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Protein

SH3 domain-containing protein 19

Gene

SH3D19

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

Functioni

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.3 Publications

GO - Molecular functioni

  • proline-rich region binding Source: BHF-UCL

GO - Biological processi

  • cytoskeleton organization Source: UniProtKB
  • membrane organization Source: Reactome
  • positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  • post-Golgi vesicle-mediated transport Source: Reactome
  • regulation of cell morphogenesis Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 domain-containing protein 19
Alternative name(s):
ADAM-binding protein Eve-1
EEN-binding protein
Short name:
EBP
Gene namesi
Name:SH3D19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:30418. SH3D19.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Is recruited to the nucleus by the KMT2A/MLL1-EEN fusion protein.

GO - Cellular componenti

  • cytosol Source: Reactome
  • Golgi apparatus Source: HPA
  • nucleoplasm Source: HPA
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162403244.

Polymorphism and mutation databases

BioMutaiSH3D19.
DMDMi166977688.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 790790SH3 domain-containing protein 19PRO_0000318197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651PhosphoserineBy similarity
Modified residuei762 – 7621Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5HYK7.
PaxDbiQ5HYK7.
PRIDEiQ5HYK7.

PTM databases

PhosphoSiteiQ5HYK7.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ5HYK7.
CleanExiHS_SH3D19.
GenevisibleiQ5HYK7. HS.

Organism-specific databases

HPAiHPA016424.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SH3YL1Q96HL83EBI-2563437,EBI-722667

Protein-protein interaction databases

BioGridi127448. 6 interactions.
IntActiQ5HYK7. 4 interactions.
MINTiMINT-1203586.
STRINGi9606.ENSP00000302913.

Structurei

3D structure databases

ProteinModelPortaliQ5HYK7.
SMRiQ5HYK7. Positions 422-788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini415 – 47056SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 55460SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini571 – 63060SH3 3PROSITE-ProRule annotationAdd
BLAST
Domaini661 – 72060SH3 4PROSITE-ProRule annotationAdd
BLAST
Domaini730 – 78960SH3 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni342 – 35817Interaction with SH3GL1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi86 – 350265Pro-richAdd
BLAST

Sequence similaritiesi

Contains 5 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG296456.
GeneTreeiENSGT00760000119190.
HOVERGENiHBG108486.
InParanoidiQ5HYK7.
OMAiSLSGEWC.
OrthoDBiEOG761BW2.
PhylomeDBiQ5HYK7.
TreeFamiTF330850.

Family and domain databases

InterProiIPR011511. SH3_2.
IPR001452. SH3_domain.
IPR028505. SH3D19.
[Graphical view]
PANTHERiPTHR10661:SF127. PTHR10661:SF127. 1 hit.
PfamiPF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 5 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 5 hits.
PROSITEiPS50002. SH3. 4 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5HYK7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNIMNTEQSQ NSIVSRIKVF EGQTNIETSG LPKKPEITPR SLPPKPTVSS
60 70 80 90 100
GKPSVAPKPA ANRASGEWDS GTENRLKVTS KEGLTPYPPL QEAGSIPVTK
110 120 130 140 150
PELPKKPNPG LIRSVNPEIP GRGPLAESSD SGKKVPTPAP RPLLLKKSVS
160 170 180 190 200
SENPTYPSAP LKPVTVPPRL AGASQAKAYK SLGEGPPANP PVPVLQSKPL
210 220 230 240 250
VDIDLISFDD DVLPTPSGNL AEESVGSEMV LDPFQLPAKT EPIKERAVQP
260 270 280 290 300
APTRKPTVIR IPAKPGKCLH EDPQSPPPLP AEKPIGNTFS TVSGKLSNVE
310 320 330 340 350
RTRNLESNHP GQTGGFVRVP PRLPPRPVNG KTIPTQQPPT KVPPERPPPP
360 370 380 390 400
KLSATRRSNK KLPFNRSSSD MDLQKKQSNL ATGLSKAKSQ VFKNQDPVLP
410 420 430 440 450
PRPKPGHPLY SKYMLSVPHG IANEDIVSQN PGELSCKRGD VLVMLKQTEN
460 470 480 490 500
NYLECQKGED TGRVHLSQMK IITPLDEHLR SRPNDPSHAQ KPVDSGAPHA
510 520 530 540 550
VVLHDFPAEQ VDDLNLTSGE IVYLLEKIDT DWYRGNCRNQ IGIFPANYVK
560 570 580 590 600
VIIDIPEGGN GKRECVSSHC VKGSRCVARF EYIGEQKDEL SFSEGEIIIL
610 620 630 640 650
KEYVNEEWAR GEVRGRTGIF PLNFVEPVED YPTSGANVLS TKVPLKTKKE
660 670 680 690 700
DSGSNSQVNS LPAEWCEALH SFTAETSDDL SFKRGDRIQI LERLDSDWCR
710 720 730 740 750
GRLQDREGIF PAVFVRPCPA EAKSMLAIVP KGRKAKALYD FRGENEDELS
760 770 780 790
FKAGDIITEL ESVDDDWMSG ELMGKSGIFP KNYIQFLQIS
Length:790
Mass (Da):86,525
Last modified:February 5, 2008 - v2
Checksum:iFA860FB41FE8CDD5
GO
Isoform 2 (identifier: Q5HYK7-2) [UniParc]FASTAAdd to basket

Also known as: Eve-1b

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

Show »
Length:767
Mass (Da):84,136
Checksum:i9DC52412DD810D43
GO
Isoform 3 (identifier: Q5HYK7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     232-268: DPFQLPAKTEPIKERAVQPAPTRKPTVIRIPAKPGKC → G
     415-437: Missing.

Show »
Length:731
Mass (Da):80,131
Checksum:i34B191C247F3D367
GO
Isoform 4 (identifier: Q5HYK7-4) [UniParc]FASTAAdd to basket

Also known as: Eve-1c

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

Show »
Length:420
Mass (Da):47,056
Checksum:iC49CE5F2A5DCAF1C
GO
Isoform 5 (identifier: Q5HYK7-5) [UniParc]FASTAAdd to basket

Also known as: Eve-1d

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

Show »
Length:397
Mass (Da):44,667
Checksum:i813BAA810E48B27B
GO

Sequence cautioni

The sequence AAI08891.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI08892.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI08893.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI08894.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAF83714.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI46052.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → V in CAI46052 (PubMed:17974005).Curated
Sequence conflicti264 – 2641K → R in CAI46052 (PubMed:17974005).Curated
Sequence conflicti267 – 2671K → E in CAI46052 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 370370Missing in isoform 4 and isoform 5. CuratedVSP_031182Add
BLAST
Alternative sequencei232 – 26837DPFQL…KPGKC → G in isoform 3. 1 PublicationVSP_031183Add
BLAST
Alternative sequencei415 – 43723Missing in isoform 2, isoform 3 and isoform 5. 2 PublicationsVSP_031184Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34077.2. [Q5HYK7-1]
CCDS47143.1. [Q5HYK7-3]
CCDS47144.1. [Q5HYK7-2]
RefSeqiNP_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_011529948.1. XM_011531646.1. [Q5HYK7-1]
XP_011529951.1. XM_011531649.1. [Q5HYK7-3]
UniGeneiHs.744983.

Genome annotation databases

EnsembliENST00000304527; ENSP00000302913; ENSG00000109686.
ENST00000409252; ENSP00000386848; ENSG00000109686.
ENST00000409598; ENSP00000387030; ENSG00000109686. [Q5HYK7-2]
ENST00000427414; ENSP00000415694; ENSG00000109686. [Q5HYK7-3]
ENST00000514152; ENSP00000423449; ENSG00000109686. [Q5HYK7-2]
GeneIDi152503.
KEGGihsa:152503.
UCSCiuc003imc.2. human. [Q5HYK7-3]
uc003ime.2. human. [Q5HYK7-2]
uc010ipl.1. human. [Q5HYK7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34077.2. [Q5HYK7-1]
CCDS47143.1. [Q5HYK7-3]
CCDS47144.1. [Q5HYK7-2]
RefSeqiNP_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_011529948.1. XM_011531646.1. [Q5HYK7-1]
XP_011529951.1. XM_011531649.1. [Q5HYK7-3]
UniGeneiHs.744983.

3D structure databases

ProteinModelPortaliQ5HYK7.
SMRiQ5HYK7. Positions 422-788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127448. 6 interactions.
IntActiQ5HYK7. 4 interactions.
MINTiMINT-1203586.
STRINGi9606.ENSP00000302913.

PTM databases

PhosphoSiteiQ5HYK7.

Polymorphism and mutation databases

BioMutaiSH3D19.
DMDMi166977688.

Proteomic databases

MaxQBiQ5HYK7.
PaxDbiQ5HYK7.
PRIDEiQ5HYK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304527; ENSP00000302913; ENSG00000109686.
ENST00000409252; ENSP00000386848; ENSG00000109686.
ENST00000409598; ENSP00000387030; ENSG00000109686. [Q5HYK7-2]
ENST00000427414; ENSP00000415694; ENSG00000109686. [Q5HYK7-3]
ENST00000514152; ENSP00000423449; ENSG00000109686. [Q5HYK7-2]
GeneIDi152503.
KEGGihsa:152503.
UCSCiuc003imc.2. human. [Q5HYK7-3]
uc003ime.2. human. [Q5HYK7-2]
uc010ipl.1. human. [Q5HYK7-1]

Organism-specific databases

CTDi152503.
GeneCardsiGC04M152041.
HGNCiHGNC:30418. SH3D19.
HPAiHPA016424.
MIMi608674. gene.
neXtProtiNX_Q5HYK7.
PharmGKBiPA162403244.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG296456.
GeneTreeiENSGT00760000119190.
HOVERGENiHBG108486.
InParanoidiQ5HYK7.
OMAiSLSGEWC.
OrthoDBiEOG761BW2.
PhylomeDBiQ5HYK7.
TreeFamiTF330850.

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiSH3D19. human.
GenomeRNAii152503.
NextBioi86965.
PROiQ5HYK7.
SOURCEiSearch...

Gene expression databases

BgeeiQ5HYK7.
CleanExiHS_SH3D19.
GenevisibleiQ5HYK7. HS.

Family and domain databases

InterProiIPR011511. SH3_2.
IPR001452. SH3_domain.
IPR028505. SH3D19.
[Graphical view]
PANTHERiPTHR10661:SF127. PTHR10661:SF127. 1 hit.
PfamiPF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 5 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 5 hits.
PROSITEiPS50002. SH3. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSH319_HUMAN
AccessioniPrimary (citable) accession number: Q5HYK7
Secondary accession number(s): B7Z296
, Q08EK1, Q32N10, Q5U3B8, Q86XB3, Q8N5E7, Q9UFC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 22, 2015
This is version 94 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

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. 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.