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Protein

EH domain-binding protein 1

Gene

EHBP1

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 actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton.1 Publication

Names & Taxonomyi

Protein namesi
Recommended name:
EH domain-binding protein 1
Gene namesi
Name:EHBP1
Synonyms:KIAA0903, NACSIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:29144. EHBP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Prostate cancer, hereditary, 12 (HPC12)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
See also OMIM:611868

Organism-specific databases

MalaCardsiEHBP1.
MIMi611868. phenotype.
PharmGKBiPA128394620.

Polymorphism and mutation databases

BioMutaiEHBP1.
DMDMi223590228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12311231EH domain-binding protein 1PRO_0000285202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711PhosphoserineCombined sources
Modified residuei174 – 1741PhosphoserineCombined sources
Modified residuei177 – 1771PhosphoserineCombined sources
Modified residuei222 – 2221PhosphoserineBy similarity
Modified residuei335 – 3351PhosphoserineCombined sources
Modified residuei426 – 4261PhosphoserineBy similarity
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei436 – 4361PhosphoserineCombined sources
Modified residuei636 – 6361PhosphoserineBy similarity
Modified residuei710 – 7101PhosphoserineCombined sources
Modified residuei854 – 8541PhosphoserineCombined sources
Modified residuei964 – 9641PhosphoserineCombined sources
Modified residuei1058 – 10581PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NDI1.
MaxQBiQ8NDI1.
PaxDbiQ8NDI1.
PRIDEiQ8NDI1.

PTM databases

iPTMnetiQ8NDI1.
PhosphoSiteiQ8NDI1.

Expressioni

Gene expression databases

BgeeiQ8NDI1.
ExpressionAtlasiQ8NDI1. baseline and differential.
GenevisibleiQ8NDI1. HS.

Organism-specific databases

HPAiHPA035468.
HPA035469.

Interactioni

Subunit structurei

Interacts with EHD2.1 Publication

Protein-protein interaction databases

BioGridi116893. 10 interactions.
IntActiQ8NDI1. 6 interactions.
STRINGi9606.ENSP00000263991.

Structurei

Secondary structure

1
1231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi446 – 45611Combined sources
Turni457 – 4593Combined sources
Helixi470 – 4734Combined sources
Helixi476 – 48510Combined sources
Turni487 – 4893Combined sources
Helixi492 – 4943Combined sources
Helixi501 – 51111Combined sources
Turni512 – 5154Combined sources
Helixi522 – 5276Combined sources
Beta strandi528 – 5303Combined sources
Helixi533 – 54715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D89NMR-A443-548[»]
ProteinModelPortaliQ8NDI1.
SMRiQ8NDI1. Positions 443-548.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NDI1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 163151NT-C2Sequence analysisAdd
BLAST
Domaini443 – 545103CHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili185 – 21026Sequence analysisAdd
BLAST
Coiled coili808 – 87972Sequence analysisAdd
BLAST
Coiled coili1076 – 110025Sequence analysisAdd
BLAST
Coiled coili1136 – 123095Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi362 – 3654Poly-Glu
Compositional biasi1110 – 11134Poly-Glu

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 NT-C2 domain.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOVERGENiHBG057909.
InParanoidiQ8NDI1.
OMAiKNVRPVD.
OrthoDBiEOG7ZKS97.
PhylomeDBiQ8NDI1.
TreeFamiTF105382.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR029944. EHBP1.
IPR019448. NT-C2.
[Graphical view]
PANTHERiPTHR11915:SF289. PTHR11915:SF289. 2 hits.
PfamiPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF10358. NT-C2. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NDI1-1) [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
MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR
60 70 80 90 100
KSSKAHSWQP GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF
110 120 130 140 150
VIENESPSGR RKALATSSIN MKQYASPMPT QTDVKLKFKP LSKKVVSAAL
160 170 180 190 200
QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ ADIGNLDDFE EDNEDDDENR
210 220 230 240 250
VNQEEKAAKI TEIVNQLNAL SSLDEDQDDC IKQANMRSAK SASSSEELIN
260 270 280 290 300
KLNFLDEAEK DLATVNSNPF DDPDAAELNP FGDPDSEEPI TETASPRKTE
310 320 330 340 350
DSFYNNSYNP FKEVQTPQYL NPFDEPEAFV TIKDSPPQST KRKNIRPVDM
360 370 380 390 400
SKYLYADSSK TEEEELDESN PFYEPKSTPP PNNLVNPVQE LETERRVKRK
410 420 430 440 450
APAPPVLSPK TGVLNENTVS AGKDLSTSPK PSPIPSPVLG RKPNASQSLL
460 470 480 490 500
VWCKEVTKNY RGVKITNFTT SWRNGLSFCA ILHHFRPDLI DYKSLNPQDI
510 520 530 540 550
KENNKKAYDG FASIGISRLL EPSDMVLLAI PDKLTVMTYL YQIRAHFSGQ
560 570 580 590 600
ELNVVQIEEN SSKSTYKVGN YETDTNSSVD QEKFYAELSD LKREPELQQP
610 620 630 640 650
ISGAVDFLSQ DDSVFVNDSG VGESESEHQT PDDHLSPSTA SPYCRRTKSD
660 670 680 690 700
TEPQKSQQSS GRTSGSDDPG ICSNTDSTQA QVLLGKKRLL KAETLELSDL
710 720 730 740 750
YVSDKKKDMS PPFICEETDE QKLQTLDIGS NLEKEKLENS RSLECRSDPE
760 770 780 790 800
SPIKKTSLSP TSKLGYSYSR DLDLAKKKHA SLRQTESDPD ADRTTLNHAD
810 820 830 840 850
HSSKIVQHRL LSRQEELKER ARVLLEQARR DAALKAGNKH NTNTATPFCN
860 870 880 890 900
RQLSDQQDEE RRRQLRERAR QLIAEARSGV KMSELPSYGE MAAEKLKERS
910 920 930 940 950
KASGDENDNI EIDTNEEIPE GFVVGGGDEL TNLENDLDTP EQNSKLVDLK
960 970 980 990 1000
LKKLLEVQPQ VANSPSSAAQ KAVTESSEQD MKSGTEDLRT ERLQKTTERF
1010 1020 1030 1040 1050
RNPVVFSKDS TVRKTQLQSF SQYIENRPEM KRQRSIQEDT KKGNEEKAAI
1060 1070 1080 1090 1100
TETQRKPSED EVLNKGFKDT SQYVVGELAA LENEQKQIDT RAALVEKRLR
1110 1120 1130 1140 1150
YLMDTGRNTE EEEAMMQEWF MLVNKKNALI RRMNQLSLLE KEHDLERRYE
1160 1170 1180 1190 1200
LLNRELRAML AIEDWQKTEA QKRREQLLLD ELVALVNKRD ALVRDLDAQE
1210 1220 1230
KQAEEEDEHL ERTLEQNKGK MAKKEEKCVL Q
Length:1,231
Mass (Da):140,017
Last modified:February 10, 2009 - v3
Checksum:iFFF39B65BCC0FC0A
GO
Isoform 2 (identifier: Q8NDI1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     212-246: Missing.

Note: No experimental confirmation available.
Show »
Length:1,196
Mass (Da):136,237
Checksum:iD6675AC34EE4DEDE
GO
Isoform 3 (identifier: Q8NDI1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     212-246: Missing.
     905-940: Missing.

Note: No experimental confirmation available.
Show »
Length:1,160
Mass (Da):132,322
Checksum:iDD7923FE0B14AF11
GO

Sequence cautioni

The sequence BAA91391.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051E → V in AAH29477 (PubMed:15489334).Curated
Sequence conflicti112 – 1121K → R in AAQ97141 (Ref. 2) Curated
Sequence conflicti112 – 1121K → R in CAD38814 (PubMed:17974005).Curated
Sequence conflicti212 – 2121E → G in AAQ97141 (Ref. 2) Curated
Sequence conflicti212 – 2121E → G in CAD38814 (PubMed:17974005).Curated
Sequence conflicti256 – 2561D → V in AAQ97141 (Ref. 2) Curated
Sequence conflicti256 – 2561D → V in CAD38814 (PubMed:17974005).Curated
Sequence conflicti342 – 3421R → G in AAQ97141 (Ref. 2) Curated
Sequence conflicti342 – 3421R → G in CAD38814 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti395 – 3951R → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035913
Natural varianti755 – 7551K → Q.
Corresponds to variant rs17432615 [ dbSNP | Ensembl ].
VAR_031992

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei212 – 24635Missing in isoform 2 and isoform 3. 3 PublicationsVSP_024834Add
BLAST
Alternative sequencei905 – 94036Missing in isoform 3. 1 PublicationVSP_024835Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY531390 mRNA. Translation: AAS48537.1.
AY331186 mRNA. Translation: AAQ97141.1.
AL833968 mRNA. Translation: CAD38814.1.
AC007098 Genomic DNA. Translation: AAY14789.1.
AC009501 Genomic DNA. Translation: AAY24356.1.
AC092567 Genomic DNA. Translation: AAX82024.1.
BC029477 mRNA. Translation: AAH29477.1.
BC067215 mRNA. Translation: AAH67215.1.
AK000828 mRNA. Translation: BAA91391.1. Sequence problems.
AB020710 mRNA. Translation: BAA74926.1.
CCDSiCCDS1872.1. [Q8NDI1-1]
CCDS46299.1. [Q8NDI1-2]
CCDS46300.1. [Q8NDI1-3]
RefSeqiNP_001136086.1. NM_001142614.1. [Q8NDI1-2]
NP_001136087.1. NM_001142615.2. [Q8NDI1-3]
NP_001136088.1. NM_001142616.1. [Q8NDI1-3]
NP_056067.2. NM_015252.3. [Q8NDI1-1]
XP_005264282.1. XM_005264225.1. [Q8NDI1-1]
XP_005264283.1. XM_005264226.1. [Q8NDI1-1]
XP_005264284.1. XM_005264227.1. [Q8NDI1-2]
XP_011531015.1. XM_011532713.1. [Q8NDI1-1]
XP_011531016.1. XM_011532714.1. [Q8NDI1-1]
XP_011531017.1. XM_011532715.1. [Q8NDI1-1]
UniGeneiHs.271667.

Genome annotation databases

EnsembliENST00000263991; ENSP00000263991; ENSG00000115504. [Q8NDI1-1]
ENST00000405015; ENSP00000384143; ENSG00000115504. [Q8NDI1-3]
ENST00000405289; ENSP00000385524; ENSG00000115504. [Q8NDI1-2]
ENST00000431489; ENSP00000403783; ENSG00000115504. [Q8NDI1-3]
GeneIDi23301.
KEGGihsa:23301.
UCSCiuc002sby.4. human. [Q8NDI1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY531390 mRNA. Translation: AAS48537.1.
AY331186 mRNA. Translation: AAQ97141.1.
AL833968 mRNA. Translation: CAD38814.1.
AC007098 Genomic DNA. Translation: AAY14789.1.
AC009501 Genomic DNA. Translation: AAY24356.1.
AC092567 Genomic DNA. Translation: AAX82024.1.
BC029477 mRNA. Translation: AAH29477.1.
BC067215 mRNA. Translation: AAH67215.1.
AK000828 mRNA. Translation: BAA91391.1. Sequence problems.
AB020710 mRNA. Translation: BAA74926.1.
CCDSiCCDS1872.1. [Q8NDI1-1]
CCDS46299.1. [Q8NDI1-2]
CCDS46300.1. [Q8NDI1-3]
RefSeqiNP_001136086.1. NM_001142614.1. [Q8NDI1-2]
NP_001136087.1. NM_001142615.2. [Q8NDI1-3]
NP_001136088.1. NM_001142616.1. [Q8NDI1-3]
NP_056067.2. NM_015252.3. [Q8NDI1-1]
XP_005264282.1. XM_005264225.1. [Q8NDI1-1]
XP_005264283.1. XM_005264226.1. [Q8NDI1-1]
XP_005264284.1. XM_005264227.1. [Q8NDI1-2]
XP_011531015.1. XM_011532713.1. [Q8NDI1-1]
XP_011531016.1. XM_011532714.1. [Q8NDI1-1]
XP_011531017.1. XM_011532715.1. [Q8NDI1-1]
UniGeneiHs.271667.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D89NMR-A443-548[»]
ProteinModelPortaliQ8NDI1.
SMRiQ8NDI1. Positions 443-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116893. 10 interactions.
IntActiQ8NDI1. 6 interactions.
STRINGi9606.ENSP00000263991.

PTM databases

iPTMnetiQ8NDI1.
PhosphoSiteiQ8NDI1.

Polymorphism and mutation databases

BioMutaiEHBP1.
DMDMi223590228.

Proteomic databases

EPDiQ8NDI1.
MaxQBiQ8NDI1.
PaxDbiQ8NDI1.
PRIDEiQ8NDI1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263991; ENSP00000263991; ENSG00000115504. [Q8NDI1-1]
ENST00000405015; ENSP00000384143; ENSG00000115504. [Q8NDI1-3]
ENST00000405289; ENSP00000385524; ENSG00000115504. [Q8NDI1-2]
ENST00000431489; ENSP00000403783; ENSG00000115504. [Q8NDI1-3]
GeneIDi23301.
KEGGihsa:23301.
UCSCiuc002sby.4. human. [Q8NDI1-1]

Organism-specific databases

CTDi23301.
GeneCardsiEHBP1.
H-InvDBHIX0030395.
HGNCiHGNC:29144. EHBP1.
HPAiHPA035468.
HPA035469.
MalaCardsiEHBP1.
MIMi609922. gene.
611868. phenotype.
neXtProtiNX_Q8NDI1.
PharmGKBiPA128394620.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOVERGENiHBG057909.
InParanoidiQ8NDI1.
OMAiKNVRPVD.
OrthoDBiEOG7ZKS97.
PhylomeDBiQ8NDI1.
TreeFamiTF105382.

Miscellaneous databases

ChiTaRSiEHBP1. human.
EvolutionaryTraceiQ8NDI1.
GenomeRNAii23301.
NextBioi45137.
PROiQ8NDI1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NDI1.
ExpressionAtlasiQ8NDI1. baseline and differential.
GenevisibleiQ8NDI1. HS.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR029944. EHBP1.
IPR019448. NT-C2.
[Graphical view]
PANTHERiPTHR11915:SF289. PTHR11915:SF289. 2 hits.
PfamiPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF10358. NT-C2. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis to the actin cytoskeleton."
    Guilherme A., Soriano N.A., Bose S., Holik J., Bose A., Pomerleau D.P., Furcinitti P., Leszyk J., Corvera S., Czech M.P.
    J. Biol. Chem. 279:10593-10605(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH EHD2.
  2. "Functional analysis of NACSIN (KIAA0903) in membrane trafficking."
    Castellano-Munoz M., Fernandez-Chacon R.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. "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].
  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] (ISOFORM 3).
    Tissue: Placenta and Uterus.
  6. "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] OF 1-341 (ISOFORM 2).
    Tissue: Adipose tissue.
  7. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1231.
    Tissue: Brain.
  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-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-174; SER-177; SER-432; SER-436; SER-710; SER-964 AND SER-1058, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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-171; SER-174; SER-432 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-171; SER-174 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-436 AND SER-1058, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-335; SER-432; SER-436; SER-854 AND SER-1058, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Solution structure of the CH domain from human EH domain binding protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 443-548.
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-395.
  18. "Common sequence variants on 2p15 and Xp11.22 confer susceptibility to prostate cancer."
    Gudmundsson J., Sulem P., Rafnar T., Bergthorsson J.T., Manolescu A., Gudbjartsson D., Agnarsson B.A., Sigurdsson A., Benediktsdottir K.R., Blondal T., Jakobsdottir M., Stacey S.N., Kostic J., Kristinsson K.T., Birgisdottir B., Ghosh S., Magnusdottir D.N., Thorlacius S.
    , Thorleifsson G., Zheng S.L., Sun J., Chang B.-L., Elmore J.B., Breyer J.P., McReynolds K.M., Bradley K.M., Yaspan B.L., Wiklund F., Stattin P., Lindstroem S., Adami H.-O., McDonnell S.K., Schaid D.J., Cunningham J.M., Wang L., Cerhan J.R., St Sauver J.L., Isaacs S.D., Wiley K.E., Partin A.W., Walsh P.C., Polo S., Ruiz-Echarri M., Navarrete S., Fuertes F., Saez B., Godino J., Weijerman P.C., Swinkels D.W., Aben K.K., Witjes J.A., Suarez B.K., Helfand B.T., Frigge M.L., Kristjansson K., Ober C., Jonsson E., Einarsson G.V., Xu J., Gronberg H., Smith J.R., Thibodeau S.N., Isaacs W.B., Catalona W.J., Mayordomo J.I., Kiemeney L.A., Barkardottir R.B., Gulcher J.R., Thorsteinsdottir U., Kong A., Stefansson K.
    Nat. Genet. 40:281-283(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO HEREDITARY PROSTATE CANCER.

Entry informationi

Entry nameiEHBP1_HUMAN
AccessioniPrimary (citable) accession number: Q8NDI1
Secondary accession number(s): O94977
, Q53TG7, Q53TV6, Q580X2, Q6NX72, Q6PIT3, Q6QNV2, Q9NWI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: February 10, 2009
Last modified: May 11, 2016
This is version 110 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.