Q9UHX1 (PUF60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(U)-binding-splicing factor PUF60

Alternative name(s):
60 kDa poly(U)-binding-splicing factor
FUSE-binding protein-interacting repressor
Short name=FBP-interacting repressor
Ro-binding protein 1
Short name=RoBP1
Siah-binding protein 1
Short name=Siah-BP1

Gene names

Name:	PUF60
Synonyms:	FIR, ROBPI, SIAHBP1

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	559 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Subunit structure	Homodimer. Associates with the spliceosome. Found in a complex with TROVE2 and Y5 RNA. Found in a complex with FUBP1 and far upstream element (FUSE) DNA segment. Interacts directly with ERCC3. Interacts with CDK7, GTF2H1 and SFRS11. Does not interact with ERCC3 in xeroderma pigmentosum complementation group B (XPB) cells. Ref.1 Ref.2 Ref.8 Ref.9 Ref.13
Subcellular location	Nucleus. Note: Colocalizes partially with TROVE2. Ref.2 Ref.13
Tissue specificity	Isoform 2 is expressed in colonic epithelium and colorectal epithelium cancer (at protein level). Isoform 6 is expressed in colorectal epithelial cancer but below detection level in colonic epithelium. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Ref.2 Ref.10
Domain	The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.
Miscellaneous	Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells.
Sequence similarities	Belongs to the RRM half pint family. Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Repressor Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay. Source: HPA ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CACNA1A	O00555	2	EBI-1053259,EBI-766279
PCBP1	Q15365	2	EBI-1053259,EBI-946095
PPP1R16A	Q96I34	2	EBI-1053259,EBI-710402
SAP30BP	Q9UHR5	4	EBI-1053259,EBI-751683

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UHX1-1)

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: Q9UHX1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     101-117: Missing.

Isoform 3 (identifier: Q9UHX1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Isoform 4 (identifier: Q9UHX1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.
     101-117: Missing.

Isoform 5 (identifier: Q9UHX1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     9-37: Missing.

Isoform 6 (identifier: Q9UHX1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     9-37: Missing.
     101-117: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 559

559

Poly(U)-binding-splicing factor PUF60

PRO_0000299519

Regions

Domain

129 – 207

79

RRM 1

Domain

226 – 304

79

RRM 2

Domain

462 – 549

88

RRM 3; atypical

Region

1 – 516

516

Inhibits homodimerization

Region

77 – 559

483

Inhibits transcriptional repression, interaction with ERCC3 and apoptosis induction

Compositional bias

321 – 343

23

Ala-rich

Amino acid modifications

Modified residue

60

1

Phosphothreonine Ref.12 Ref.16

Modified residue

112

1

Phosphoserine Ref.16

Modified residue

251

1

N6-acetyllysine Ref.15

Modified residue

314

1

Phosphothreonine Ref.16

Modified residue

454

1

N6-acetyllysine Ref.15

Natural variations

Alternative sequence

1 – 43

43

Missing in isoform 3 and isoform 4.

VSP_027717

Alternative sequence

9 – 37

29

Missing in isoform 5 and isoform 6.

VSP_027718

Alternative sequence

101 – 117

17

Missing in isoform 2, isoform 4 and isoform 6.

VSP_027719

Experimental info

Sequence conflict

3

1

T → R in AAB41656. Ref.7

Sequence conflict

123

1

R → G in AAB41656. Ref.7

Secondary structure

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559

Helix Strand Turn

Details...

Helix

118 – 128

11

Beta strand

130 – 134

5

Helix

142 – 149

8

Helix

150 – 152

3

Beta strand

155 – 160

6

Turn

164 – 166

3

Beta strand

171 – 179

9

Helix

180 – 190

11

Beta strand

194 – 199

6

Beta strand

201 – 203

3

Helix

206 – 208

3

Helix

209 – 211

3

Helix

212 – 222

11

Helix

223 – 225

3

Beta strand

227 – 231

5

Beta strand

235 – 237

3

Helix

239 – 246

8

Beta strand

252 – 259

8

Turn

261 – 263

3

Beta strand

266 – 276

11

Helix

277 – 287

11

Beta strand

293 – 296

4

Beta strand

298 – 301

4

Beta strand

306 – 309

4

Helix

445 – 448

4

Turn

449 – 452

4

Helix

453 – 459

7

Beta strand

463 – 468

6

Helix

472 – 474

3

Helix

479 – 487

9

Turn

488 – 490

3

Beta strand

493 – 506

14

Beta strand

510 – 521

12

Helix

522 – 532

11

Beta strand

536 – 541

6

Beta strand

543 – 547

5

Helix

549 – 553

5

Beta strand

557 – 559

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 619F3C30D1C5951C	FASTA	559	59,875
	10 20 30 40 50 60 MATATIALQV NGQQGGGSEP AAAAAVVAAG DKWKPPQGTD SIKMENGQST AAKLGLPPLT 70 80 90 100 110 120 PEQQEALQKA KKYAMEQSIK SVLVKQTIAH QQQQLTNLQM AAVTMGFGDP LSPLQSMAAQ 130 140 150 160 170 180 RQRALAIMCR VYVGSIYYEL GEDTIRQAFA PFGPIKSIDM SWDSVTMKHK GFAFVEYEVP 190 200 210 220 230 240 EAAQLALEQM NSVMLGGRNI KVGRPSNIGQ AQPIIDQLAE EARAFNRIYV ASVHQDLSDD 250 260 270 280 290 300 DIKSVFEAFG KIKSCTLARD PTTGKHKGYG FIEYEKAQSS QDAVSSMNLF DLGGQYLRVG 310 320 330 340 350 360 KAVTPPMPLL TPATPGGLPP AAAVAAAAAT AKITAQEAVA GAAVLGTLGT PGLVSPALTL 370 380 390 400 410 420 AQPLGTLPQA VMAAQAPGVI TGVTPARPPI PVTIPSVGVV NPILASPPTL GLLEPKKEKE 430 440 450 460 470 480 EEELFPESER PEMLSEQEHM SISGSSARHM VMQKLLRKQE STVMVLRNMV DPKDIDDDLE 490 500 510 520 530 540 GEVTEECGKF GAVNRVIIYQ EKQGEEEDAE IIVKIFVEFS IASETHKAIQ ALNGRWFAGR 550 KVVAEVYDQE RFDNSDLSA
	Isoform 2 [UniParc]. Checksum: 2C67EBE529A0922E	FASTA	542	58,171
	10 20 30 40 50 60 MATATIALQV NGQQGGGSEP AAAAAVVAAG DKWKPPQGTD SIKMENGQST AAKLGLPPLT 70 80 90 100 110 120 PEQQEALQKA KKYAMEQSIK SVLVKQTIAH QQQQLTNLQM AAQRQRALAI MCRVYVGSIY 130 140 150 160 170 180 YELGEDTIRQ AFAPFGPIKS IDMSWDSVTM KHKGFAFVEY EVPEAAQLAL EQMNSVMLGG 190 200 210 220 230 240 RNIKVGRPSN IGQAQPIIDQ LAEEARAFNR IYVASVHQDL SDDDIKSVFE AFGKIKSCTL 250 260 270 280 290 300 ARDPTTGKHK GYGFIEYEKA QSSQDAVSSM NLFDLGGQYL RVGKAVTPPM PLLTPATPGG 310 320 330 340 350 360 LPPAAAVAAA AATAKITAQE AVAGAAVLGT LGTPGLVSPA LTLAQPLGTL PQAVMAAQAP 370 380 390 400 410 420 GVITGVTPAR PPIPVTIPSV GVVNPILASP PTLGLLEPKK EKEEEELFPE SERPEMLSEQ 430 440 450 460 470 480 EHMSISGSSA RHMVMQKLLR KQESTVMVLR NMVDPKDIDD DLEGEVTEEC GKFGAVNRVI 490 500 510 520 530 540 IYQEKQGEEE DAEIIVKIFV EFSIASETHK AIQALNGRWF AGRKVVAEVY DQERFDNSDL SA
	Isoform 3 [UniParc]. Checksum: F52D8C619E874B55	FASTA	516	55,729
	10 20 30 40 50 60 MENGQSTAAK LGLPPLTPEQ QEALQKAKKY AMEQSIKSVL VKQTIAHQQQ QLTNLQMAAV 70 80 90 100 110 120 TMGFGDPLSP LQSMAAQRQR ALAIMCRVYV GSIYYELGED TIRQAFAPFG PIKSIDMSWD 130 140 150 160 170 180 SVTMKHKGFA FVEYEVPEAA QLALEQMNSV MLGGRNIKVG RPSNIGQAQP IIDQLAEEAR 190 200 210 220 230 240 AFNRIYVASV HQDLSDDDIK SVFEAFGKIK SCTLARDPTT GKHKGYGFIE YEKAQSSQDA 250 260 270 280 290 300 VSSMNLFDLG GQYLRVGKAV TPPMPLLTPA TPGGLPPAAA VAAAAATAKI TAQEAVAGAA 310 320 330 340 350 360 VLGTLGTPGL VSPALTLAQP LGTLPQAVMA AQAPGVITGV TPARPPIPVT IPSVGVVNPI 370 380 390 400 410 420 LASPPTLGLL EPKKEKEEEE LFPESERPEM LSEQEHMSIS GSSARHMVMQ KLLRKQESTV 430 440 450 460 470 480 MVLRNMVDPK DIDDDLEGEV TEECGKFGAV NRVIIYQEKQ GEEEDAEIIV KIFVEFSIAS 490 500 510 ETHKAIQALN GRWFAGRKVV AEVYDQERFD NSDLSA
	Isoform 4 [UniParc]. Checksum: 77881512A09C3EFD	FASTA	499	54,025
	10 20 30 40 50 60 MENGQSTAAK LGLPPLTPEQ QEALQKAKKY AMEQSIKSVL VKQTIAHQQQ QLTNLQMAAQ 70 80 90 100 110 120 RQRALAIMCR VYVGSIYYEL GEDTIRQAFA PFGPIKSIDM SWDSVTMKHK GFAFVEYEVP 130 140 150 160 170 180 EAAQLALEQM NSVMLGGRNI KVGRPSNIGQ AQPIIDQLAE EARAFNRIYV ASVHQDLSDD 190 200 210 220 230 240 DIKSVFEAFG KIKSCTLARD PTTGKHKGYG FIEYEKAQSS QDAVSSMNLF DLGGQYLRVG 250 260 270 280 290 300 KAVTPPMPLL TPATPGGLPP AAAVAAAAAT AKITAQEAVA GAAVLGTLGT PGLVSPALTL 310 320 330 340 350 360 AQPLGTLPQA VMAAQAPGVI TGVTPARPPI PVTIPSVGVV NPILASPPTL GLLEPKKEKE 370 380 390 400 410 420 EEELFPESER PEMLSEQEHM SISGSSARHM VMQKLLRKQE STVMVLRNMV DPKDIDDDLE 430 440 450 460 470 480 GEVTEECGKF GAVNRVIIYQ EKQGEEEDAE IIVKIFVEFS IASETHKAIQ ALNGRWFAGR 490 KVVAEVYDQE RFDNSDLSA
	Isoform 5 [UniParc]. Checksum: 850251A390ECD30C	FASTA	530	57,103
	10 20 30 40 50 60 MATATIALGT DSIKMENGQS TAAKLGLPPL TPEQQEALQK AKKYAMEQSI KSVLVKQTIA 70 80 90 100 110 120 HQQQQLTNLQ MAAVTMGFGD PLSPLQSMAA QRQRALAIMC RVYVGSIYYE LGEDTIRQAF 130 140 150 160 170 180 APFGPIKSID MSWDSVTMKH KGFAFVEYEV PEAAQLALEQ MNSVMLGGRN IKVGRPSNIG 190 200 210 220 230 240 QAQPIIDQLA EEARAFNRIY VASVHQDLSD DDIKSVFEAF GKIKSCTLAR DPTTGKHKGY 250 260 270 280 290 300 GFIEYEKAQS SQDAVSSMNL FDLGGQYLRV GKAVTPPMPL LTPATPGGLP PAAAVAAAAA 310 320 330 340 350 360 TAKITAQEAV AGAAVLGTLG TPGLVSPALT LAQPLGTLPQ AVMAAQAPGV ITGVTPARPP 370 380 390 400 410 420 IPVTIPSVGV VNPILASPPT LGLLEPKKEK EEEELFPESE RPEMLSEQEH MSISGSSARH 430 440 450 460 470 480 MVMQKLLRKQ ESTVMVLRNM VDPKDIDDDL EGEVTEECGK FGAVNRVIIY QEKQGEEEDA 490 500 510 520 530 EIIVKIFVEF SIASETHKAI QALNGRWFAG RKVVAEVYDQ ERFDNSDLSA
	Isoform 6 [UniParc]. Checksum: 2A5BA6848E391E3A	FASTA	513	55,399
	10 20 30 40 50 60 MATATIALGT DSIKMENGQS TAAKLGLPPL TPEQQEALQK AKKYAMEQSI KSVLVKQTIA 70 80 90 100 110 120 HQQQQLTNLQ MAAQRQRALA IMCRVYVGSI YYELGEDTIR QAFAPFGPIK SIDMSWDSVT 130 140 150 160 170 180 MKHKGFAFVE YEVPEAAQLA LEQMNSVMLG GRNIKVGRPS NIGQAQPIID QLAEEARAFN 190 200 210 220 230 240 RIYVASVHQD LSDDDIKSVF EAFGKIKSCT LARDPTTGKH KGYGFIEYEK AQSSQDAVSS 250 260 270 280 290 300 MNLFDLGGQY LRVGKAVTPP MPLLTPATPG GLPPAAAVAA AAATAKITAQ EAVAGAAVLG 310 320 330 340 350 360 TLGTPGLVSP ALTLAQPLGT LPQAVMAAQA PGVITGVTPA RPPIPVTIPS VGVVNPILAS 370 380 390 400 410 420 PPTLGLLEPK KEKEEEELFP ESERPEMLSE QEHMSISGSS ARHMVMQKLL RKQESTVMVL 430 440 450 460 470 480 RNMVDPKDID DDLEGEVTEE CGKFGAVNRV IIYQEKQGEE EDAEIIVKIF VEFSIASETH 490 500 510 KAIQALNGRW FAGRKVVAEV YDQERFDNSD LSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The FBP interacting repressor targets TFIIH to inhibit activated transcription." Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D. Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN A COMPLEX WITH FUBP1 AND FUSE DNA, INTERACTION WITH CDK7; ERCC3; FUBP1 AND GTF2H1.
[2]	"Interaction cloning and characterization of RoBPI, a novel protein binding to human Ro ribonucleoproteins." Bouffard P., Barbar E., Briere F., Boire G. RNA 6:66-78(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 5), IDENTIFICATION IN A COMPLEX WITH TROVE2 AND Y5 RNA, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"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] (ISOFORM 1).
[4]	"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 1). Tissue: Testis.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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; 3 AND 4). Tissue: Brain, Lung, Muscle and Ovary.
[7]	"Interaction of sina and siah ring finger proteins with proteins involved in RNA metabolism, detected using the yeast two hybrid system." Hu Y., Holloway A.J., Bowtell D.D.L. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-559 (ISOFORM 2).
[8]	"PUF60: a novel U2AF65-related splicing activity." Page-McCaw P.S., Amonlirdviman K., Sharp P.A. RNA 5:1548-1560(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-559 (ISOFORM 1), PROTEIN SEQUENCE OF 32-43; 53-69; 72-80; 156-167; 169-185; 227-243; 267-296; 301-313; 332-342; 419-437 AND 527-559, FUNCTION, SUBUNIT, RNA-BINDING, INTERACTION WITH SFRS11.
[9]	"Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum." Liu J., Akoulitchev S., Weber A., Ge H., Chuikov S., Libutti D., Wang X.W., Conaway J.W., Harris C.C., Conaway R.C., Reinberg D., Levens D. Cell 104:353-363(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ERCC3.
[10]	"An essential role of alternative splicing of c-myc suppressor FUSE-binding protein-interacting repressor in carcinogenesis." Matsushita K., Tomonaga T., Shimada H., Shioya A., Higashi M., Matsubara H., Harigaya K., Nomura F., Libutti D., Levens D., Ochiai T. Cancer Res. 66:1409-1417(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 6), TISSUE SPECIFICITY.
[11]	"The FUSE/FBP/FIR/TFIIH system is a molecular machine programming a pulse of c-myc expression." Liu J., Kouzine F., Nie Z., Chung H.-J., Elisha-Feil Z., Weber A., Zhao K., Levens D. EMBO J. 25:2119-2130(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Control of pre-mRNA splicing by the general splicing factors PUF60 and U2AF." Hastings M.L., Allemand E., Duelli D.M., Myers M.P., Krainer A.R. PLoS ONE 2:E538-E538(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SPLICEOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING, SUBCELLULAR LOCATION.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-251 AND LYS-454, MASS SPECTROMETRY.
[16]	"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 THR-60; SER-112 AND THR-314, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"Solution structure of the third RNA binding domain of FBP-interacting repressor, SIAHBP1." RIKEN structural genomics initiative (RSGI) Submitted (APR-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 454-559.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF217197 mRNA. Translation: AAF27522.2.
AF114818 mRNA. Translation: AAF23589.1.
AK292373 mRNA. Translation: BAF85062.1.
CR457143 mRNA. Translation: CAG33424.1.
CH471162 Genomic DNA. Translation: EAW82187.1.
CH471162 Genomic DNA. Translation: EAW82189.1.
BC008875 mRNA. Translation: AAH08875.1.
BC009734 mRNA. Translation: AAH09734.1.
BC011265 mRNA. Translation: AAH11265.1.
BC011979 mRNA. Translation: AAH11979.1.
U51586 mRNA. Translation: AAB41656.1.
AF190744 mRNA. Translation: AAF05605.1.

IPI

IPI00069750.
IPI00100716.
IPI00788826.
IPI00797595.
IPI00855912.
IPI00856076.

RefSeq

NP_001129505.1. NM_001136033.2.
NP_001258025.1. NM_001271096.1.
NP_001258026.1. NM_001271097.1.
NP_001258027.1. NM_001271098.1.
NP_001258028.1. NM_001271099.1.
NP_001258029.1. NM_001271100.1.
NP_055096.2. NM_014281.4.
NP_510965.1. NM_078480.2.

UniGene

Hs.521924.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DNY	NMR	-	A	454-559	[»]
2KXF	NMR	-	A	119-314	[»]
2KXH	NMR	-	A	119-314	[»]
2QFJ	X-ray	2.10	A/B	118-316	[»]
3DXB	X-ray	2.20	A/B/C/D/E/F/G/H	460-559	[»]
3UE2	X-ray	1.23	A	443-559	[»]
3US5	X-ray	1.38	A	443-559	[»]
3UWT	X-ray	2.50	A	118-316	[»]

ProteinModelPortal

Q9UHX1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34636N.

IntAct

Q9UHX1. 20 interactions.

MINT

MINT-1374433.

STRING

9606.ENSP00000322016.

PTM databases

PhosphoSite

Q9UHX1.

Polymorphism databases

DMDM

74761960.

Proteomic databases

PaxDb

Q9UHX1.

PRIDE

Q9UHX1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313352; ENSP00000322016; ENSG00000179950.
ENST00000349157; ENSP00000322036; ENSG00000179950.
ENST00000453551; ENSP00000402953; ENSG00000179950.
ENST00000456095; ENSP00000395417; ENSG00000179950.
ENST00000526683; ENSP00000434359; ENSG00000179950.
ENST00000527197; ENSP00000431960; ENSG00000179950.
ENST00000563311; ENSP00000454452; ENSG00000260485.
ENST00000563654; ENSP00000454436; ENSG00000260485.
ENST00000566765; ENSP00000455879; ENSG00000260485.
ENST00000567937; ENSP00000456640; ENSG00000260485.
ENST00000568960; ENSP00000454822; ENSG00000260485.
ENST00000569567; ENSP00000456170; ENSG00000260485.

GeneID

22827.

KEGG

hsa:22827.

UCSC

uc003yzq.3. human.
uc003yzr.3. human.
uc003yzt.3. human.

Organism-specific databases

CTD

22827.

GeneCards

GC08M144898.

HGNC

HGNC:17042. PUF60.

HPA

HPA045733.

MIM

604819. gene.

neXtProt

NX_Q9UHX1.

PharmGKB

PA162400364.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOVERGEN

HBG055622.

InParanoid

Q9UHX1.

KO

K12838.

OMA

CLQQVNG.

Gene expression databases

ArrayExpress

Q9UHX1.

Bgee

Q9UHX1.

CleanEx

HS_PUF60.

Genevestigator

Q9UHX1.

Family and domain databases

Gene3D

3.30.70.330. 3 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR006532. PolyU-bd.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
SM00361. RRM_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01645. half-pint. 1 hit.

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UHX1.

GenomeRNAi

22827.

NextBio

43236.

SOURCE

Search...

Entry information

Entry name

PUF60_HUMAN

Accession

Primary (citable) accession number: Q9UHX1
Secondary accession number(s): A8K8K8 , Q969E7, Q96D94, Q96H63, Q99628, Q9NZA0, Q9UJY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 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.