Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q14677 (EPN4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Clathrin interactor 1
Alternative name(s):
Clathrin-interacting protein localized in the trans-Golgi region
Short name=Clint
Enthoprotin
Epsin-4
Epsin-related protein
Short name=EpsinR
Gene names
Name:CLINT1
Synonyms:ENTH, EPN4, EPNR, KIAA0171
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. Ref.8 Ref.9

Subunit structure

Binds clathrin heavy chain, GGA2, AP-2 and AP1G1.

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Membrane; Peripheral membrane protein. Cytoplasmic vesicleclathrin-coated vesicle. Note: Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network. Ref.1 Ref.8 Ref.9

Tissue specificity

Ubiquitously expressed at low to intermediate levels. Ref.8 Ref.9

Polymorphism

Genetic variations in CLINT1 may contribute to susceptibility to schizophrenia and psychotic disorders in some populations.

Sequence similarities

Belongs to the epsin family.

Contains 1 ENTH (epsin N-terminal homology) domain.

Sequence caution

The sequence BAA11488.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ap1g1P2289210EBI-1171113,EBI-1040262From a different organism.
GABARAPL1Q9H0R82EBI-1171113,EBI-746969
MAP1LC3BQ9GZQ82EBI-1171113,EBI-373144

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14677-1)

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: Q14677-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.
     460-460: Q → QPLQNVSTVLQKPNPLYNQ
Isoform 3 (identifier: Q14677-3)

The sequence of this isoform differs from the canonical sequence as follows:
     459-459: S → SQPLQNVSTVLQKPNPLYN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 625625Clathrin interactor 1
PRO_0000074521

Regions

Domain16 – 149134ENTH
Compositional bias549 – 60557Met-rich

Sites

Binding site291Phosphatidylinositol lipid headgroup By similarity
Binding site671Phosphatidylinositol lipid headgroup By similarity

Amino acid modifications

Modified residue1631Phosphoserine By similarity
Modified residue2271Phosphoserine Ref.11 Ref.14
Modified residue2451Phosphoserine Ref.12 Ref.13 Ref.17
Modified residue2991Phosphoserine Ref.12 Ref.13 Ref.16 Ref.17 Ref.19

Natural variations

Alternative sequence1 – 1818Missing in isoform 2.
VSP_009160
Alternative sequence4591S → SQPLQNVSTVLQKPNPLYN in isoform 3.
VSP_043302
Alternative sequence4601Q → QPLQNVSTVLQKPNPLYNQ in isoform 2.
VSP_009161

Experimental info

Mutagenesis291R → L: Reduces lipid binding. Abolishes lipid binding; when associated with G-34.
Mutagenesis341D → G: Abolishes lipid binding; when associated with L-29. Ref.9
Mutagenesis3491D → R: Decreases AP-1 and AP-2 binding. Ref.9
Mutagenesis3711D → R: Slightly decreases AP-1 binding. Ref.9
Mutagenesis4221D → R: Strongly decreases clathrin binding. Ref.9
Mutagenesis423 – 4264LFDL → AFAA: Strongly reduces clathrin binding. Ref.8
Sequence conflict4761T → A in BAC03971. Ref.4

Secondary structure

..................... 625
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6C8C6689861E9F0D

FASTA62568,259
        10         20         30         40         50         60 
MLNMWKVREL VDKATNVVMN YSEIESKVRE ATNDDPWGPS GQLMGEIAKA TFMYEQFPEL 

        70         80         90        100        110        120 
MNMLWSRMLK DNKKNWRRVY KSLLLLAYLI RNGSERVVTS AREHIYDLRS LENYHFVDEH 

       130        140        150        160        170        180 
GKDQGINIRQ KVKELVEFAQ DDDRLREERK KAKKNKDKYV GVSSDSVGGF RYSERYDPEP 

       190        200        210        220        230        240 
KSKWDEEWDK NKSAFPFSDK LGELSDKIGS TIDDTISKFR RKDREDSPER CSDSDEEKKA 

       250        260        270        280        290        300 
RRGRSPKGEF KDEEETVTTK HIHITQATET TTTRHKRTAN PSKTIDLGAA AHYTGDKASP 

       310        320        330        340        350        360 
DQNASTHTPQ SSVKTSVPSS KSSGDLVDLF DGTSQSTGGS ADLFGGFADF GSAAASGSFP 

       370        380        390        400        410        420 
SQVTATSGNG DFGDWSAFNQ APSGPVASSG EFFGSASQPA VELVSGSQSA LGPPPAASNS 

       430        440        450        460        470        480 
SDLFDLMGSS QATMTSSQSM NFSMMSTNTV GLGLPMSRSQ NTDMVQKSVS KTLPSTWSDP 

       490        500        510        520        530        540 
SVNISLDNLL PGMQPSKPQQ PSLNTMIQQQ NMQQPMNVMT QSFGAVNLSS PSNMLPVRPQ 

       550        560        570        580        590        600 
TNALIGGPMP MSMPNVMTGT MGMAPLGNTP MMNQSMMGMN MNIGMSAAGM GLTGTMGMGM 

       610        620 
PNIAMTSGTV QPKQDAFANF ANFSK 

« Hide

Isoform 2 [UniParc].

Checksum: 5081B36E2F4F85F2
Show »

FASTA62568,166
Isoform 3 [UniParc].

Checksum: FD6381C2E1957E9C
Show »

FASTA64370,295

References

« Hide 'large scale' references
[1]"Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics."
Wasiak S., Legendre-Guillemin V., Puertollano R., Blondeau F., Girard M., de Heuvel E., Boismenu D., Bell A.W., Bonifacino J.S., McPherson P.S.
J. Cell Biol. 158:855-862(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 14-27; 30-49; 110-129; 134-146; 157-171; 201-218; 248-274 AND 284-297 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CLATHRIN; AP1G1 AND GGA2, SUBCELLULAR LOCATION.
[2]"KIAA0171 as a new member (epsin 4) of the epsin family."
Hong W.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[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. expand/collapse author list , 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 2 AND 3).
Tissue: Placenta and Small intestine.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Lung and Skin.
[8]"Clint: a novel clathrin-binding ENTH-domain protein at the Golgi."
Kalthoff C., Groos S., Kohl R., Mahrhold S., Ungewickell E.J.
Mol. Biol. Cell 13:4060-4073(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 423-LEU--LEU-426, INTERACTION WITH CLATHRIN; AP1G1 AND AP-2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[9]"EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking."
Mills I.G., Praefcke G.J.K., Vallis Y., Peter B.J., Olesen L.E., Gallop J.L., Butler P.J.G., Evans P.R., McMahon H.T.
J. Cell Biol. 160:213-222(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-34; ASP-349; ASP-371 AND ASP-422, INTERACTION WITH AP1G1; AP-2 AND CLATHRIN.
[10]"The Epsin 4 gene on chromosome 5q, which encodes the clathrin-associated protein enthoprotin, is involved in the genetic susceptibility to schizophrenia."
Pimm J., McQuillin A., Thirumalai S., Lawrence J., Quested D., Bass N., Lamb G., Moorey H., Datta S.R., Kalsi G., Badacsonyi A., Kelly K., Morgan J., Punukollu B., Curtis D., Gurling H.
Am. J. Hum. Genet. 76:902-907(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN SCZD1.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BK000414 Genomic DNA. Translation: DAA00062.1.
AF434813 mRNA. Translation: AAL30768.1.
D79993 mRNA. Translation: BAA11488.2. Different initiation.
AK092765 mRNA. Translation: BAC03971.1.
AK300257 mRNA. Translation: BAH13244.1.
AC011394 Genomic DNA. No translation available.
AC026407 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61585.1.
CH471062 Genomic DNA. Translation: EAW61588.1.
BC004467 mRNA. Translation: AAH04467.1.
BC013091 mRNA. Translation: AAH13091.1.
RefSeqNP_001182484.1. NM_001195555.1.
NP_001182485.1. NM_001195556.1.
NP_055481.1. NM_014666.3.
UniGeneHs.644000.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XGWX-ray1.90A1-165[»]
2QY7X-ray2.00A/B/C20-166[»]
2V8SX-ray2.22E20-166[»]
ProteinModelPortalQ14677.
SMRQ14677. Positions 17-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115038. 31 interactions.
DIPDIP-45604N.
IntActQ14677. 20 interactions.
MINTMINT-4999242.
STRING9606.ENSP00000388340.

PTM databases

PhosphoSiteQ14677.

Polymorphism databases

DMDM41016993.

Proteomic databases

PaxDbQ14677.
PRIDEQ14677.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296951; ENSP00000296951; ENSG00000113282. [Q14677-2]
ENST00000411809; ENSP00000388340; ENSG00000113282. [Q14677-1]
ENST00000523094; ENSP00000429345; ENSG00000113282. [Q14677-2]
ENST00000523908; ENSP00000429824; ENSG00000113282. [Q14677-3]
ENST00000530742; ENSP00000433419; ENSG00000113282. [Q14677-2]
GeneID9685.
KEGGhsa:9685.
UCSCuc003lxi.2. human. [Q14677-2]
uc003lxj.2. human. [Q14677-1]
uc011ddv.2. human. [Q14677-3]

Organism-specific databases

CTD9685.
GeneCardsGC05M157212.
HGNCHGNC:23186. CLINT1.
HPAHPA043280.
MIM607265. gene.
neXtProtNX_Q14677.
Orphanet3140. Schizophrenia.
PharmGKBPA145149115.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290795.
HOGENOMHOG000082415.
HOVERGENHBG048921.
InParanoidQ14677.
OMAPMSRSQP.
OrthoDBEOG73V6K0.
PhylomeDBQ14677.
TreeFamTF313361.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

BgeeQ14677.
CleanExHS_CLINT1.
GenevestigatorQ14677.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
[Graphical view]
PfamPF01417. ENTH. 1 hit.
[Graphical view]
SMARTSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLINT1. human.
EvolutionaryTraceQ14677.
GeneWikiCLINT1.
GenomeRNAi9685.
NextBio36372.
PROQ14677.
SOURCESearch...

Entry information

Entry nameEPN4_HUMAN
AccessionPrimary (citable) accession number: Q14677
Secondary accession number(s): B7Z6F8 expand/collapse secondary AC list , D3DQJ6, Q8NAF1, Q96E05
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM