Reviewed, UniProtKB/Swiss-Prot O00291 (HIP1_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

HIP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1037 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.6 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
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.6 Ref.10 Ref.13 Ref.17 Ref.3 Ref.5 Ref.16 Ref.18
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.10 Ref.12 Ref.13 Ref.17 Ref.11
Tissue specificity	Ubiquitously expressed with the highest level in brain. Expression is up-regulated in prostate and colon cancer. Ref.6 Ref.14 Ref.5
Domain	The pseudo DED region (pDED) mediates the interaction with IFT57. Ref.3 Binds F-actin via the talin-like I/LWEQ domain. Ref.3
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.

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
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of caspase activity Ref.3 Inferred from direct assay. Source: MGI cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW clathrin coat assembly Ref.12 Ref.13 Inferred from direct assay. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Ref.8 Inferred from direct assay. Source: UniProtKB positive regulation of receptor-mediated endocytosis Ref.10 Ref.12 Inferred from mutant phenotype. Source: UniProtKB regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Ref.3 Inferred from direct assay. Source: MGI clathrin coated vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Ref.6 Traceable author statement. Source: ProtInc membrane fraction Ref.6 Traceable author statement. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW clathrin binding Ref.12 Inferred from direct assay. Source: MGI phosphoinositide binding Ref.15 Inferred from direct assay. Source: UniProtKB structural constituent of cytoskeleton Ref.5 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [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.

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

Amino acid modifications

Modified residue

154

1

Phosphothreonine By similarity

Natural variations

Natural variant

263

1

M → K: dbSNP rs17149023.

VAR_051032

Experimental info

Mutagenesis

56

1

K → E: Abolishes 3-phosphoinositide-binding; when associated with GLU-58. Ref.17

Mutagenesis

58

1

K → E: Abolishes 3-phosphoinositide-binding; when associated with GLU-56. Ref.17

Mutagenesis

432

1

F → G: Abolishes HIP1-induced cell death. Ref.8

Mutagenesis

1005

1

R → E: Reduces AR-induced nuclear translocation. Ref.17

Sequence conflict

89

1

A → P in AAC33564. Ref.3

Sequence conflict

245 – 251

7

KLHSCLP → EFAAAST in CAA70574. Ref.6

Sequence conflict

639 – 644

6

LNQLEE → STRPRI in CAA70574. Ref.6

Sequence conflict

688

1

L → F in AAL87037. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

1037

Helix Strand Turn

Details...

Helix

482 – 522

41

Helix

526 – 552

27

Helix

556 – 580

25

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).	FASTA	–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: 11788820] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1037, INTERACTION WITH IFT57, SUBUNIT, DOMAIN.
[4]	"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.
[5]	"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: 9140394] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-1037, INTERACTION WITH HTT, TISSUE SPECIFICITY.
[6]	"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: 9147654] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-644, FUNCTION, INTERACTION WITH HTT, TISSUE SPECIFICITY. Tissue: Brain.
[7]	"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: 9616134] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION.
[8]	"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: 11007801] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-432.
[9]	"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: 11063258] [Abstract] Cited for: ALTERNATIVE SPLICING.
[10]	"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: 11532990] [Abstract] Cited for: FUNCTION, INTERACTION WITH AP2A1; AP2A2 AND CLTC, SUBCELLULAR LOCATION.
[11]	"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: 11517213] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"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: 11577110] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"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: 11889126] [Abstract] Cited for: FUNCTION, INTERACTION WITH CLTB AND HIP1R, SUBCELLULAR LOCATION.
[14]	"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: 12163454] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[15]	"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: 14732715] [Abstract] Cited for: FUNCTION.
[16]	"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: 15533940] [Abstract] Cited for: INTERACTION WITH CLTB.
[17]	"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: 16027218] [Abstract] Cited for: FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56; LYS-58 AND ARG-1005.
[18]	"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: 18790740] [Abstract] Cited for: SUBUNIT, INTERACTION WITH F-ACTIN.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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: 17257618] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 474-579.
[21]	"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: 18155047] [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

EMBLGenBankDDBJ

AC004491 Genomic DNA. No translation available.
AC018720 Genomic DNA. No translation available.
BC110545 mRNA. Translation: AAI10546.1.
AF365404 mRNA. Translation: AAL87037.1.
AF052288 , AF052261, AF052262, AF052263, AF052264, AF052265, AF052266, AF052267, AF052268, AF052269, AF052270, AF052271, AF052272, AF052273, AF052274, AF052275, AF052276, AF052277, AF052278, AF052279, AF052280, AF052281, AF052282, AF052283, AF052284, AF052285, AF052286, AF052287 Genomic DNA. Translation: AAC33564.1.
U79734 mRNA. Translation: AAC51257.1. Different initiation.
Y09420 mRNA. Translation: CAA70574.1.

IPI

IPI00782965.

RefSeq

NP_005329.3.

UniGene

Hs.329266
Hs.619089

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:17041N.

IntAct

O00291. 4 interactions.

STRING

O00291.

Proteomic databases

PRIDE

O00291.

Genome annotation databases

Ensembl

ENST00000336926; ENSP00000336747; ENSG00000127946; Homo sapiens. [Genome view]
ENST00000404944; ENSP00000385314; ENSG00000127946; Homo sapiens. [Genome view]
ENST00000420909; ENSP00000414280; ENSG00000127946; Homo sapiens. [Genome view]
ENST00000434438; ENSP00000410300; ENSG00000127946; Homo sapiens. [Genome view]

GeneID

3092.

KEGG

hsa:3092.

UCSC

uc003uds.1. human.

Organism-specific databases

CTD

3092.

GeneCards

GC07M075001.

H-InvDB

HIX0006779.

HGNC

HGNC:4913. HIP1.

HPA

CAB015334.
CAB016402.
HPA013606.
HPA017964.

MIM

601767. gene.

PharmGKB

PA29289.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O00291.

OMA

KQELATS.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

O00291.

Bgee

O00291.

CleanEx

HS_HIP1.

Genevestigator

O00291.

GermOnline

ENSG00000127946. Homo sapiens.

Family and domain databases

InterPro

IPR011417. ANTH.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR002558. ILWEQ.
[Graphical view]

Gene3D

G3DSA:1.25.40.90. ENTH_VHS. 1 hit.

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]

PROSITE

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

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

HIP1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	September 23, 2008
Last modified:	November 3, 2009
This is version 100 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.