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O95208

- EPN2_HUMAN

UniProt

O95208 - EPN2_HUMAN

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Protein

Epsin-2

Gene
EPN2, KIAA1065
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in the formation of clathrin-coated invaginations and endocytosis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Phosphatidylinositol lipid headgroup By similarity
Binding sitei11 – 111Phosphatidylinositol lipid headgroup By similarity
Binding sitei25 – 251Phosphatidylinositol lipid headgroup By similarity
Binding sitei30 – 301Phosphatidylinositol lipid headgroup By similarity
Binding sitei63 – 631Phosphatidylinositol lipid headgroup By similarity
Binding sitei73 – 731Phosphatidylinositol lipid headgroup By similarity

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. embryonic organ development Source: Ensembl
  2. endocytosis Source: UniProtKB-KW
  3. in utero embryonic development Source: Ensembl
  4. Notch signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-2
Alternative name(s):
EPS-15-interacting protein 2
Gene namesi
Name:EPN2
Synonyms:KIAA1065
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:18639. EPN2.

Subcellular locationi

Cytoplasm. Cytoplasmic vesicleclathrin-coated vesicle
Note: In punctate structures throughout the cell, associated with clathrin-coated vesicles, and particularly concentrated in the region of the Golgi complex.1 Publication

GO - Cellular componenti

  1. clathrin coat of endocytic vesicle Source: InterPro
  2. Golgi apparatus Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38615.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 641641Epsin-2PRO_0000074516Add
BLAST

Post-translational modificationi

Ubiquitinated By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95208.
PaxDbiO95208.
PRIDEiO95208.

PTM databases

PhosphoSiteiO95208.

Miscellaneous databases

PMAP-CutDBO95208.

Expressioni

Tissue specificityi

Highest expression is found in brain. Detected at lower levels in lung and liver.1 Publication

Gene expression databases

ArrayExpressiO95208.
BgeeiO95208.
CleanExiHS_EPN2.
GenevestigatoriO95208.

Organism-specific databases

HPAiHPA049809.
HPA053360.

Interactioni

Subunit structurei

Binds EPS15 By similarity. Binds AP-2 and clathrin.

Protein-protein interaction databases

BioGridi116569. 8 interactions.
STRINGi9606.ENSP00000320543.

Structurei

3D structure databases

ProteinModelPortaliO95208.
SMRiO95208. Positions 1-144.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 144133ENTHAdd
BLAST
Repeati275 – 29420UIM 1Add
BLAST
Repeati300 – 31920UIM 2Add
BLAST
Repeati352 – 35431
Repeati364 – 36632
Repeati377 – 37933
Repeati391 – 39334
Repeati409 – 41135
Repeati427 – 42936
Repeati537 – 53931
Repeati552 – 55432
Repeati637 – 63933

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni352 – 6392886 X 3 AA repeats of [DE]-P-WAdd
BLAST
Regioni537 – 6391033 X 3 AA repeats of N-P-FAdd
BLAST

Domaini

The NPF repeat domain is involved in EPS15 binding.
The DPW repeat domain is involved in AP-2 and clathrin binding.

Sequence similaritiesi

Belongs to the epsin family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG263730.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiO95208.
KOiK12471.
OMAiQEYGKSG.
OrthoDBiEOG7F511Z.
PhylomeDBiO95208.
TreeFamiTF313361.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR027319. Epsin-2_metazoa.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PANTHERiPTHR12276:SF50. PTHR12276:SF50. 1 hit.
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95208-1) [UniParc]FASTAAdd to Basket

Also known as: 2b

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.

« Hide

MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV    50
VAFSEIMSMV WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI 100
FAIQTLKDFQ YIDRDGKDQG INVREKSKQL VALLKDEERL KAERAQALKT 150
KERMAQVATG MGSNQITFGR GSSQPNLSTS HSEQEYGKAG GSPASYHGSP 200
EASLCPQHRT GAPLGQSEEL QPLSQRHPFL PHLGLASRPN GDWSQPCLTC 250
DRAARATSPR VSSELEQARP QTSGEEELQL QLALAMSREV AEQEERLRRG 300
DDLRLQMALE ESRRDTVKIP KKKEHGSLPQ QTTLLDLMDA LPSSGPAAQK 350
AEPWGPSAST NQTNPWGGPA APASTSDPWP SFGTKPAASI DPWGVPTGAT 400
VQSVPKNSDP WAASQQPASS AGKRASDAWG AVSTTKPVSV SGSFELFSNL 450
NGTIKDDFSE FDNLRTSKKT AESVTSLPSQ NNGTTSPDPF ESQPLTVASS 500
KPSSARKTPE SFLGPNAALV NLDSLVTRPA PPAQSLNPFL APGAPATSAP 550
VNPFQVNQPQ PLTLNQLRGS PVLGTSTSFG PGPGVESMAV ASMTSAAPQP 600
ALGATGSSLT PLGPAMMNMV GSVGIPPSAA QATGTTNPFL L 641
Length:641
Mass (Da):68,482
Last modified:December 16, 2008 - v3
Checksum:i0BE24CBD824F357A
GO
Isoform 2 (identifier: O95208-2) [UniParc]FASTAAdd to Basket

Also known as: 2a

The sequence of this isoform differs from the canonical sequence as follows:
     200-256: Missing.

Note: Contains a phosphoserine at position 192. Contains a phosphoserine at position 195.

Show »
Length:584
Mass (Da):62,300
Checksum:iD668242ECACD26EF
GO
Isoform 3 (identifier: O95208-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     200-256: Missing.

Note: No experimental confirmation available. Contains a phosphoserine at position 153. Contains a phosphoserine at position 156.

Show »
Length:545
Mass (Da):57,919
Checksum:iC8D6661429926997
GO
Isoform 4 (identifier: O95208-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-285: Missing.

Note: No experimental confirmation available.

Show »
Length:356
Mass (Da):36,729
Checksum:iEF6741C03E5744A3
GO

Sequence cautioni

The sequence BAA83017.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAG52540.1 differs from that shown. Reason: Erroneous termination at position 324. Translated as Glu.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti401 – 4011V → A.5 Publications
Corresponds to variant rs6587220 [ dbSNP | Ensembl ].
VAR_053080
Natural varianti531 – 5311P → T.
Corresponds to variant rs1062727 [ dbSNP | Ensembl ].
VAR_047923
Natural varianti532 – 5321P → T.
Corresponds to variant rs1062727 [ dbSNP | Ensembl ].
VAR_053081

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 285285Missing in isoform 4. VSP_047003Add
BLAST
Alternative sequencei1 – 3939Missing in isoform 3. VSP_009154Add
BLAST
Alternative sequencei200 – 25657Missing in isoform 2 and isoform 3. VSP_009155Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561A → AS in AAC78609. 1 Publication
Sequence conflicti547 – 5471T → N in AAC78608. 1 Publication
Sequence conflicti547 – 5471T → N in AAC78609. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF062084 mRNA. Translation: AAC78608.1.
AF062085 mRNA. Translation: AAC78609.1.
AB028988 mRNA. Translation: BAA83017.2. Different initiation.
AK001996 mRNA. Translation: BAG51000.1.
AK024115 mRNA. Translation: BAB14831.1.
AK092366 mRNA. Translation: BAG52540.1. Sequence problems.
AC106017 Genomic DNA. No translation available.
AC124066 Genomic DNA. No translation available.
CH471212 Genomic DNA. Translation: EAW50876.1.
BC093972 mRNA. Translation: AAH93972.1.
BC093974 mRNA. Translation: AAH93974.1.
CCDSiCCDS11203.1. [O95208-1]
CCDS11204.1. [O95208-2]
CCDS42277.1. [O95208-5]
RefSeqiNP_001096134.1. NM_001102664.1. [O95208-5]
NP_055779.2. NM_014964.4. [O95208-1]
NP_683723.2. NM_148921.3. [O95208-2]
UniGeneiHs.743983.

Genome annotation databases

EnsembliENST00000314728; ENSP00000320543; ENSG00000072134. [O95208-1]
ENST00000347697; ENSP00000261495; ENSG00000072134. [O95208-2]
ENST00000395618; ENSP00000378980; ENSG00000072134. [O95208-5]
ENST00000395620; ENSP00000378982; ENSG00000072134. [O95208-2]
GeneIDi22905.
KEGGihsa:22905.
UCSCiuc002gvd.4. human. [O95208-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF062084 mRNA. Translation: AAC78608.1 .
AF062085 mRNA. Translation: AAC78609.1 .
AB028988 mRNA. Translation: BAA83017.2 . Different initiation.
AK001996 mRNA. Translation: BAG51000.1 .
AK024115 mRNA. Translation: BAB14831.1 .
AK092366 mRNA. Translation: BAG52540.1 . Sequence problems.
AC106017 Genomic DNA. No translation available.
AC124066 Genomic DNA. No translation available.
CH471212 Genomic DNA. Translation: EAW50876.1 .
BC093972 mRNA. Translation: AAH93972.1 .
BC093974 mRNA. Translation: AAH93974.1 .
CCDSi CCDS11203.1. [O95208-1 ]
CCDS11204.1. [O95208-2 ]
CCDS42277.1. [O95208-5 ]
RefSeqi NP_001096134.1. NM_001102664.1. [O95208-5 ]
NP_055779.2. NM_014964.4. [O95208-1 ]
NP_683723.2. NM_148921.3. [O95208-2 ]
UniGenei Hs.743983.

3D structure databases

ProteinModelPortali O95208.
SMRi O95208. Positions 1-144.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116569. 8 interactions.
STRINGi 9606.ENSP00000320543.

PTM databases

PhosphoSitei O95208.

Proteomic databases

MaxQBi O95208.
PaxDbi O95208.
PRIDEi O95208.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314728 ; ENSP00000320543 ; ENSG00000072134 . [O95208-1 ]
ENST00000347697 ; ENSP00000261495 ; ENSG00000072134 . [O95208-2 ]
ENST00000395618 ; ENSP00000378980 ; ENSG00000072134 . [O95208-5 ]
ENST00000395620 ; ENSP00000378982 ; ENSG00000072134 . [O95208-2 ]
GeneIDi 22905.
KEGGi hsa:22905.
UCSCi uc002gvd.4. human. [O95208-1 ]

Organism-specific databases

CTDi 22905.
GeneCardsi GC17P019118.
H-InvDB HIX0013614.
HGNCi HGNC:18639. EPN2.
HPAi HPA049809.
HPA053360.
MIMi 607263. gene.
neXtProti NX_O95208.
PharmGKBi PA38615.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263730.
HOGENOMi HOG000008298.
HOVERGENi HBG006690.
InParanoidi O95208.
KOi K12471.
OMAi QEYGKSG.
OrthoDBi EOG7F511Z.
PhylomeDBi O95208.
TreeFami TF313361.

Miscellaneous databases

ChiTaRSi EPN2. human.
GeneWikii EPN2.
GenomeRNAii 22905.
NextBioi 43557.
PMAP-CutDB O95208.
PROi O95208.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95208.
Bgeei O95208.
CleanExi HS_EPN2.
Genevestigatori O95208.

Family and domain databases

Gene3Di 1.25.40.90. 1 hit.
InterProi IPR008942. ENTH_VHS.
IPR027319. Epsin-2_metazoa.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view ]
PANTHERi PTHR12276:SF50. PTHR12276:SF50. 1 hit.
Pfami PF01417. ENTH. 1 hit.
[Graphical view ]
SMARTi SM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view ]
SUPFAMi SSF48464. SSF48464. 1 hit.
PROSITEi PS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module."
    Rosenthal J.A., Chen H., Slepnev V.I., Pellegrini L., Salcini A.E., Di Fiore P.P., De Camilli P.
    J. Biol. Chem. 274:33959-33965(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH AP-2 AND CLATHRIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ALA-401.
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-401.
    Tissue: Brain.
  3. "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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-467 (ISOFORM 3), VARIANT ALA-401.
    Tissue: Embryo, Fetal brain and Placenta.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-401.
  6. "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], VARIANT ALA-401.
    Tissue: Brain.
  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 SER-192 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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-192 AND SER-195 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-156 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEPN2_HUMAN
AccessioniPrimary (citable) accession number: O95208
Secondary accession number(s): A8MTV8
, B3KRX8, E9PBC2, O95207, Q52LD0, Q9H7Z2, Q9UPT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 16, 2008
Last modified: September 3, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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