O00291 (HIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Huntingtin-interacting protein 1
Short name=HIP-1

Alternative name(s):
Huntingtin-interacting protein I
Short name=HIP-I

Gene names

Name:

HIP1

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1037 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18
Subunit structure	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. Ref.4 Ref.6 Ref.7 Ref.11 Ref.14 Ref.17 Ref.18 Ref.19
Subcellular location	Cytoplasm. Nucleus. Endomembrane system. Cytoplasmic vesicle › clathrin-coated vesicle membrane. Note: Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR. Ref.11 Ref.12 Ref.13 Ref.14 Ref.18
Tissue specificity	Ubiquitously expressed with the highest level in brain. Expression is up-regulated in prostate and colon cancer. Ref.6 Ref.7 Ref.15
Domain	The pseudo DED region (pDED) mediates the interaction with IFT57. Ref.4 Binds F-actin via the talin-like I/LWEQ domain. Ref.4
Involvement in disease	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.
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.
Sequence similarities	Belongs to the SLA2 family. Contains 1 ENTH (epsin N-terminal homology) domain. Contains 1 I/LWEQ domain.
Sequence caution	The sequence AAC51257.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Differentiation Endocytosis Transcription Transcription regulation
Cellular component	Cytoplasm Cytoplasmic vesicle Membrane Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Neurodegeneration
Domain	Coiled coil
Ligand	Actin-binding
Molecular function	Activator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay Ref.4. Source: MGI apoptotic process Inferred from direct assay Ref.4. Source: MGI apoptotic signaling pathway Inferred from direct assay Ref.9. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW clathrin coat assembly Inferred from direct assay Ref.14. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of receptor-mediated endocytosis Inferred from mutant phenotype Ref.11Ref.13. Source: UniProtKB regulation of apoptotic process Inferred from direct assay Ref.4. Source: MGI regulation of transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay Ref.4. Source: MGI clathrin-coated vesicle Inferred from direct assay Ref.12. Source: UniProtKB clathrin-coated vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay PubMed 11604514. Source: MGI cytoskeleton Traceable author statement Ref.7. Source: ProtInc intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA membrane Traceable author statement Ref.7. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	clathrin binding Inferred from direct assay Ref.13. Source: MGI phosphatidylinositol binding Inferred from direct assay Ref.16. Source: UniProtKB structural constituent of cytoskeleton Traceable author statement Ref.6. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Apaf1	Q9EPV5	2	EBI-473886,EBI-6978501	From a different organism.
HTT	P42858	4	EBI-473886,EBI-466029
Necap1	Q9CR95	3	EBI-473886,EBI-7592476	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform HIP1-1 (identifier: O00291-1)

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 HIP1-2 (identifier: O00291-2)

The sequence of this isoform is not available.

Isoform 3 (identifier: O00291-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1037

1037

Huntingtin-interacting protein 1

PRO_0000083986

Regions

Domain

32 – 160

129

ENTH

Domain

771 – 1012

242

I/LWEQ

Region

410 – 491

82

pDED

Region

867 – 924

58

Important for actin binding By similarity

Coiled coil

368 – 644

277

Potential

Natural variations

Alternative sequence

803 – 853

51

Missing in isoform 3.

VSP_044736

Natural variant

263

1

M → K.
Corresponds to variant rs17149023 [ dbSNP | Ensembl ].

VAR_051032

Experimental info

Mutagenesis

56

1

K → E: Abolishes 3-phosphoinositide-binding; when associated with E-58. Ref.18

Mutagenesis

58

1

K → E: Abolishes 3-phosphoinositide-binding; when associated with E-56. Ref.18

Mutagenesis

432

1

F → G: Abolishes HIP1-induced cell death. Ref.9

Mutagenesis

1005

1

R → E: Reduces AR-induced nuclear translocation. Ref.18

Sequence conflict

89

1

A → P in AAC33564. Ref.4

Sequence conflict

245 – 251

7

KLHSCLP → EFAAAST in CAA70574. Ref.7

Sequence conflict

357

1

S → R in BAG65499. Ref.1

Sequence conflict

639 – 644

6

LNQLEE → STRPRI in CAA70574. Ref.7

Sequence conflict

688

1

L → F in AAL87037. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

1037

Helix Strand Turn

Details...

Helix

373 – 441

69

Turn

459 – 461

3

Helix

462 – 465

4

Helix

482 – 580

99

Sequences

	Sequence		Length	Mass (Da)
	Isoform HIP1-1 [UniParc]. Last modified September 23, 2008. Version 5. Checksum: F8C0369DBF0A836F	FASTA	1,037	116,221
	10 20 30 40 50 60 MDRMASSMKQ VPNPLPKVLS RRGVGAGLEA AERESFERTQ TVSINKAINT QEVAVKEKHA 70 80 90 100 110 120 RTCILGTHHE KGAQTFWSVV NRLPLSSNAV LCWKFCHVFH KLLRDGHPNV LKDSLRYRNE 130 140 150 160 170 180 LSDMSRMWGH LSEGYGQLCS IYLKLLRTKM EYHTKNPRFP GNLQMSDRQL DEAGESDVNN 190 200 210 220 230 240 FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTAAGQC RLAPLIQVIL DCSHLYDYTV 250 260 270 280 290 300 KLLFKLHSCL PADTLQGHRD RFMEQFTKLK DLFYRSSNLQ YFKRLIQIPQ LPENPPNFLR 310 320 330 340 350 360 ASALSEHISP VVVIPAEASS PDSEPVLEKD DLMDMDASQQ NLFDNKFDDI FGSSFSSDPF 370 380 390 400 410 420 NFNSQNGVNK DEKDHLIERL YREISGLKAQ LENMKTESQR VVLQLKGHVS ELEADLAEQQ 430 440 450 460 470 480 HLRQQAADDC EFLRAELDEL RRQREDTEKA QRSLSEIERK AQANEQRYSK LKEKYSELVQ 490 500 510 520 530 540 NHADLLRKNA EVTKQVSMAR QAQVDLEREK KELEDSLERI SDQGQRKTQE QLEVLESLKQ 550 560 570 580 590 600 ELATSQRELQ VLQGSLETSA QSEANWAAEF AELEKERDSL VSGAAHREEE LSALRKELQD 610 620 630 640 650 660 TQLKLASTEE SMCQLAKDQR KMLLVGSRKA AEQVIQDALN QLEEPPLISC AGSADHLLST 670 680 690 700 710 720 VTSISSCIEQ LEKSWSQYLA CPEDISGLLH SITLLAHLTS DAIAHGATTC LRAPPEPADS 730 740 750 760 770 780 LTEACKQYGR ETLAYLASLE EEGSLENADS TAMRNCLSKI KAIGEELLPR GLDIKQEELG 790 800 810 820 830 840 DLVDKEMAAT SAAIETATAR IEEMLSKSRA GDTGVKLEVN ERILGCCTSL MQAIQVLIVA 850 860 870 880 890 900 SKDLQREIVE SGRGTASPKE FYAKNSRWTE GLISASKAVG WGATVMVDAA DLVVQGRGKF 910 920 930 940 950 960 EELMVCSHEI AASTAQLVAA SKVKADKDSP NLAQLQQASR GVNQATAGVV ASTISGKSQI 970 980 990 1000 1010 1020 EETDNMDFSS MTLTQIKRQE MDSQVRVLEL ENELQKERQK LGELRKKHYE LAGVAEGWEE 1030 GTEASPPTLQ EVVTEKE
	Isoform HIP1-2 (Sequence not available).		–	–
	Isoform 3 [UniParc]. Checksum: C09BAD680242941A	FASTA	986	110,663
	10 20 30 40 50 60 MDRMASSMKQ VPNPLPKVLS RRGVGAGLEA AERESFERTQ TVSINKAINT QEVAVKEKHA 70 80 90 100 110 120 RTCILGTHHE KGAQTFWSVV NRLPLSSNAV LCWKFCHVFH KLLRDGHPNV LKDSLRYRNE 130 140 150 160 170 180 LSDMSRMWGH LSEGYGQLCS IYLKLLRTKM EYHTKNPRFP GNLQMSDRQL DEAGESDVNN 190 200 210 220 230 240 FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTAAGQC RLAPLIQVIL DCSHLYDYTV 250 260 270 280 290 300 KLLFKLHSCL PADTLQGHRD RFMEQFTKLK DLFYRSSNLQ YFKRLIQIPQ LPENPPNFLR 310 320 330 340 350 360 ASALSEHISP VVVIPAEASS PDSEPVLEKD DLMDMDASQQ NLFDNKFDDI FGSSFSSDPF 370 380 390 400 410 420 NFNSQNGVNK DEKDHLIERL YREISGLKAQ LENMKTESQR VVLQLKGHVS ELEADLAEQQ 430 440 450 460 470 480 HLRQQAADDC EFLRAELDEL RRQREDTEKA QRSLSEIERK AQANEQRYSK LKEKYSELVQ 490 500 510 520 530 540 NHADLLRKNA EVTKQVSMAR QAQVDLEREK KELEDSLERI SDQGQRKTQE QLEVLESLKQ 550 560 570 580 590 600 ELATSQRELQ VLQGSLETSA QSEANWAAEF AELEKERDSL VSGAAHREEE LSALRKELQD 610 620 630 640 650 660 TQLKLASTEE SMCQLAKDQR KMLLVGSRKA AEQVIQDALN QLEEPPLISC AGSADHLLST 670 680 690 700 710 720 VTSISSCIEQ LEKSWSQYLA CPEDISGLLH SITLLAHLTS DAIAHGATTC LRAPPEPADS 730 740 750 760 770 780 LTEACKQYGR ETLAYLASLE EEGSLENADS TAMRNCLSKI KAIGEELLPR GLDIKQEELG 790 800 810 820 830 840 DLVDKEMAAT SAAIETATAR IEGTASPKEF YAKNSRWTEG LISASKAVGW GATVMVDAAD 850 860 870 880 890 900 LVVQGRGKFE ELMVCSHEIA ASTAQLVAAS KVKADKDSPN LAQLQQASRG VNQATAGVVA 910 920 930 940 950 960 STISGKSQIE ETDNMDFSSM TLTQIKRQEM DSQVRVLELE NELQKERQKL GELRKKHYEL 970 980 AGVAEGWEEG TEASPPTLQE VVTEKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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].
[3]	"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].
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain." Hackam A.S., Yassa A.S., Singaraja R., Metzler M., Gutekunst C.-A., Gan L., Warby S., Wellington C.L., Vaillancourt J., Chen N., Gervais F.G., Raymond L., Nicholson D.W., Hayden M.R. J. Biol. Chem. 275:41299-41308(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-432.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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.
[23]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK304738 mRNA. Translation: BAG65499.1.
AC004491 Genomic DNA. No translation available.
AC018720 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.

RefSeq

NP_001230127.1. NM_001243198.2.
NP_005329.3. NM_005338.6.

UniGene

Hs.329266.
Hs.619089.
Hs.674397.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NO2	X-ray	2.80	A	482-586	[»]
2QA7	X-ray	2.80	A/B/C/D	370-481	[»]
3I00	X-ray	2.30	A/B	361-480	[»]

ProteinModelPortal

O00291.

SMR

O00291. Positions 371-472, 481-581, 773-966.

ModBase

Search...

MobiDB

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Protein-protein interaction databases

BioGrid

109339. 15 interactions.

DIP

DIP-17041N.

IntAct

O00291. 11 interactions.

MINT

MINT-208214.

STRING

9606.ENSP00000336747.

PTM databases

PhosphoSite

O00291.

Proteomic databases

PaxDb

O00291.

PRIDE

O00291.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000336926; ENSP00000336747; ENSG00000127946. [O00291-1]
ENST00000434438; ENSP00000410300; ENSG00000127946. [O00291-3]
ENST00000575057; ENSP00000460815; ENSG00000263334. [O00291-1]
ENST00000576304; ENSP00000459517; ENSG00000263334. [O00291-3]

GeneID

3092.

KEGG

hsa:3092.

UCSC

uc003uds.2. human. [O00291-1]

Organism-specific databases

CTD

3092.

GeneCards

GC07M075162.

HGNC

HGNC:4913. HIP1.

HPA

CAB015334.
CAB016402.
HPA013606.
HPA017964.

MIM

601767. gene.

neXtProt

NX_O00291.

PharmGKB

PA29289.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG280957.

HOGENOM

HOG000020612.

HOVERGEN

HBG005968.

InParanoid

O00291.

KO

K04559.

OMA

GRGKFEE.

PhylomeDB

O00291.

TreeFam

TF316860.

Gene expression databases

ArrayExpress

O00291.

Bgee

O00291.

CleanEx

HS_HIP1.

Genevestigator

O00291.

Family and domain databases

Gene3D

1.20.1410.10. 1 hit.
1.25.40.90. 1 hit.

InterPro

IPR011417. ANTH_dom.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR002558. ILWEQ_dom.
[Graphical view]

Pfam

PF07651. ANTH. 1 hit.
PF01608. I_LWEQ. 1 hit.
[Graphical view]

ProDom

PD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00273. ENTH. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]

SUPFAM

SSF109885. SSF109885. 1 hit.
SSF48464. SSF48464. 1 hit.

PROSITE

PS50942. ENTH. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

Hip1. human.

EvolutionaryTrace

O00291.

GenomeRNAi

3092.

NextBio

12271.

PRO

O00291.

SOURCE

Search...

Entry information

Entry name

HIP1_HUMAN

Accession

Primary (citable) accession number: O00291
Secondary accession number(s): B4E3I7 , E7ES17, O00328, Q2TB58, Q8TDL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	September 23, 2008
Last modified:	April 16, 2014
This is version 145 of the entry and version 5 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.