Q8NDI1 (EHBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EH domain-binding protein 1

Gene names

Name:	EHBP1
Synonyms:	KIAA0903, NACSIN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1231 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. Ref.1
Subunit structure	Interacts with EHD2. Ref.1
Subcellular location	Cytoplasm. Membrane. Note: Mostly found in cytosol and plasma membrane. Ref.1
Involvement in disease	Prostate cancer, hereditary, 12 (HPC12) [MIM:611868]: A 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Sequence similarities	Contains 1 CH (calponin-homology) domain.
Sequence caution	The sequence BAA91391.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8NDI1-1)

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: Q8NDI1-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8NDI1-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1231

1231

EH domain-binding protein 1

PRO_0000285202

Regions

Domain

443 – 545

103

CH

Coiled coil

185 – 210

26

Potential

Coiled coil

808 – 879

72

Potential

Coiled coil

1076 – 1100

25

Potential

Coiled coil

1136 – 1230

95

Potential

Compositional bias

362 – 365

4

Poly-Glu

Compositional bias

1110 – 1113

4

Poly-Glu

Amino acid modifications

Modified residue

171

1

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

174

1

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

177

1

Phosphoserine Ref.9

Modified residue

432

1

Phosphoserine Ref.9 Ref.10

Modified residue

436

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Modified residue

710

1

Phosphoserine Ref.9

Modified residue

964

1

Phosphoserine Ref.9

Modified residue

1019

1

Phosphoserine By similarity

Modified residue

1058

1

Phosphoserine Ref.9 Ref.13

Natural variations

Alternative sequence

212 – 246

35

Missing in isoform 2 and isoform 3.

VSP_024834

Alternative sequence

905 – 940

36

Missing in isoform 3.

VSP_024835

Natural variant

395

1

R → T in a breast cancer sample; somatic mutation. Ref.15

VAR_035913

Natural variant

755

1

K → Q.
Corresponds to variant rs17432615 [ dbSNP | Ensembl ].

VAR_031992

Experimental info

Sequence conflict

105

1

E → V in AAH29477. Ref.5

Sequence conflict

112

1

K → R in AAQ97141. Ref.2

Sequence conflict

112

1

K → R in CAD38814. Ref.3

Sequence conflict

212

1

E → G in AAQ97141. Ref.2

Sequence conflict

212

1

E → G in CAD38814. Ref.3

Sequence conflict

256

1

D → V in AAQ97141. Ref.2

Sequence conflict

256

1

D → V in CAD38814. Ref.3

Sequence conflict

342

1

R → G in AAQ97141. Ref.2

Sequence conflict

342

1

R → G in CAD38814. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

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1231

Helix Strand Turn

Details...

Helix

446 – 456

11

Turn

457 – 459

3

Helix

470 – 473

4

Helix

476 – 485

10

Turn

487 – 489

3

Helix

492 – 494

3

Helix

501 – 511

11

Turn

512 – 515

4

Helix

522 – 527

6

Beta strand

528 – 530

3

Helix

533 – 547

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: FFF39B65BCC0FC0A	FASTA	1,231	140,017
	10 20 30 40 50 60 MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR KSSKAHSWQP 70 80 90 100 110 120 GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF VIENESPSGR RKALATSSIN 130 140 150 160 170 180 MKQYASPMPT QTDVKLKFKP LSKKVVSAAL QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ 190 200 210 220 230 240 ADIGNLDDFE EDNEDDDENR VNQEEKAAKI TEIVNQLNAL SSLDEDQDDC IKQANMRSAK 250 260 270 280 290 300 SASSSEELIN KLNFLDEAEK DLATVNSNPF DDPDAAELNP FGDPDSEEPI TETASPRKTE 310 320 330 340 350 360 DSFYNNSYNP FKEVQTPQYL NPFDEPEAFV TIKDSPPQST KRKNIRPVDM SKYLYADSSK 370 380 390 400 410 420 TEEEELDESN PFYEPKSTPP PNNLVNPVQE LETERRVKRK APAPPVLSPK TGVLNENTVS 430 440 450 460 470 480 AGKDLSTSPK PSPIPSPVLG RKPNASQSLL VWCKEVTKNY RGVKITNFTT SWRNGLSFCA 490 500 510 520 530 540 ILHHFRPDLI DYKSLNPQDI KENNKKAYDG FASIGISRLL EPSDMVLLAI PDKLTVMTYL 550 560 570 580 590 600 YQIRAHFSGQ ELNVVQIEEN SSKSTYKVGN YETDTNSSVD QEKFYAELSD LKREPELQQP 610 620 630 640 650 660 ISGAVDFLSQ DDSVFVNDSG VGESESEHQT PDDHLSPSTA SPYCRRTKSD TEPQKSQQSS 670 680 690 700 710 720 GRTSGSDDPG ICSNTDSTQA QVLLGKKRLL KAETLELSDL YVSDKKKDMS PPFICEETDE 730 740 750 760 770 780 QKLQTLDIGS NLEKEKLENS RSLECRSDPE SPIKKTSLSP TSKLGYSYSR DLDLAKKKHA 790 800 810 820 830 840 SLRQTESDPD ADRTTLNHAD HSSKIVQHRL LSRQEELKER ARVLLEQARR DAALKAGNKH 850 860 870 880 890 900 NTNTATPFCN RQLSDQQDEE RRRQLRERAR QLIAEARSGV KMSELPSYGE MAAEKLKERS 910 920 930 940 950 960 KASGDENDNI EIDTNEEIPE GFVVGGGDEL TNLENDLDTP EQNSKLVDLK LKKLLEVQPQ 970 980 990 1000 1010 1020 VANSPSSAAQ KAVTESSEQD MKSGTEDLRT ERLQKTTERF RNPVVFSKDS TVRKTQLQSF 1030 1040 1050 1060 1070 1080 SQYIENRPEM KRQRSIQEDT KKGNEEKAAI TETQRKPSED EVLNKGFKDT SQYVVGELAA 1090 1100 1110 1120 1130 1140 LENEQKQIDT RAALVEKRLR YLMDTGRNTE EEEAMMQEWF MLVNKKNALI RRMNQLSLLE 1150 1160 1170 1180 1190 1200 KEHDLERRYE LLNRELRAML AIEDWQKTEA QKRREQLLLD ELVALVNKRD ALVRDLDAQE 1210 1220 1230 KQAEEEDEHL ERTLEQNKGK MAKKEEKCVL Q
	Isoform 2 [UniParc]. Checksum: D6675AC34EE4DEDE	FASTA	1,196	136,237
	10 20 30 40 50 60 MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR KSSKAHSWQP 70 80 90 100 110 120 GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF VIENESPSGR RKALATSSIN 130 140 150 160 170 180 MKQYASPMPT QTDVKLKFKP LSKKVVSAAL QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ 190 200 210 220 230 240 ADIGNLDDFE EDNEDDDENR VNQEEKAAKI TELINKLNFL DEAEKDLATV NSNPFDDPDA 250 260 270 280 290 300 AELNPFGDPD SEEPITETAS PRKTEDSFYN NSYNPFKEVQ TPQYLNPFDE PEAFVTIKDS 310 320 330 340 350 360 PPQSTKRKNI RPVDMSKYLY ADSSKTEEEE LDESNPFYEP KSTPPPNNLV NPVQELETER 370 380 390 400 410 420 RVKRKAPAPP VLSPKTGVLN ENTVSAGKDL STSPKPSPIP SPVLGRKPNA SQSLLVWCKE 430 440 450 460 470 480 VTKNYRGVKI TNFTTSWRNG LSFCAILHHF RPDLIDYKSL NPQDIKENNK KAYDGFASIG 490 500 510 520 530 540 ISRLLEPSDM VLLAIPDKLT VMTYLYQIRA HFSGQELNVV QIEENSSKST YKVGNYETDT 550 560 570 580 590 600 NSSVDQEKFY AELSDLKREP ELQQPISGAV DFLSQDDSVF VNDSGVGESE SEHQTPDDHL 610 620 630 640 650 660 SPSTASPYCR RTKSDTEPQK SQQSSGRTSG SDDPGICSNT DSTQAQVLLG KKRLLKAETL 670 680 690 700 710 720 ELSDLYVSDK KKDMSPPFIC EETDEQKLQT LDIGSNLEKE KLENSRSLEC RSDPESPIKK 730 740 750 760 770 780 TSLSPTSKLG YSYSRDLDLA KKKHASLRQT ESDPDADRTT LNHADHSSKI VQHRLLSRQE 790 800 810 820 830 840 ELKERARVLL EQARRDAALK AGNKHNTNTA TPFCNRQLSD QQDEERRRQL RERARQLIAE 850 860 870 880 890 900 ARSGVKMSEL PSYGEMAAEK LKERSKASGD ENDNIEIDTN EEIPEGFVVG GGDELTNLEN 910 920 930 940 950 960 DLDTPEQNSK LVDLKLKKLL EVQPQVANSP SSAAQKAVTE SSEQDMKSGT EDLRTERLQK 970 980 990 1000 1010 1020 TTERFRNPVV FSKDSTVRKT QLQSFSQYIE NRPEMKRQRS IQEDTKKGNE EKAAITETQR 1030 1040 1050 1060 1070 1080 KPSEDEVLNK GFKDTSQYVV GELAALENEQ KQIDTRAALV EKRLRYLMDT GRNTEEEEAM 1090 1100 1110 1120 1130 1140 MQEWFMLVNK KNALIRRMNQ LSLLEKEHDL ERRYELLNRE LRAMLAIEDW QKTEAQKRRE 1150 1160 1170 1180 1190 QLLLDELVAL VNKRDALVRD LDAQEKQAEE EDEHLERTLE QNKGKMAKKE EKCVLQ
	Isoform 3 [UniParc]. Checksum: DD7923FE0B14AF11	FASTA	1,160	132,322
	10 20 30 40 50 60 MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR KSSKAHSWQP 70 80 90 100 110 120 GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF VIENESPSGR RKALATSSIN 130 140 150 160 170 180 MKQYASPMPT QTDVKLKFKP LSKKVVSAAL QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ 190 200 210 220 230 240 ADIGNLDDFE EDNEDDDENR VNQEEKAAKI TELINKLNFL DEAEKDLATV NSNPFDDPDA 250 260 270 280 290 300 AELNPFGDPD SEEPITETAS PRKTEDSFYN NSYNPFKEVQ TPQYLNPFDE PEAFVTIKDS 310 320 330 340 350 360 PPQSTKRKNI RPVDMSKYLY ADSSKTEEEE LDESNPFYEP KSTPPPNNLV NPVQELETER 370 380 390 400 410 420 RVKRKAPAPP VLSPKTGVLN ENTVSAGKDL STSPKPSPIP SPVLGRKPNA SQSLLVWCKE 430 440 450 460 470 480 VTKNYRGVKI TNFTTSWRNG LSFCAILHHF RPDLIDYKSL NPQDIKENNK KAYDGFASIG 490 500 510 520 530 540 ISRLLEPSDM VLLAIPDKLT VMTYLYQIRA HFSGQELNVV QIEENSSKST YKVGNYETDT 550 560 570 580 590 600 NSSVDQEKFY AELSDLKREP ELQQPISGAV DFLSQDDSVF VNDSGVGESE SEHQTPDDHL 610 620 630 640 650 660 SPSTASPYCR RTKSDTEPQK SQQSSGRTSG SDDPGICSNT DSTQAQVLLG KKRLLKAETL 670 680 690 700 710 720 ELSDLYVSDK KKDMSPPFIC EETDEQKLQT LDIGSNLEKE KLENSRSLEC RSDPESPIKK 730 740 750 760 770 780 TSLSPTSKLG YSYSRDLDLA KKKHASLRQT ESDPDADRTT LNHADHSSKI VQHRLLSRQE 790 800 810 820 830 840 ELKERARVLL EQARRDAALK AGNKHNTNTA TPFCNRQLSD QQDEERRRQL RERARQLIAE 850 860 870 880 890 900 ARSGVKMSEL PSYGEMAAEK LKERSKASGE QNSKLVDLKL KKLLEVQPQV ANSPSSAAQK 910 920 930 940 950 960 AVTESSEQDM KSGTEDLRTE RLQKTTERFR NPVVFSKDST VRKTQLQSFS QYIENRPEMK 970 980 990 1000 1010 1020 RQRSIQEDTK KGNEEKAAIT ETQRKPSEDE VLNKGFKDTS QYVVGELAAL ENEQKQIDTR 1030 1040 1050 1060 1070 1080 AALVEKRLRY LMDTGRNTEE EEAMMQEWFM LVNKKNALIR RMNQLSLLEK EHDLERRYEL 1090 1100 1110 1120 1130 1140 LNRELRAMLA IEDWQKTEAQ KRREQLLLDE LVALVNKRDA LVRDLDAQEK QAEEEDEHLE 1150 1160 RTLEQNKGKM AKKEEKCVLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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: 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-174; SER-177; SER-432; SER-436; SER-710; SER-964 AND SER-1058, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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, MASS SPECTROMETRY.
[14]	"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.
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-395.
[16]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00178187.
IPI00433194.
IPI00845271.

RefSeq

NP_001136086.1. NM_001142614.1.
NP_001136087.1. NM_001142615.2.
NP_001136088.1. NM_001142616.1.
NP_056067.2. NM_015252.3.

UniGene

Hs.271667.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D89	NMR	-	A	443-548	[»]

ProteinModelPortal

Q8NDI1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8NDI1. 3 interactions.

PTM databases

PhosphoSite

Q8NDI1.

Polymorphism databases

DMDM

223590228.

Proteomic databases

PaxDb

Q8NDI1.

PRIDE

Q8NDI1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263991; ENSP00000263991; ENSG00000115504.
ENST00000354487; ENSP00000346482; ENSG00000115504.
ENST00000405015; ENSP00000384143; ENSG00000115504.
ENST00000405289; ENSP00000385524; ENSG00000115504.
ENST00000431489; ENSP00000403783; ENSG00000115504.

GeneID

23301.

KEGG

hsa:23301.

UCSC

uc002sby.3. human.
uc002sbz.3. human.
uc002scb.3. human.

Organism-specific databases

CTD

23301.

GeneCards

GC02P062844.

H-InvDB

HIX0030395.

HGNC

HGNC:29144. EHBP1.

HPA

HPA035468.
HPA035469.

MIM

609922. gene.
611868. phenotype.

neXtProt

NX_Q8NDI1.

PharmGKB

PA128394620.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5069.

HOVERGEN

HBG057909.

InParanoid

Q8NDI1.

OMA

KASGDEN.

PhylomeDB

Q8NDI1.

Gene expression databases

ArrayExpress

Q8NDI1.

Bgee

Q8NDI1.

Genevestigator

Q8NDI1.

Family and domain databases

Gene3D

1.10.418.10. 1 hit.

InterPro

IPR001715. CH-domain.
IPR022735. DUF3585.
IPR019448. NT-C2.
[Graphical view]

Pfam

PF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF10358. NT-C2. 1 hit.
[Graphical view]

SMART

SM00033. CH. 1 hit.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS50021. CH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

EHBP1. human.

EvolutionaryTrace

Q8NDI1.

GenomeRNAi

23301.

NextBio

45137.

SOURCE

Search...

Entry information

Entry name

EHBP1_HUMAN

Accession

Primary (citable) accession number: Q8NDI1
Secondary accession number(s): O94977 , Q53TG7, Q53TV6, Q580X2, Q6NX72, Q6PIT3, Q6QNV2, Q9NWI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.