Reviewed, UniProtKB/Swiss-Prot Q9Y230 (RUVB2_HUMAN)

Names and origin

Protein names

Recommended name:
    RuvB-like 2
    EC=3.6.1.-
Alternative name(s):
    48 kDa TATA box-binding protein-interacting protein
      Short name=48 kDa TBP-interacting protein
    TIP49b
    Repressing pontin 52
      Short name=Reptin 52
    51 kDa erythrocyte cytosolic protein
      Short name=ECP-51
    TIP60-associated protein 54-beta
      Short name=TAP54-beta
    INO80 complex subunit J

Gene names

Name:	RUVBL2
Synonyms:	INO80J, TIP48, TIP49B
ORF Names:	CGI-46

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. RUVBL2 plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2.
Subunit structure	Forms a multimeric complex with RUVBL1. Interacts with the transcriptional activation domain of MYC. Interacts With ATF2. Component of the RNA polymerase II holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1 complex and TBP. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit HTATIP/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and EAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. RUVBL2 interacts with EP400. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Interacts with NPAT. Component of the chromatin-remodeling INO80 complex, at least composed of ACTL6A, ACTR5, ACTR8, RVBL1, RVBL2, INO80, INO80B, INO80C, INO80D and INO80E. Ref.2 Ref.5 Ref.15 Ref.19
Subcellular location	Nucleus matrix. Nucleus › nucleoplasm. Cytoplasm. Membrane. Note: Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol. Although it is also present in the cytoplasm and associated with the cell membranes.
Tissue specificity	Ubiquitously expressed. Highly expressed in testis and thymus.
Domain	The C-terminal domain is required for association with ATF2.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.18
Sequence similarities	Belongs to the ruvB family.
Sequence caution	The sequence AAD34041.1 differs from that shown. Reason: Frameshift at position 401. The sequence AAH08355.1 differs from that shown. Reason: Frameshift at position 191.

Ontologies

Keywords
Biological process	DNA recombination Growth regulation Transcription Transcription regulation
Cellular component	Cytoplasm Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Chromatin regulator Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA recombination Ref.2 Traceable author statement. Source: ProtInc DNA repair Ref.2 Traceable author statement. Source: ProtInc histone H2A acetylation Inferred from direct assay. Source: UniProtKB histone H4 acetylation Inferred from direct assay. Source: UniProtKB protein folding Ref.1 Traceable author statement. Source: ProtInc regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Ref.13 Ref.16 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Ref.2 Traceable author statement. Source: ProtInc damaged DNA binding Inferred from electronic annotation. Source: InterPro identical protein binding Ref.13 Inferred from direct assay. Source: UniProtKB unfolded protein binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCAS1	O75363	1	EBI-352939,EBI-1042966
C2orf44	Q9H6R7	1	EBI-352939,EBI-346906
DNASE2	O00115	1	EBI-352939,EBI-1051412
DPCD	Q9BVM2	1	EBI-352939,EBI-749988
EXOSC10	Q01780	1	EBI-352939,EBI-358236
IKBKE	Q14164	1	EBI-352939,EBI-307369
NDRG1	Q92597	1	EBI-352939,EBI-716486
NEK6	Q9HC98	1	EBI-352939,EBI-740364
NME2	P22392	1	EBI-352939,EBI-713693
PLOD2	O00469	1	EBI-352939,EBI-1047459
RGS20	O76081	1	EBI-352939,EBI-1052678
RIOK3	O14730	1	EBI-352939,EBI-1047061
RPS11	P62280	1	EBI-352939,EBI-1047710
RUVBL1	Q9Y265	4	EBI-352939,EBI-353675
SSSCA1	O60232	1	EBI-352939,EBI-741415
UQCRC1	P31930	1	EBI-352939,EBI-1052596
USP7	Q93009	1	EBI-352939,EBI-302474

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11 Ref.12

Chain

2 – 463

462

RuvB-like 2

PRO_0000165644

Regions

Nucleotide binding

77 – 84

8

ATP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.12

Modified residue

220

1

Phosphoserine Ref.18

Experimental info

Sequence conflict

214

1

D → N in AAD34041. Ref.6

Sequence conflict

257 – 258

2

FL → YV AA sequence Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

463

Helix Strand Turn

Details...

Beta strand

135 – 147

13

Beta strand

151 – 155

5

Beta strand

157 – 163

7

Beta strand

165 – 173

9

Helix

176 – 183

8

Beta strand

190 – 195

6

Turn

196 – 199

4

Beta strand

200 – 205

6

Sequences

	Sequence		Length	Mass (Da)
	Q9Y230-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 54C78E9C587D975A	FASTA	463	51,157
	10 20 30 40 50 60 MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL 70 80 90 100 110 120 EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT 130 140 150 160 170 180 QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE 190 200 210 220 230 240 SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH 250 260 270 280 290 300 TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 310 320 330 340 350 360 VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT 370 380 390 400 410 420 PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE 430 440 450 460 VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins." Salzer U., Kubicek M., Prohaska R. Biochim. Biophys. Acta 1446:365-370(1999) [PubMed: 10524211] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-83; 131-144; 212-223; 369-372 AND 440-457. Tissue: Bone marrow.
[2]	"TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a." Kanemaki M., Kurokawa Y., Matsu-ura T., Makino Y., Masani A., Okazaki K., Morishita T., Tamura T.-A. J. Biol. Chem. 274:22437-22444(1999) [PubMed: 10428817] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH RUVBL1. Tissue: Liver.
[3]	"Human TIP49b/RUVBL2 gene: genomic structure, expression pattern, physical link to the human CGB/LHB gene cluster on chromosome 19q13.3." Parfait B., Giovangrandi Y., Asheuer M., Laurendeau I., Olivi M., Vodovar N., Vidaud D., Vidaud M., Bieche I. Ann. Genet. 43:69-74(2000) [PubMed: 10998447] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[4]	"Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity." Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U., Aragnol D., Kemler R., Pradel J. EMBO J. 19:6121-6130(2000) [PubMed: 11080158] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal liver.
[5]	"An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc." Wood M.A., McMahon S.B., Cole M.D. Mol. Cell 5:321-330(2000) [PubMed: 10882073] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-83; 116-124; 237-253 AND 254-269, INTERACTION WITH MYC.
[6]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed: 10810093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[8]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
[9]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon and Lung.
[11]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Tissue: Platelet.
[12]	Bienvenut W.V., Heiserich L., Gottlieb E. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-18; 30-53; 55-64; 72-83; 116-124; 165-177; 237-269; 335-368; 393-400 AND 418-438, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[13]	"Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis." Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y. Cell 102:463-473(2000) [PubMed: 10966108] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-40; 185-197; 354-365 AND 417-427, IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[14]	"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex." Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W. J. Biol. Chem. 278:42733-42736(2003) [PubMed: 12963728] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-40; 72-83; 165-177; 187-197; 254-269; 354-365; 418-438 AND 445-463, IDENTIFICATION IN NUA4 COMPLEX, MASS SPECTROMETRY.
[15]	"TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage." Cho S.-G., Bhoumik A., Broday L., Ivanov V., Rosenstein B., Ronai Z. Mol. Cell. Biol. 21:8398-8413(2001) [PubMed: 11713276] [Abstract] Cited for: INTERACTION WITH ATF2.
[16]	"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans." Doyon Y., Selleck W., Lane W.S., Tan S., Cote J. Mol. Cell. Biol. 24:1884-1896(2004) [PubMed: 14966270] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING COMPLEX.
[17]	"A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex." Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K., Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P., Conaway R.C., Conaway J.W. J. Biol. Chem. 280:41207-41212(2005) [PubMed: 16230350] [Abstract] Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[18]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, MASS SPECTROMETRY.
[19]	"Transcriptional activation of histone genes requires NPAT-dependent recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S phase transition." DeRan M., Pulvino M., Greene E., Su C., Zhao J. Mol. Cell. Biol. 28:435-447(2008) [PubMed: 17967892] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NPAT.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"Solution structure of RSGI ruh-039, a fragment of C-terminal domain of RuvB-like 2 from human cDNA." Mycobacterium tuberculosis structural genomics consortium (TB) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 132-213.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y18417 mRNA. Translation: CAB46270.1.
AB024301 mRNA. Translation: BAA76708.1.
AF155138 mRNA. Translation: AAD38073.1.
AF124607 mRNA. Translation: AAF87087.1.
AF151804 mRNA. Translation: AAD34041.1. Frameshift.
AL136743 mRNA. Translation: CAB66677.1.
AK074542 mRNA. Translation: BAC11048.1.
CR533507 mRNA. Translation: CAG38538.1.
BC000428 mRNA. Translation: AAH00428.1.
BC004531 mRNA. Translation: AAH04531.1.
BC008355 mRNA. Translation: AAH08355.1. Frameshift.

IPI

IPI00009104.

PIR

T46313.

RefSeq

NP_006657.1.

UniGene

Hs.515846

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CQA	NMR	-	A	132-212	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:28153N.

IntAct

Q9Y230. 74 interactions.

PTM databases

PhosphoSite

Q9Y230.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00009104.

Proteomic databases

PeptideAtlas

Q9Y230.

PRIDE

Q9Y230.

Genome annotation databases

Ensembl

ENSG00000183207. Homo sapiens. [Contig view]

GeneID

10856.

KEGG

hsa:10856.

UCSC

uc002plr.1. human.

Organism-specific databases

GeneCards

GC19P054188.

H-InvDB

HIX0015312.

HGNC

HGNC:10475. RUVBL2.

HPA

CAB012432.

MIM

604788. gene.

PharmGKB

PA34888.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9Y230.

HOVERGEN

Q9Y230.

OMA

Q9Y230. TTDMETI.

Gene expression databases

Bgee

Q9Y230.

CleanEx

HS_RUVBL2.

GermOnline

ENSG00000183207. Homo sapiens.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR004504. DNA_repair_RadA.
IPR010339. TIP49_C.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
PF06068. TIP49. 1 hit.
[Graphical view]

PRINTS

PR01874. DNAREPAIRADA.

SMART

SM00382. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

41211.

SOURCE

Search...

Entry information

Entry name

RUVB2_HUMAN

Accession

Primary (citable) accession number: Q9Y230
Secondary accession number(s): Q6FIB9, Q6PK27, Q9Y361

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)