Q14677 (EPN4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	625 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › perinuclear region. Membrane; Peripheral membrane protein. Cytoplasmic vesicle › clathrin-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.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cytoplasm Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular membrane organization Traceable author statement. Source: Reactome endocytosis Inferred from electronic annotation. Source: UniProtKB-KW post-Golgi vesicle-mediated transport Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 10942595. Source: UniProtKB clathrin-coated vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAPL1	Q9H0R8	2	EBI-1171113,EBI-746969
MAP1LC3B	Q9GZQ8	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 625

625

Clathrin interactor 1

PRO_0000074521

Regions

Domain

16 – 149

134

ENTH

Compositional bias

549 – 605

57

Met-rich

Sites

Binding site

29

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

67

1

Phosphatidylinositol lipid headgroup By similarity

Amino acid modifications

Modified residue

163

1

Phosphoserine By similarity

Modified residue

227

1

Phosphoserine Ref.11 Ref.14

Modified residue

232

1

Phosphoserine By similarity

Modified residue

234

1

Phosphoserine By similarity

Modified residue

245

1

Phosphoserine Ref.12 Ref.13 Ref.16

Modified residue

299

1

Phosphoserine Ref.12 Ref.13 Ref.15 Ref.16 Ref.18

Natural variations

Alternative sequence

1 – 18

18

Missing in isoform 2.

VSP_009160

Alternative sequence

459

1

S → SQPLQNVSTVLQKPNPLYN in isoform 3.

VSP_043302

Alternative sequence

460

1

Q → QPLQNVSTVLQKPNPLYNQ in isoform 2.

VSP_009161

Experimental info

Mutagenesis

29

1

R → L: Reduces lipid binding. Abolishes lipid binding; when associated with G-34.

Mutagenesis

34

1

D → G: Abolishes lipid binding; when associated with L-29. Ref.9

Mutagenesis

349

1

D → R: Decreases AP-1 and AP-2 binding. Ref.9

Mutagenesis

371

1

D → R: Slightly decreases AP-1 binding. Ref.9

Mutagenesis

422

1

D → R: Strongly decreases clathrin binding. Ref.9

Mutagenesis

423 – 426

4

LFDL → AFAA: Strongly reduces clathrin binding. Ref.8

Sequence conflict

476

1

T → A in BAC03971. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

625

Helix Strand Turn

Details...

Helix

23 – 31

9

Beta strand

33 – 37

5

Helix

41 – 50

10

Turn

54 – 56

3

Helix

57 – 69

13

Helix

76 – 92

17

Helix

95 – 103

9

Helix

105 – 109

5

Helix

110 – 113

4

Helix

125 – 139

15

Helix

142 – 151

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6C8C6689861E9F0D	FASTA	625	68,259
	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
	Isoform 2 [UniParc]. Checksum: 5081B36E2F4F85F2	FASTA	625	68,166
	10 20 30 40 50 60 MNYSEIESKV REATNDDPWG PSGQLMGEIA KATFMYEQFP ELMNMLWSRM LKDNKKNWRR 70 80 90 100 110 120 VYKSLLLLAY LIRNGSERVV TSAREHIYDL RSLENYHFVD EHGKDQGINI RQKVKELVEF 130 140 150 160 170 180 AQDDDRLREE RKKAKKNKDK YVGVSSDSVG GFRYSERYDP EPKSKWDEEW DKNKSAFPFS 190 200 210 220 230 240 DKLGELSDKI GSTIDDTISK FRRKDREDSP ERCSDSDEEK KARRGRSPKG EFKDEEETVT 250 260 270 280 290 300 TKHIHITQAT ETTTTRHKRT ANPSKTIDLG AAAHYTGDKA SPDQNASTHT PQSSVKTSVP 310 320 330 340 350 360 SSKSSGDLVD LFDGTSQSTG GSADLFGGFA DFGSAAASGS FPSQVTATSG NGDFGDWSAF 370 380 390 400 410 420 NQAPSGPVAS SGEFFGSASQ PAVELVSGSQ SALGPPPAAS NSSDLFDLMG SSQATMTSSQ 430 440 450 460 470 480 SMNFSMMSTN TVGLGLPMSR SQPLQNVSTV LQKPNPLYNQ 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
	Isoform 3 [UniParc]. Checksum: FD6381C2E1957E9C	FASTA	643	70,295
	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 PLQNVSTVLQ KPNPLYNQNT 490 500 510 520 530 540 DMVQKSVSKT LPSTWSDPSV NISLDNLLPG MQPSKPQQPS LNTMIQQQNM QQPMNVMTQS 550 560 570 580 590 600 FGAVNLSSPS NMLPVRPQTN ALIGGPMPMS MPNVMTGTMG MAPLGNTPMM NQSMMGMNMN 610 620 630 640 IGMSAAGMGL TGTMGMGMPN IAMTSGTVQP KQDAFANFAN FSK

References

	« Hide 'large scale' referencesShow '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), 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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"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, MASS SPECTROMETRY.
+	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.

IPI

IPI00291930.
IPI00397519.
IPI00975549.

RefSeq

NP_001182484.1. NM_001195555.1.
NP_001182485.1. NM_001195556.1.
NP_055481.1. NM_014666.3.

UniGene

Hs.644000.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XGW	X-ray	1.90	A	1-165	[»]
2QY7	X-ray	2.00	A/B/C	20-166	[»]
2V8S	X-ray	2.22	E	20-166	[»]

ProteinModelPortal

Q14677.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14677. 17 interactions.

STRING

9606.ENSP00000388340.

PTM databases

PhosphoSite

Q14677.

Polymorphism databases

DMDM

41016993.

Proteomic databases

PaxDb

Q14677.

PRIDE

Q14677.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296951; ENSP00000296951; ENSG00000113282.
ENST00000411809; ENSP00000388340; ENSG00000113282.
ENST00000523094; ENSP00000429345; ENSG00000113282.
ENST00000523908; ENSP00000429824; ENSG00000113282.
ENST00000530742; ENSP00000433419; ENSG00000113282.

GeneID

9685.

KEGG

hsa:9685.

UCSC

uc003lxi.2. human.
uc003lxj.2. human.

Organism-specific databases

CTD

9685.

GeneCards

GC05M157212.

HGNC

HGNC:23186. CLINT1.

HPA

HPA043280.

MIM

607265. gene.

neXtProt

NX_Q14677.

Orphanet

3140. Schizophrenia.

PharmGKB

PA145149115.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290795.

HOGENOM

HOG000082415.

HOVERGEN

HBG048921.

InParanoid

Q14677.

OMA

ELMNMLW.

OrthoDB

EOG4BK53R.

PhylomeDB

Q14677.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

Bgee

Q14677.

CleanEx

HS_CLINT1.

Genevestigator

Q14677.

GermOnline

ENSG00000113282. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.90. 1 hit.

InterPro

IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
[Graphical view]

Pfam

PF01417. ENTH. 1 hit.
[Graphical view]

SMART

SM00273. ENTH. 1 hit.
[Graphical view]

SUPFAM

SSF48464. ENTH_VHS. 1 hit.

PROSITE

PS50942. ENTH. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

CLINT1. human.

EvolutionaryTrace

Q14677.

GenomeRNAi

9685.

NextBio

36372.

SOURCE

Search...

Entry information

Entry name

EPN4_HUMAN

Accession

Primary (citable) accession number: Q14677
Secondary accession number(s): B7Z6F8 , D3DQJ6, Q8NAF1, Q96E05

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 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.