926; ENSP00000336747; ENSG00000127946. [O00291-1]
ENST00000434438; ENSP00000410300; ENSG00000127946. [O00291-3]
ENST00000616821; ENSP00000484528; ENSG00000127946. [O00291-4]
GeneIDi3092.
KEGGihsa:3092.
UCSCiuc003uds.2. human. [O00291-1]

Polymorphism and mutation databases

BioMutaiHIP1.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF437291 mRNA. Translation: AHA56631.1.
AK304738 mRNA. Translation: BAG65499.1.
AC004491 Genomic DNA. No translation available.
AC018720 Genomic DNA. No translation available.
AC211429 Genomic DNA. No translation available.
KF495977 Genomic DNA. No translation available.
BC110545 mRNA. Translation: AAI10546.1.
AF365404 mRNA. Translation: AAL87037.1.
AH006397 Genomic DNA. Translation: AAC33564.1.
U79734 mRNA. Translation: AAC51257.1. Different initiation.
Y09420 mRNA. Translation: CAA70574.1.
CCDSiCCDS34669.1. [O00291-1]
CCDS59060.1. [O00291-3]
RefSeqiNP_001230127.1. NM_001243198.2. [O00291-3]
NP_005329.3. NM_005338.6. [O00291-1]
XP_005250361.1. XM_005250304.2. [O00291-4]
UniGeneiHs.329266.
Hs.619089.
Hs.674397.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NO2X-ray2.80A482-586[»]
2QA7X-ray2.80A/B/C/D370-481[»]
3I00X-ray2.30A/B361-480[»]
ProteinModelPortaliO00291.
SMRiO00291. Positions 371-472, 481-581, 773-966.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109339. 19 interactions.
DIPiDIP-17041N.
IntActiO00291. 18 interactions.
MINTiMINT-208214.
STRINGi9606.ENSP00000336747.

PTM databases

PhosphoSiteiO00291.

Polymorphism and mutation databases

BioMutaiHIP1.

Proteomic databases

MaxQBiO00291.
PaxDbiO00291.
PRIDEiO00291.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336926; ENSP00000336747; ENSG00000127946. [O00291-1]
ENST00000434438; ENSP00000410300; ENSG00000127946. [O00291-3]
ENST00000616821; ENSP00000484528; ENSG00000127946. [O00291-4]
GeneIDi3092.
KEGGihsa:3092.
UCSCiuc003uds.2. human. [O00291-1]

Organism-specific databases

CTDi3092.
GeneCardsiGC07M075162.
HGNCiHGNC:4913. HIP1.
HPAiCAB015334.
CAB016402.
HPA013606.
HPA017964.
MIMi601767. gene.
neXtProtiNX_O00291.
PharmGKBiPA29289.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG280957.
GeneTreeiENSGT00550000074542.
HOGENOMiHOG000020612.
HOVERGENiHBG005968.
InParanoidiO00291.
KOiK04559.
OMAiVQGRGKF.
PhylomeDBiO00291.
TreeFamiTF316860.

Miscellaneous databases

ChiTaRSiHIP1. human.
EvolutionaryTraceiO00291.
GenomeRNAii3092.
NextBioi12271.
PROiO00291.
SOURCEiSearch...

Gene expression databases

BgeeiO00291.
CleanExiHS_HIP1.
ExpressionAtlasiO00291. baseline and differential.
GenevestigatoriO00291.

Family and domain databases

Gene3Di1.20.1410.10. 1 hit.
1.25.40.90. 1 hit.
InterProiIPR011417. ANTH_dom.
IPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR030554. HIP1.
IPR002558. ILWEQ_dom.
IPR030224. Sla2_fam.
[Graphical view]
PANTHERiPTHR10407. PTHR10407. 1 hit.
PTHR10407:SF14. PTHR10407:SF14. 1 hit.
PfamiPF07651. ANTH. 1 hit.
PF01608. I_LWEQ. 1 hit.
[Graphical view]
ProDomiPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00273. ENTH. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMiSSF109885. SSF109885. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Kim R.N., Lira M.E., Takeuchi K., Song J.Y., Hong M., Oh E., Mao M., Han J., Choi S.J., Kim J., Choi Y.L.
    Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi."
    Gervais F.G., Singaraja R., Xanthoudakis S., Gutekunst C.-A., Leavitt B.R., Metzler M., Hackam A.S., Tam J., Vaillancourt J.P., Houtzager V., Rasper D.M., Roy S., Hayden M.R., Nicholson D.W.
    Nat. Cell Biol. 4:95-105(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1037, INTERACTION WITH IFT57, SUBUNIT, DOMAIN.
  6. "Genomic organization of the human HIP1 gene and its exclusion as a candidate gene in a family diagnosed with Huntington disease without CAG expansion."
    Huq A.H.M.M., Nichol K., Osborne L., Scherer S.W., Squitieri F., Hayden M.R.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-1037.
  7. "HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain."
    Kalchman M.A., Koide H.B., McCutcheon K., Graham R.K., Nichol K., Nishiyama K., Kazemi-Esfarjani P., Lynn F.C., Wellington C., Metzler M., Goldberg Y.P., Kanazawa I., Geitz R.D., Hayden M.R.
    Nat. Genet. 16:44-53(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-1037, INTERACTION WITH HTT, TISSUE SPECIFICITY.
  8. "HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system."
    Wanker E.E., Rovira C., Scherzinger E., Hasenbank R., Waelter S., Tait D., Colicelli J., Lehrach H.
    Hum. Mol. Genet. 6:487-495(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-644, FUNCTION, INTERACTION WITH HTT, TISSUE SPECIFICITY.
    Tissue: Brain.
  9. "Fusion of Huntingtin interacting protein 1 to platelet-derived growth factor beta receptor (PDGFbetaR) in chronic myelomonocytic leukemia with t(5;7)(q33;q11.2)."
    Ross T.S., Bernard O.A., Berger R., Gilliland D.G.
    Blood 91:4419-4426(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION.
  10. Cited for: FUNCTION, MUTAGENESIS OF PHE-432.
  11. "HIP12 is a non-proapoptotic member of a gene family including HIP1, an interacting protein with huntingtin."
    Chopra V.S., Metzler M., Rasper D.M., Engqvist-Goldstein A.E.Y., Singaraja R., Gan L., Fichter K.M., McCutcheon K., Drubin D., Nicholson D.W., Hayden M.R.
    Mamm. Genome 11:1006-1015(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  12. "The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis."
    Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R., Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H., Wanker E.E.
    Hum. Mol. Genet. 10:1807-1817(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AP2A1; AP2A2 AND CLTC, SUBCELLULAR LOCATION.
  13. "HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2."
    Metzler M., Legendre-Guillemin V., Gan L., Chopra V., Kwok A., McPherson P.S., Hayden M.R.
    J. Biol. Chem. 276:39271-39276(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins."
    Mishra S.K., Agostinelli N.R., Brett T.J., Mizukami I., Ross T.S., Traub L.M.
    J. Biol. Chem. 276:46230-46236(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain."
    Legendre-Guillemin V., Metzler M., Charbonneau M., Gan L., Chopra V., Philie J., Hayden M.R., McPherson P.S.
    J. Biol. Chem. 277:19897-19904(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLTB AND HIP1R, SUBCELLULAR LOCATION.
  16. "Huntingtin-interacting protein 1 is overexpressed in prostate and colon cancer and is critical for cellular survival."
    Rao D.S., Hyun T.S., Kumar P.D., Mizukami I.F., Rubin M.A., Lucas P.C., Sanda M.G., Ross T.S.
    J. Clin. Invest. 110:351-360(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  17. "HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-phosphoinositides via epsin N-terminal homology domains."
    Hyun T.S., Rao D.S., Saint-Dic D., Michael L.E., Kumar P.D., Bradley S.V., Mizukami I.F., Oravecz-Wilson K.I., Ross T.S.
    J. Biol. Chem. 279:14294-14306(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo."
    Chen C.-Y., Brodsky F.M.
    J. Biol. Chem. 280:6109-6117(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLTB.
  19. "Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors."
    Mills I.G., Gaughan L., Robson C., Ross T., McCracken S., Kelly J., Neal D.E.
    J. Cell Biol. 170:191-200(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56; LYS-58 AND ARG-1005.
  20. "Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1-related protein) is regulated by clathrin light chain."
    Wilbur J.D., Chen C.-Y., Manalo V., Hwang P.K., Fletterick R.J., Brodsky F.M.
    J. Biol. Chem. 283:32870-32879(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH F-ACTIN.
  21. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding."
    Ybe J.A., Mishra S., Helms S., Nix J.
    J. Mol. Biol. 367:8-15(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 474-579.
  25. "Crystal structure at 2.8 A of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI)."
    Niu Q., Ybe J.A.
    J. Mol. Biol. 375:1197-1205(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 362-474.

Entry informationi

Entry nameiHIP1_HUMAN
AccessioniPrimary (citable) accession number: O00291
Secondary accession number(s): B4E3I7
, E7ES17, O00328, Q2TB58, Q8TDL4, V5LU97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 23, 2008
Last modified: April 29, 2015
This is version 156 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The affinity of the huntingtin protein-HIP1 interaction is inversely correlated to the length of the polyglutamine tract added to the huntingtin protein in Huntington disease.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.