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Q9Y6I3 (EPN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epsin-1
Alternative name(s):
EH domain-binding mitotic phosphoprotein
EPS-15-interacting protein 1
Gene names
Name:EPN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length576 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). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations By similarity. Regulates receptor-mediated endocytosis. Ref.1

Subunit structure

Monomer. Binds clathrin, ZBTB16/ZNF145 and ITSN1. Binds ubiquitinated proteins By similarity. Binds REPS2, EPS15, AP2A1 and AP2A2. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1. Ref.1 Ref.5 Ref.6 Ref.8

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Membraneclathrin-coated pit By similarity. Note: Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 By similarity.

Domain

The NPF repeat domain is involved in EPS15 binding.

The DPW repeat domain is involved in AP2A2 and clathrin binding.

The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction with the AP-2 complex subunit AP2B1 By similarity.

Post-translational modification

Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. Ref.5

Ubiquitinated By similarity.

Sequence similarities

Belongs to the epsin family.

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

Contains 3 UIM (ubiquitin-interacting motif) repeats.

Sequence caution

Isoform 2: The sequence AAD38326.1 differs from that shown. Reason: Frameshift at position 98.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6I3-2)

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: Q9Y6I3-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGDQSWLWNQ...CPLLLQPGTM
     202-226: Missing.
Isoform 3 (identifier: Q9Y6I3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     202-226: Missing.
     393-393: Missing.
Note: May be due to a competing donor splice site. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576Epsin-1
PRO_0000074513

Regions

Domain12 – 144133ENTH
Repeat183 – 20220UIM 1
Repeat208 – 22720UIM 2
Repeat233 – 25220UIM 3
Repeat274 – 27631
Repeat294 – 29632
Repeat306 – 30833
Repeat319 – 32134
Repeat332 – 33435
Repeat349 – 35136
Repeat367 – 36937
Repeat377 – 37938
Repeat502 – 50431
Repeat518 – 52032
Repeat572 – 57433
Region274 – 3791068 X 3 AA repeats of [ED]-P-W
Region502 – 574733 X 3 AA repeats of N-P-F
Motif402 – 41110[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif
Compositional bias267 – 573307Ala/Gly/Pro-rich

Sites

Binding site81Phosphatidylinositol lipid headgroup By similarity
Binding site111Phosphatidylinositol lipid headgroup By similarity
Binding site251Phosphatidylinositol lipid headgroup By similarity
Binding site301Phosphatidylinositol lipid headgroup By similarity
Binding site631Phosphatidylinositol lipid headgroup By similarity
Binding site731Phosphatidylinositol lipid headgroup By similarity

Amino acid modifications

Modified residue3821Phosphoserine; by CDK1 Ref.5
Modified residue4191Phosphoserine Ref.12
Modified residue4201Phosphoserine Ref.12
Modified residue4351Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue4541Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13
Modified residue4601Phosphothreonine Ref.9 Ref.11 Ref.12 Ref.13
Modified residue4701Phosphothreonine Ref.12
Modified residue4941Phosphothreonine Ref.7 Ref.11 Ref.13

Natural variations

Alternative sequence11M → MGDQSWLWNQAAPGVRSPVF ACSVEKGNVPLVLSEHLAHS RDPGSGAVRFLISPEPWASA ILGTSGLLASPVLPAALDAV TCQHLPQPSSGSRPISPRIG ALCPLLLQPGTM in isoform 2.
VSP_041010
Alternative sequence202 – 22625Missing in isoform 2 and isoform 3.
VSP_041011
Alternative sequence3931Missing in isoform 3.
VSP_041012

Experimental info

Mutagenesis3821S → A: Abolishes phosphorylation by CDK1. Ref.5
Mutagenesis3821S → D: Abolishes phosphorylation by CDK1 and reduces REPS2 binding. Ref.5
Mutagenesis4041F → A: Reduces interaction with AP2B1. Ref.8

Secondary structure

................ 576
Helix Strand Turn

Details...

Sequences

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

Last modified May 3, 2011. Version 2.
Checksum: 68DD433F3168E975

FASTA57660,293
        10         20         30         40         50         60 
MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV VAFSEIMSMI 

        70         80         90        100        110        120 
WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM YAVQTLKDFQ YVDRDGKDQG 

       130        140        150        160        170        180 
VNVREKAKQL VALLRDEDRL REERAHALKT KEKLAQTATA SSAAVGSGPP PEAEQAWPQS 

       190        200        210        220        230        240 
SGEEELQLQL ALAMSKEEAD QPPSCGPEDD AQLQLALSLS REEHDKEERI RRGDDLRLQM 

       250        260        270        280        290        300 
AIEESKRETG GKEESSLMDL ADVFTAPAPA PTTDPWGGPA PMAAAVPTAA PTSDPWGGPP 

       310        320        330        340        350        360 
VPPAADPWGG PAPTPASGDP WRPAAPAGPS VDPWGGTPAP AAGEGPTPDP WGSSDGGVPV 

       370        380        390        400        410        420 
SGPSASDPWT PAPAFSDPWG GSPAKPSTNG TTAAGGFDTE PDEFSDFDRL RTALPTSGSS 

       430        440        450        460        470        480 
AGELELLAGE VPARSPGAFD MSGVRGSLAE AVGSPPPAAT PTPTPPTRKT PESFLGPNAA 

       490        500        510        520        530        540 
LVDLDSLVSR PGPTPPGAKA SNPFLPGGGP ATGPSVTNPF QPAPPATLTL NQLRLSPVPP 

       550        560        570 
VPGAPPTYIS PLGGGPGLPP MMPPGPPAPN TNPFLL 

« Hide

Isoform 2 [UniParc].

Checksum: BE8DD37499E2DB6A
Show »

FASTA66269,040
Isoform 3 [UniParc].

Checksum: DC8BA5EBEB1D5111
Show »

FASTA55057,504

References

« Hide 'large scale' references
[1]"Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis."
Morinaka K., Koyama S., Nakashima S., Hinoi T., Okawa K., Iwamatsu A., Kikuchi A.
Oncogene 18:5915-5922(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH REPS2.
Tissue: Brain.
[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. 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] (ISOFORM 1).
Tissue: Mammary gland.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [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] (ISOFORM 3).
Tissue: Brain.
[5]"Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation."
Kariya K., Koyama S., Nakashima S., Oshiro T., Morinaka K., Kikuchi A.
J. Biol. Chem. 275:18399-18406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-382, MUTAGENESIS OF SER-382, INTERACTION WITH REPS2; EPS15 AND AP-2 ALPHA SUBUNIT.
[6]"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RALBP1.
[7]"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 THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly."
Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., Roth R., Heuser J.E., Owen D.J., Traub L.M.
Dev. Cell 10:329-342(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2B1, MUTAGENESIS OF PHE-404.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454 AND THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[11]"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-435; SER-454; THR-460 AND THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-419; SER-420; SER-435; SER-454; THR-460 AND THR-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-435; SER-454; THR-460 AND THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin."
Koshiba S., Kigawa T., Kikuchi A., Yokoyama S.
J. Struct. Funct. Genomics 2:1-8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-144.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The bubble's bend - Issue 42 of January 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF073727 mRNA. Translation: AAD38326.1. Frameshift.
AK022454 mRNA. Translation: BAB14041.1.
AC008735 Genomic DNA. No translation available.
AC010525 Genomic DNA. No translation available.
BC044651 mRNA. Translation: AAH44651.1.
CCDSCCDS46198.1. [Q9Y6I3-1]
CCDS46199.1. [Q9Y6I3-2]
CCDS46200.1. [Q9Y6I3-3]
RefSeqNP_001123543.1. NM_001130071.1. [Q9Y6I3-1]
NP_001123544.1. NM_001130072.1. [Q9Y6I3-2]
NP_037465.2. NM_013333.3. [Q9Y6I3-3]
XP_005258886.1. XM_005258829.1. [Q9Y6I3-2]
UniGeneHs.279953.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1INZNMR-A1-144[»]
ProteinModelPortalQ9Y6I3.
SMRQ9Y6I3. Positions 1-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118965. 41 interactions.
IntActQ9Y6I3. 9 interactions.
MINTMINT-110599.
STRING9606.ENSP00000406209.

PTM databases

PhosphoSiteQ9Y6I3.

Polymorphism databases

DMDM332278179.

Proteomic databases

MaxQBQ9Y6I3.
PaxDbQ9Y6I3.
PRIDEQ9Y6I3.

Protocols and materials databases

DNASU29924.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000085079; ENSP00000085079; ENSG00000063245. [Q9Y6I3-3]
ENST00000270460; ENSP00000270460; ENSG00000063245. [Q9Y6I3-2]
ENST00000411543; ENSP00000406209; ENSG00000063245. [Q9Y6I3-1]
GeneID29924.
KEGGhsa:29924.
UCSCuc002qlv.3. human. [Q9Y6I3-3]
uc002qlw.3. human. [Q9Y6I3-2]
uc002qlx.3. human. [Q9Y6I3-1]

Organism-specific databases

CTD29924.
GeneCardsGC19P056186.
H-InvDBHIX0202721.
HGNCHGNC:21604. EPN1.
HPACAB009729.
MIM607262. gene.
neXtProtNX_Q9Y6I3.
PharmGKBPA134860916.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263730.
HOGENOMHOG000008298.
HOVERGENHBG006690.
KOK12471.
OMADPWGGTQ.
OrthoDBEOG7F511Z.
TreeFamTF313361.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkQ9Y6I3.

Gene expression databases

ArrayExpressQ9Y6I3.
BgeeQ9Y6I3.
CleanExHS_EPN1.
GenevestigatorQ9Y6I3.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PfamPF01417. ENTH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]
SMARTSM00273. ENTH. 1 hit.
SM00726. UIM. 3 hits.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
PS50330. UIM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y6I3.
GeneWikiEPN1.
GenomeRNAi29924.
NextBio52535.
PROQ9Y6I3.
SOURCESearch...

Entry information

Entry nameEPN1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6I3
Secondary accession number(s): Q86ST3, Q9HA18
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 3, 2011
Last modified: July 9, 2014
This is version 134 of the entry and version 2 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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 19

Human chromosome 19: entries, gene names and cross-references to MIM