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Q5HYK7 (SH319_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SH3 domain-containing protein 19
Alternative name(s):
ADAM-binding protein Eve-1
EEN-binding protein
Short name=EBP
Gene names
Name:SH3D19
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length790 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in regulating A disintegrin and metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May be involved in suppression of Ras-induced cellular transformation and Ras-mediated activation of ELK1. Plays a role in the regulation of cell morphology and cytoskeletal organization. Ref.6 Ref.7 Ref.9

Subunit structure

Interacts with ADAM12. Isoform 4 and isoform 5 (but not isoform 1 and isoform 2)interact with ADAM9, ADAM10, ADAM15 and ADAM17. Interacts with SH3GL1 SH3 domain. Interacts via SH3 3 and SH3 4 or SH3 4 and SH3 5 domains with SOS2. Probably forms a trimeric complex with SH3GL1 and SOS2. Interacts with SH3YL1 By similarity. Ref.6 Ref.7

Subcellular location

Cytoplasm. Nucleus. Note: Is recruited to the nucleus by the KMT2A/MLL1-EEN fusion protein. Ref.6

Tissue specificity

Widely expressed with highest levels in heart, skeletal muscle, kidney, liver, placenta, small intestine and lung. Expressed at low levels in colon, thymus, spleen and leukocytes. Ref.7

Sequence similarities

Contains 5 SH3 domains.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Sequence caution

The sequence AAI08891.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI08892.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI08893.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI08894.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAF83714.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI46052.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5HYK7-1)

Also known as: Eve-1a;

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: Q5HYK7-2)

Also known as: Eve-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     415-437: Missing.
Isoform 3 (identifier: Q5HYK7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     232-268: DPFQLPAKTEPIKERAVQPAPTRKPTVIRIPAKPGKC → G
     415-437: Missing.
Isoform 4 (identifier: Q5HYK7-4)

Also known as: Eve-1c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-370: Missing.
Isoform 5 (identifier: Q5HYK7-5)

Also known as: Eve-1d;

The sequence of this isoform differs from the canonical sequence as follows:
     1-370: Missing.
     415-437: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 790790SH3 domain-containing protein 19
PRO_0000318197

Regions

Domain415 – 47056SH3 1
Domain495 – 55460SH3 2
Domain571 – 63060SH3 3
Domain661 – 72060SH3 4
Domain730 – 78960SH3 5
Region342 – 35817Interaction with SH3GL1
Compositional bias86 – 350265Pro-rich

Amino acid modifications

Modified residue651Phosphoserine By similarity

Natural variations

Alternative sequence1 – 370370Missing in isoform 4 and isoform 5.
VSP_031182
Alternative sequence232 – 26837DPFQL…KPGKC → G in isoform 3.
VSP_031183
Alternative sequence415 – 43723Missing in isoform 2, isoform 3 and isoform 5.
VSP_031184

Experimental info

Sequence conflict11M → V in CAI46052. Ref.2
Sequence conflict2641K → R in CAI46052. Ref.2
Sequence conflict2671K → E in CAI46052. Ref.2

Sequences

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

Last modified February 5, 2008. Version 2.
Checksum: FA860FB41FE8CDD5

FASTA79086,525
        10         20         30         40         50         60 
MNIMNTEQSQ NSIVSRIKVF EGQTNIETSG LPKKPEITPR SLPPKPTVSS GKPSVAPKPA 

        70         80         90        100        110        120 
ANRASGEWDS GTENRLKVTS KEGLTPYPPL QEAGSIPVTK PELPKKPNPG LIRSVNPEIP 

       130        140        150        160        170        180 
GRGPLAESSD SGKKVPTPAP RPLLLKKSVS SENPTYPSAP LKPVTVPPRL AGASQAKAYK 

       190        200        210        220        230        240 
SLGEGPPANP PVPVLQSKPL VDIDLISFDD DVLPTPSGNL AEESVGSEMV LDPFQLPAKT 

       250        260        270        280        290        300 
EPIKERAVQP APTRKPTVIR IPAKPGKCLH EDPQSPPPLP AEKPIGNTFS TVSGKLSNVE 

       310        320        330        340        350        360 
RTRNLESNHP GQTGGFVRVP PRLPPRPVNG KTIPTQQPPT KVPPERPPPP KLSATRRSNK 

       370        380        390        400        410        420 
KLPFNRSSSD MDLQKKQSNL ATGLSKAKSQ VFKNQDPVLP PRPKPGHPLY SKYMLSVPHG 

       430        440        450        460        470        480 
IANEDIVSQN PGELSCKRGD VLVMLKQTEN NYLECQKGED TGRVHLSQMK IITPLDEHLR 

       490        500        510        520        530        540 
SRPNDPSHAQ KPVDSGAPHA VVLHDFPAEQ VDDLNLTSGE IVYLLEKIDT DWYRGNCRNQ 

       550        560        570        580        590        600 
IGIFPANYVK VIIDIPEGGN GKRECVSSHC VKGSRCVARF EYIGEQKDEL SFSEGEIIIL 

       610        620        630        640        650        660 
KEYVNEEWAR GEVRGRTGIF PLNFVEPVED YPTSGANVLS TKVPLKTKKE DSGSNSQVNS 

       670        680        690        700        710        720 
LPAEWCEALH SFTAETSDDL SFKRGDRIQI LERLDSDWCR GRLQDREGIF PAVFVRPCPA 

       730        740        750        760        770        780 
EAKSMLAIVP KGRKAKALYD FRGENEDELS FKAGDIITEL ESVDDDWMSG ELMGKSGIFP 

       790 
KNYIQFLQIS 

« Hide

Isoform 2 (Eve-1b) [UniParc].

Checksum: 9DC52412DD810D43
Show »

FASTA76784,136
Isoform 3 [UniParc].

Checksum: 34B191C247F3D367
Show »

FASTA73180,131
Isoform 4 (Eve-1c) [UniParc].

Checksum: C49CE5F2A5DCAF1C
Show »

FASTA42047,056
Isoform 5 (Eve-1d) [UniParc].

Checksum: 813BAA810E48B27B
Show »

FASTA39744,667

References

« Hide 'large scale' references
[1]"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-790 (ISOFORM 1).
Tissue: Amygdala.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon endothelium and Testis.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[5]"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 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-790 (ISOFORM 1).
Tissue: Brain, Chondrosarcoma and Lung.
[6]"Identification and characterization of EBP, a novel EEN binding protein that inhibits Ras signaling and is recruited into the nucleus by the MLL-EEN fusion protein."
Yam J.W., Jin D.Y., So C.W., Chan L.C.
Blood 103:1445-1453(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SH3GL1 AND SOS2.
[7]"ADAM binding protein Eve-1 is required for ectodomain shedding of epidermal growth factor receptor ligands."
Tanaka M., Nanba D., Mori S., Shiba F., Ishiguro H., Yoshino K., Matsuura N., Higashiyama S.
J. Biol. Chem. 279:41950-41959(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1; 2; 4 AND 5), TISSUE SPECIFICITY, INTERACTION WITH ADAM9; ADAM10; ADAM12; ADAM15 AND ADAM17.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK291025 mRNA. Translation: BAF83714.1. Different initiation.
AK294476 mRNA. Translation: BAH11782.1.
AL133047 mRNA. Translation: CAB61374.1.
BX647422 mRNA. Translation: CAI46052.1. Different initiation.
AC095055 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04986.1.
BC032468 mRNA. Translation: AAH32468.1.
BC045742 mRNA. Translation: AAH45742.1.
BC085613 mRNA. Translation: AAH85613.2.
BC108890 mRNA. Translation: AAI08891.1. Different initiation.
BC108891 mRNA. Translation: AAI08892.1. Different initiation.
BC108892 mRNA. Translation: AAI08893.1. Different initiation.
BC108893 mRNA. Translation: AAI08894.1. Different initiation.
CCDSCCDS34077.2. [Q5HYK7-1]
CCDS47143.1. [Q5HYK7-3]
CCDS47144.1. [Q5HYK7-2]
RefSeqNP_001009555.3. NM_001009555.3. [Q5HYK7-1]
NP_001122395.1. NM_001128923.1. [Q5HYK7-2]
NP_001122396.1. NM_001128924.1. [Q5HYK7-3]
NP_001230278.1. NM_001243349.1. [Q5HYK7-2]
XP_005262824.1. XM_005262767.1. [Q5HYK7-1]
XP_006714165.1. XM_006714102.1. [Q5HYK7-1]
UniGeneHs.744983.

3D structure databases

ProteinModelPortalQ5HYK7.
SMRQ5HYK7. Positions 421-472, 503-787.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127448. 6 interactions.
IntActQ5HYK7. 4 interactions.
MINTMINT-1203586.
STRING9606.ENSP00000302913.

PTM databases

PhosphoSiteQ5HYK7.

Polymorphism databases

DMDM166977688.

Proteomic databases

MaxQBQ5HYK7.
PaxDbQ5HYK7.
PRIDEQ5HYK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304527; ENSP00000302913; ENSG00000109686. [Q5HYK7-1]
ENST00000409252; ENSP00000386848; ENSG00000109686. [Q5HYK7-1]
ENST00000409598; ENSP00000387030; ENSG00000109686. [Q5HYK7-2]
ENST00000424281; ENSP00000404542; ENSG00000109686. [Q5HYK7-3]
ENST00000427414; ENSP00000415694; ENSG00000109686. [Q5HYK7-3]
ENST00000455740; ENSP00000416708; ENSG00000109686. [Q5HYK7-2]
ENST00000514152; ENSP00000423449; ENSG00000109686. [Q5HYK7-2]
GeneID152503.
KEGGhsa:152503.
UCSCuc003imc.2. human. [Q5HYK7-3]
uc003ime.2. human. [Q5HYK7-2]
uc010ipl.1. human. [Q5HYK7-1]

Organism-specific databases

CTD152503.
GeneCardsGC04M152041.
HGNCHGNC:30418. SH3D19.
HPAHPA016424.
MIM608674. gene.
neXtProtNX_Q5HYK7.
PharmGKBPA162403244.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296456.
HOVERGENHBG108486.
InParanoidQ5HYK7.
OMAVLDPFQL.
OrthoDBEOG761BW2.
PhylomeDBQ5HYK7.
TreeFamTF330850.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ5HYK7.
BgeeQ5HYK7.
CleanExHS_SH3D19.
GenevestigatorQ5HYK7.

Family and domain databases

InterProIPR011511. SH3_2.
IPR001452. SH3_domain.
IPR028505. SH3D19.
[Graphical view]
PANTHERPTHR10661:SF127. PTHR10661:SF127. 1 hit.
PfamPF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 5 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 5 hits.
PROSITEPS50002. SH3. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSH3D19. human.
GenomeRNAi152503.
NextBio86965.
PROQ5HYK7.
SOURCESearch...

Entry information

Entry nameSH319_HUMAN
AccessionPrimary (citable) accession number: Q5HYK7
Secondary accession number(s): B7Z296 expand/collapse secondary AC list , Q08EK1, Q32N10, Q5U3B8, Q86XB3, Q8N5E7, Q9UFC8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 84 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

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM