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Protein

Epidermal growth factor receptor kinase substrate 8-like protein 2

Gene

EPS8L2

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

Functioni

Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton.1 Publication

GO - Molecular functioni

  1. actin binding Source: UniProtKB

GO - Biological processi

  1. positive regulation of Rac GTPase activity Source: GOC
  2. positive regulation of Rho GTPase activity Source: GOC
  3. positive regulation of ruffle assembly Source: UniProtKB
  4. regulation of Rho protein signal transduction Source: UniProtKB
  5. Rho protein signal transduction Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor kinase substrate 8-like protein 2
Short name:
EPS8-like protein 2
Alternative name(s):
Epidermal growth factor receptor pathway substrate 8-related protein 2
Short name:
EPS8-related protein 2
Gene namesi
Name:EPS8L2
Synonyms:EPS8R2
ORF Names:PP13181
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:21296. EPS8L2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProtKB
  3. plasma membrane Source: HPA
  4. protein complex Source: UniProtKB
  5. ruffle membrane Source: UniProtKB
  6. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134981048.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Epidermal growth factor receptor kinase substrate 8-like protein 2PRO_0000239084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei303 – 3031PhosphothreonineBy similarity
Modified residuei449 – 4491Phosphoserine1 Publication
Modified residuei469 – 4691Phosphothreonine1 Publication
Modified residuei570 – 5701Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H6S3.
PaxDbiQ9H6S3.
PRIDEiQ9H6S3.

PTM databases

PhosphoSiteiQ9H6S3.

Expressioni

Tissue specificityi

Detected in fibroblasts and placenta.1 Publication

Gene expression databases

BgeeiQ9H6S3.
CleanExiHS_EPS8L2.
ExpressionAtlasiQ9H6S3. baseline and differential.
GenevestigatoriQ9H6S3.

Organism-specific databases

HPAiHPA041143.

Interactioni

Subunit structurei

Interacts with ABI1. Part of a complex that contains SOS1, ABI1 and EPS8L2. Associates with F-actin.1 Publication

Protein-protein interaction databases

BioGridi122297. 6 interactions.
IntActiQ9H6S3. 6 interactions.
MINTiMINT-5002000.
STRINGi9606.ENSP00000320828.

Structurei

Secondary structure

1
715
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi506 – 5105Combined sources
Beta strandi518 – 5236Combined sources
Beta strandi525 – 5328Combined sources
Beta strandi538 – 5425Combined sources
Turni543 – 5453Combined sources
Helixi630 – 64011Combined sources
Helixi646 – 6494Combined sources
Helixi655 – 6595Combined sources
Helixi663 – 6708Combined sources
Turni671 – 6733Combined sources
Helixi674 – 68916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWUNMR-A612-697[»]
1WXBNMR-A495-549[»]
ProteinModelPortaliQ9H6S3.
SMRiQ9H6S3. Positions 46-175, 494-555, 612-697.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H6S3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 202157PIDPROSITE-ProRule annotationAdd
BLAST
Domaini492 – 55160SH3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the EPS8 family.Curated
Contains 1 PID domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG263108.
GeneTreeiENSGT00390000003646.
HOVERGENiHBG003090.
InParanoidiQ9H6S3.
KOiK17277.
OMAiERSQPVH.
OrthoDBiEOG7TMZR9.
PhylomeDBiQ9H6S3.
TreeFamiTF313069.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H6S3-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MSQSGAVSCC PGATNGSLGR SDGVAKMSPK DLFEQRKKYS NSNVIMHETS
60 70 80 90 100
QYHVQHLATF IMDKSEAITS VDDAIRKLVQ LSSKEKIWTQ EMLLQVNDQS
110 120 130 140 150
LRLLDIESQE ELEDFPLPTV QRSQTVLNQL RYPSVLLLVC QDSEQSKPDV
160 170 180 190 200
HFFHCDEVEA ELVHEDIESA LADCRLGKKM RPQTLKGHQE KIRQRQSILP
210 220 230 240 250
PPQGPAPIPF QHRGGDSPEA KNRVGPQVPL SEPGFRRRES QEEPRAVLAQ
260 270 280 290 300
KIEKETQILN CALDDIEWFV ARLQKAAEAF KQLNQRKKGK KKGKKAPAEG
310 320 330 340 350
VLTLRARPPS EGEFIDCFQK IKLAINLLAK LQKHIQNPSA AELVHFLFGP
360 370 380 390 400
LDLIVNTCSG PDIARSVSCP LLSRDAVDFL RGHLVPKEMS LWESLGESWM
410 420 430 440 450
RPRSEWPREP QVPLYVPKFH SGWEPPVDVL QEAPWEVEGL ASAPIEEVSP
460 470 480 490 500
VSRQSIRNSQ KHSPTSEPTP PGDALPPVSS PHTHRGYQPT PAMAKYVKIL
510 520 530 540 550
YDFTARNANE LSVLKDEVLE VLEDGRQWWK LRSRSGQAGY VPCNILGEAR
560 570 580 590 600
PEDAGAPFEQ AGQKYWGPAS PTHKLPPSFP GNKDELMQHM DEVNDELIRK
610 620 630 640 650
ISNIRAQPQR HFRVERSQPV SQPLTYESGP DEVRAWLEAK AFSPRIVENL
660 670 680 690 700
GILTGPQLFS LNKEELKKVC GEEGVRVYSQ LTMQKAFLEK QQSGSELEEL
710
MNKFHSMNQR RGEDS
Length:715
Mass (Da):80,621
Last modified:May 30, 2006 - v2
Checksum:iDAB07744B04CFEE2
GO
Isoform 2 (identifier: Q9H6S3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-388: Missing.

Show »
Length:327
Mass (Da):37,113
Checksum:i9D933D44E34CC320
GO
Isoform 3 (identifier: Q9H6S3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-108: S → SQSAQTPGASRVRAMYP

Note: No experimental confirmation available.

Show »
Length:731
Mass (Da):82,323
Checksum:i9D355BAFCF33601B
GO

Sequence cautioni

The sequence AAL55838.1 differs from that shown. Reason: Frameshift at position 593. Curated
The sequence BAB15180.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461S → N in BAD96623. 1 PublicationCurated
Sequence conflicti198 – 1981I → F in BAB15180. (PubMed:14702039)Curated
Sequence conflicti589 – 5891H → R in BAB15180. (PubMed:14702039)Curated
Sequence conflicti620 – 6201V → A in BAB15180. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 388388Missing in isoform 2. 2 PublicationsVSP_019092Add
BLAST
Alternative sequencei108 – 1081S → SQSAQTPGASRVRAMYP in isoform 3. 1 PublicationVSP_054144

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY074929 mRNA. Translation: AAL76118.1.
AF318331 mRNA. Translation: AAL55838.1. Frameshift.
AK025588 mRNA. Translation: BAB15180.1. Different initiation.
AK025824 mRNA. Translation: BAB15248.1.
AK027765 mRNA. Translation: BAB55354.1.
AK094539 mRNA. Translation: BAG52883.1.
AK222903 mRNA. Translation: BAD96623.1.
BC080636 mRNA. Translation: AAH80636.1.
BC093878 mRNA. Translation: AAH93878.1.
BC101481 mRNA. Translation: AAI01482.1.
BC143242 mRNA. Translation: AAI43243.1.
AC131934 Genomic DNA. No translation available.
AP006621 Genomic DNA. No translation available.
CCDSiCCDS31328.1. [Q9H6S3-1]
RefSeqiNP_073609.2. NM_022772.3. [Q9H6S3-1]
XP_006718336.1. XM_006718273.1. [Q9H6S3-1]
XP_006718337.1. XM_006718274.1. [Q9H6S3-1]
XP_006718338.1. XM_006718275.1. [Q9H6S3-1]
UniGeneiHs.55016.

Genome annotation databases

EnsembliENST00000318562; ENSP00000320828; ENSG00000177106. [Q9H6S3-1]
ENST00000526198; ENSP00000436230; ENSG00000177106. [Q9H6S3-3]
ENST00000530636; ENSP00000436035; ENSG00000177106. [Q9H6S3-1]
ENST00000533256; ENSP00000435585; ENSG00000177106. [Q9H6S3-1]
ENST00000614442; ENSP00000480201; ENSG00000177106. [Q9H6S3-3]
GeneIDi64787.
KEGGihsa:64787.
UCSCiuc001lqt.3. human. [Q9H6S3-1]
uc001lqw.3. human. [Q9H6S3-2]
uc010qwk.2. human.

Polymorphism databases

DMDMi108864726.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY074929 mRNA. Translation: AAL76118.1.
AF318331 mRNA. Translation: AAL55838.1. Frameshift.
AK025588 mRNA. Translation: BAB15180.1. Different initiation.
AK025824 mRNA. Translation: BAB15248.1.
AK027765 mRNA. Translation: BAB55354.1.
AK094539 mRNA. Translation: BAG52883.1.
AK222903 mRNA. Translation: BAD96623.1.
BC080636 mRNA. Translation: AAH80636.1.
BC093878 mRNA. Translation: AAH93878.1.
BC101481 mRNA. Translation: AAI01482.1.
BC143242 mRNA. Translation: AAI43243.1.
AC131934 Genomic DNA. No translation available.
AP006621 Genomic DNA. No translation available.
CCDSiCCDS31328.1. [Q9H6S3-1]
RefSeqiNP_073609.2. NM_022772.3. [Q9H6S3-1]
XP_006718336.1. XM_006718273.1. [Q9H6S3-1]
XP_006718337.1. XM_006718274.1. [Q9H6S3-1]
XP_006718338.1. XM_006718275.1. [Q9H6S3-1]
UniGeneiHs.55016.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWUNMR-A612-697[»]
1WXBNMR-A495-549[»]
ProteinModelPortaliQ9H6S3.
SMRiQ9H6S3. Positions 46-175, 494-555, 612-697.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122297. 6 interactions.
IntActiQ9H6S3. 6 interactions.
MINTiMINT-5002000.
STRINGi9606.ENSP00000320828.

PTM databases

PhosphoSiteiQ9H6S3.

Polymorphism databases

DMDMi108864726.

Proteomic databases

MaxQBiQ9H6S3.
PaxDbiQ9H6S3.
PRIDEiQ9H6S3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318562; ENSP00000320828; ENSG00000177106. [Q9H6S3-1]
ENST00000526198; ENSP00000436230; ENSG00000177106. [Q9H6S3-3]
ENST00000530636; ENSP00000436035; ENSG00000177106. [Q9H6S3-1]
ENST00000533256; ENSP00000435585; ENSG00000177106. [Q9H6S3-1]
ENST00000614442; ENSP00000480201; ENSG00000177106. [Q9H6S3-3]
GeneIDi64787.
KEGGihsa:64787.
UCSCiuc001lqt.3. human. [Q9H6S3-1]
uc001lqw.3. human. [Q9H6S3-2]
uc010qwk.2. human.

Organism-specific databases

CTDi64787.
GeneCardsiGC11P000696.
HGNCiHGNC:21296. EPS8L2.
HPAiHPA041143.
MIMi614988. gene.
neXtProtiNX_Q9H6S3.
PharmGKBiPA134981048.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG263108.
GeneTreeiENSGT00390000003646.
HOVERGENiHBG003090.
InParanoidiQ9H6S3.
KOiK17277.
OMAiERSQPVH.
OrthoDBiEOG7TMZR9.
PhylomeDBiQ9H6S3.
TreeFamiTF313069.

Miscellaneous databases

ChiTaRSiEPS8L2. human.
EvolutionaryTraceiQ9H6S3.
GeneWikiiEPS8L2.
GenomeRNAii64787.
NextBioi35481152.
PROiQ9H6S3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H6S3.
CleanExiHS_EPS8L2.
ExpressionAtlasiQ9H6S3. baseline and differential.
GenevestigatoriQ9H6S3.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "In silico analysis of the EPS8 gene family: genomic organization, expression profile, and protein structure."
    Tocchetti A., Confalonieri S., Scita G., Di Fiore P.P., Betsholtz C.
    Genomics 81:234-244(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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 1 AND 2).
    Tissue: Brain cortex and Placenta.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 3).
    Tissue: Brain and Prostate.
  7. "The eps8 family of proteins links growth factor stimulation to actin reorganization generating functional redundancy in the Ras/Rac pathway."
    Offenhaeuser N., Borgonovo A., Disanza A., Romano P., Ponzanelli I., Iannolo G., Di Fiore P.P., Scita G.
    Mol. Biol. Cell 15:91-98(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH ABI1 AND SOS1, INTERACTION WITH ABI1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-469 AND SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "solution structure of the SH3 domain from human epidermal growth factor receptor pathway substrate 8-like protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 495-549.

Entry informationi

Entry nameiES8L2_HUMAN
AccessioniPrimary (citable) accession number: Q9H6S3
Secondary accession number(s): B3KSX1
, B7ZKL3, Q53GM8, Q8WYW7, Q96K06, Q9H6K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: January 7, 2015
This is version 108 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.