O75400 (PR40A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pre-mRNA-processing factor 40 homolog A

Alternative name(s):
Fas ligand-associated factor 1
Formin-binding protein 11
Formin-binding protein 3
Huntingtin yeast partner A
Huntingtin-interacting protein 10
Short name=HIP-10
Huntingtin-interacting protein A
Renal carcinoma antigen NY-REN-6

Gene names

Name:	PRPF40A
Synonyms:	FBP11, FLAF1, FNBP3, HIP10, HYPA
ORF Names:	HSPC225

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

General annotation (Comments)

Function	Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function By similarity. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. Ref.16
Subunit structure	Interacts with the N-terminus of HTT. Interacts with the phosphorylated C-terminal domain of POLR2A. Interacts with AKAP8L, SF1, SRPK1, CARD8, ATBF1 and MECP2 By similarity. Interacts through the WW domains with formin proline-rich regions and with WASL/N-WASP By similarity. Ref.3 Ref.8
Subcellular location	Nucleus speckle By similarity. Nucleus matrix. Note: Colocalizes with AKAP8L in the nuclear matrix By similarity. Ref.9
Tissue specificity	Expressed in the brain cortex (at protein level). Widely expressed. Ref.3 Ref.9
Domain	The WW domains are essential for localization to nuclear speckles By similarity.
Sequence similarities	Belongs to the PRPF40 family. Contains 5 FF domains. Contains 2 WW domains.
Sequence caution	The sequence AAC27501.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAC27502.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAC27506.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAD42862.1 differs from that shown. Reason: Frameshift at position 953. The sequence AAF36145.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAH11788.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 409. The sequence BAA91277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB15016.1 differs from that shown. Reason:

Ontologies

Keywords
Biological process	Cell cycle Cell division mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell migration Inferred from mutant phenotype Ref.16. Source: UniProtKB cytoskeleton organization Inferred from mutant phenotype Ref.16. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from mutant phenotype Ref.16. Source: UniProtKB regulation of cytokinesis Inferred from mutant phenotype Ref.16. Source: UniProtKB
Cellular_component	nuclear matrix Inferred from direct assay Ref.9. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHD3	Q12873	2	EBI-473291,EBI-523590
HTT	P42858	3	EBI-473291,EBI-466029

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75400-1)

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: O75400-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCSGSGRRRSSLSPTM
     14-55: Missing.

Isoform 3 (identifier: O75400-3)

The sequence of this isoform differs from the canonical sequence as follows:
     220-237: Missing.

Isoform 5 (identifier: O75400-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCSGSGRRRSSLSPTM
     14-55: Missing.
     127-128: PG → LN
     129-957: Missing.

Note: Probable target of nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 957

957

Pre-mRNA-processing factor 40 homolog A

PRO_0000076085

Regions

Domain

140 – 173

34

WW 1

Domain

181 – 214

34

WW 2

Domain

393 – 447

55

FF 1

Domain

460 – 519

60

FF 2

Domain

527 – 587

61

FF 3

Domain

607 – 667

61

FF 4

Domain

743 – 799

57

FF 5

Amino acid modifications

Modified residue

36

1

Phosphoserine By similarity

Modified residue

151

1

Phosphoserine Ref.15

Modified residue

196

1

N6-acetyllysine Ref.14

Modified residue

373

1

Phosphothreonine Ref.10 Ref.15 Ref.18

Modified residue

828

1

Phosphoserine By similarity

Modified residue

830

1

Phosphoserine By similarity

Modified residue

832

1

Phosphoserine By similarity

Modified residue

834

1

Phosphoserine By similarity

Modified residue

883

1

Phosphoserine Ref.10 Ref.18

Modified residue

885

1

Phosphoserine Ref.10

Modified residue

888

1

Phosphoserine Ref.10 Ref.18

Modified residue

932

1

Phosphothreonine Ref.12

Modified residue

933

1

Phosphoserine Ref.12 Ref.15 Ref.18

Modified residue

935

1

Phosphoserine Ref.12

Modified residue

938

1

Phosphoserine Ref.10 Ref.12 Ref.15 Ref.18

Natural variations

Alternative sequence

1

1

M → MCSGSGRRRSSLSPTM in isoform 2 and isoform 5.

VSP_040781

Alternative sequence

14 – 55

42

Missing in isoform 2 and isoform 5.

VSP_008047

Alternative sequence

127 – 128

2

PG → LN in isoform 5.

VSP_040782

Alternative sequence

129 – 957

829

Missing in isoform 5.

VSP_040783

Alternative sequence

220 – 237

18

Missing in isoform 3.

VSP_008048

Experimental info

Sequence conflict

372 – 373

2

FT → LL in AAB93495. Ref.5

Sequence conflict

433

1

K → N in AAC27501. Ref.3

Sequence conflict

433

1

K → N in AAC27506. Ref.3

Sequence conflict

787

1

S → P in BAA91277. Ref.1

Secondary structure

1

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957

Helix Strand Turn

Details...

Beta strand

136 – 138

3

Turn

142 – 145

4

Beta strand

146 – 151

6

Turn

152 – 154

3

Beta strand

155 – 160

6

Turn

161 – 164

4

Beta strand

165 – 169

5

Helix

172 – 174

3

Helix

177 – 183

7

Beta strand

186 – 191

6

Beta strand

197 – 201

5

Turn

202 – 205

4

Beta strand

206 – 209

4

Helix

213 – 216

4

Beta strand

218 – 220

3

Helix

393 – 406

14

Beta strand

411 – 413

3

Helix

415 – 423

9

Helix

426 – 430

5

Helix

434 – 447

14

Helix

743 – 755

13

Helix

767 – 774

8

Helix

778 – 781

4

Helix

786 – 804

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 22, 2003. Version 2. Checksum: 8874D0C1CE1FCDAF	FASTA	957	108,805
	10 20 30 40 50 60 MRPGTGAERG GLMVSEMESH PPSQGPGDGE RRLSGSSLCS GSWVSADGFL RRRPSMGHPG 70 80 90 100 110 120 MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM PGMMSSVMPG MMMSHMSQAS 130 140 150 160 170 180 MQPALPPGVN SMDVAAGTAS GAKSMWTEHK SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ 190 200 210 220 230 240 LLSKCPWKEY KSDSGKPYYY NSQTKESRWA KPKELEDLEG YQNTIVAGSL ITKSNLHAMI 250 260 270 280 290 300 KAEESSKQEE CTTTSTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA AAAANANAST 310 320 330 340 350 360 SASNTVSGTV PVVPEPEVTS IVATVVDNEN TVTISTEEQA QLTSTPAIQD QSVEVSSNTG 370 380 390 400 410 420 EETSKQETVA DFTPKKEEEE SQPAKKTYTW NTKEEAKQAF KELLKEKRVP SNASWEQAMK 430 440 450 460 470 480 MIINDPRYSA LAKLSEKKQA FNAYKVQTEK EEKEEARSKY KEAKESFQRF LENHEKMTST 490 500 510 520 530 540 TRYKKAEQMF GEMEVWNAIS ERDRLEIYED VLFFLSKKEK EQAKQLRKRN WEALKNILDN 550 560 570 580 590 600 MANVTYSTTW SEAQQYLMDN PTFAEDEELQ NMDKEDALIC FEEHIRALEK EEEEEKQKSL 610 620 630 640 650 660 LRERRRQRKN RESFQIFLDE LHEHGQLHSM SSWMELYPTI SSDIRFTNML GQPGSTALDL 670 680 690 700 710 720 FKFYVEDLKA RYHDEKKIIK DILKDKGFVV EVNTTFEDFV AIISSTKRST TLDAGNIKLA 730 740 750 760 770 780 FNSLLEKAEA REREREKEEA RKMKRKESAF KSMLKQAAPP IELDAVWEDI RERFVKEPAF 790 800 810 820 830 840 EDITLESERK RIFKDFMHVL EHECQHHHSK NKKHSKKSKK HHRKRSRSRS GSDSDDDDSH 850 860 870 880 890 900 SKKKRQRSES RSASEHSSSA ESERSYKKSK KHKKKSKKRR HKSDSPESDA EREKDKKEKD 910 920 930 940 950 RESEKDRTRQ RSESKHKSPK KKTGKDSGNW DTSGSELSEG ELEKRRRTLL EQLDDDQ
	Isoform 2 [UniParc]. Checksum: 6AFC2E30F4FAEB47	FASTA	930	105,927
	10 20 30 40 50 60 MCSGSGRRRS SLSPTMRPGT GAERGGLMMG HPGMHYAPMG MHPMGQRANM PPVPHGMMPQ 70 80 90 100 110 120 MMPPMGGPPM GQMPGMMSSV MPGMMMSHMS QASMQPALPP GVNSMDVAAG TASGAKSMWT 130 140 150 160 170 180 EHKSPDGRTY YYNTETKQST WEKPDDLKTP AEQLLSKCPW KEYKSDSGKP YYYNSQTKES 190 200 210 220 230 240 RWAKPKELED LEGYQNTIVA GSLITKSNLH AMIKAEESSK QEECTTTSTA PVPTTEIPTT 250 260 270 280 290 300 MSTMAAAEAA AAVVAAAAAA AAAAAAANAN ASTSASNTVS GTVPVVPEPE VTSIVATVVD 310 320 330 340 350 360 NENTVTISTE EQAQLTSTPA IQDQSVEVSS NTGEETSKQE TVADFTPKKE EEESQPAKKT 370 380 390 400 410 420 YTWNTKEEAK QAFKELLKEK RVPSNASWEQ AMKMIINDPR YSALAKLSEK KQAFNAYKVQ 430 440 450 460 470 480 TEKEEKEEAR SKYKEAKESF QRFLENHEKM TSTTRYKKAE QMFGEMEVWN AISERDRLEI 490 500 510 520 530 540 YEDVLFFLSK KEKEQAKQLR KRNWEALKNI LDNMANVTYS TTWSEAQQYL MDNPTFAEDE 550 560 570 580 590 600 ELQNMDKEDA LICFEEHIRA LEKEEEEEKQ KSLLRERRRQ RKNRESFQIF LDELHEHGQL 610 620 630 640 650 660 HSMSSWMELY PTISSDIRFT NMLGQPGSTA LDLFKFYVED LKARYHDEKK IIKDILKDKG 670 680 690 700 710 720 FVVEVNTTFE DFVAIISSTK RSTTLDAGNI KLAFNSLLEK AEAREREREK EEARKMKRKE 730 740 750 760 770 780 SAFKSMLKQA APPIELDAVW EDIRERFVKE PAFEDITLES ERKRIFKDFM HVLEHECQHH 790 800 810 820 830 840 HSKNKKHSKK SKKHHRKRSR SRSGSDSDDD DSHSKKKRQR SESRSASEHS SSAESERSYK 850 860 870 880 890 900 KSKKHKKKSK KRRHKSDSPE SDAEREKDKK EKDRESEKDR TRQRSESKHK SPKKKTGKDS 910 920 930 GNWDTSGSEL SEGELEKRRR TLLEQLDDDQ
	Isoform 3 [UniParc]. Checksum: 05527BF2FC5C9449	FASTA	939	106,907
	10 20 30 40 50 60 MRPGTGAERG GLMVSEMESH PPSQGPGDGE RRLSGSSLCS GSWVSADGFL RRRPSMGHPG 70 80 90 100 110 120 MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM PGMMSSVMPG MMMSHMSQAS 130 140 150 160 170 180 MQPALPPGVN SMDVAAGTAS GAKSMWTEHK SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ 190 200 210 220 230 240 LLSKCPWKEY KSDSGKPYYY NSQTKESRWA KPKELEDLEA MIKAEESSKQ EECTTTSTAP 250 260 270 280 290 300 VPTTEIPTTM STMAAAEAAA AVVAAAAAAA AAAAAANANA STSASNTVSG TVPVVPEPEV 310 320 330 340 350 360 TSIVATVVDN ENTVTISTEE QAQLTSTPAI QDQSVEVSSN TGEETSKQET VADFTPKKEE 370 380 390 400 410 420 EESQPAKKTY TWNTKEEAKQ AFKELLKEKR VPSNASWEQA MKMIINDPRY SALAKLSEKK 430 440 450 460 470 480 QAFNAYKVQT EKEEKEEARS KYKEAKESFQ RFLENHEKMT STTRYKKAEQ MFGEMEVWNA 490 500 510 520 530 540 ISERDRLEIY EDVLFFLSKK EKEQAKQLRK RNWEALKNIL DNMANVTYST TWSEAQQYLM 550 560 570 580 590 600 DNPTFAEDEE LQNMDKEDAL ICFEEHIRAL EKEEEEEKQK SLLRERRRQR KNRESFQIFL 610 620 630 640 650 660 DELHEHGQLH SMSSWMELYP TISSDIRFTN MLGQPGSTAL DLFKFYVEDL KARYHDEKKI 670 680 690 700 710 720 IKDILKDKGF VVEVNTTFED FVAIISSTKR STTLDAGNIK LAFNSLLEKA EAREREREKE 730 740 750 760 770 780 EARKMKRKES AFKSMLKQAA PPIELDAVWE DIRERFVKEP AFEDITLESE RKRIFKDFMH 790 800 810 820 830 840 VLEHECQHHH SKNKKHSKKS KKHHRKRSRS RSGSDSDDDD SHSKKKRQRS ESRSASEHSS 850 860 870 880 890 900 SAESERSYKK SKKHKKKSKK RRHKSDSPES DAEREKDKKE KDRESEKDRT RQRSESKHKS 910 920 930 PKKKTGKDSG NWDTSGSELS EGELEKRRRT LLEQLDDDQ
	Isoform 5 [UniParc]. Checksum: 2C254F75EDA2059D	FASTA	101	10,697
	10 20 30 40 50 60 MCSGSGRRRS SLSPTMRPGT GAERGGLMMG HPGMHYAPMG MHPMGQRANM PPVPHGMMPQ 70 80 90 100 MMPPMGGPPM GQMPGMMSSV MPGMMMSHMS QASMQPALPL N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-957 (ISOFORM 1). Tissue: Smooth muscle.
[2]	"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].
[3]	"Huntingtin interacts with a family of WW domain proteins." Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., MacDonald M.E. Hum. Mol. Genet. 7:1463-1474(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-448 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-423 (ISOFORM 2), INTERACTION WITH HTT, TISSUE SPECIFICITY. Tissue: Frontal cortex.
[4]	"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] OF 1-449 AND 743-957 (ISOFORM 2). Tissue: Lymphoma.
[5]	"A Fas-ligand associated factor 1, FLAF1, potentiates Fas-ligand stability." Hachiya T., Kobayasi A., Touji S., Tamai K. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-374 (ISOFORM 3). Tissue: Placenta.
[6]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 542-957, IDENTIFICATION AS A RENAL CANCER ANTIGEN.
[7]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-957. Tissue: Umbilical cord blood.
[8]	"The structure of an FF domain from human HYPA/FBP11." Allen M., Friedler A., Schon O., Bycroft M. J. Mol. Biol. 323:411-416(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POLR2A, STRUCTURE BY NMR OF 381-450.
[9]	"Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: implications for nuclear toxicity in Huntington's disease pathogenesis." Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M. NeuroMolecular Med. 7:297-310(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-373; SER-883; SER-885; SER-888 AND SER-938, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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 THR-932; SER-933; SER-935 AND SER-938, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[14]	"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-196, MASS SPECTROMETRY.
[15]	"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-151; THR-373; SER-933 AND SER-938, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration." Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J. BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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]	"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 THR-373; SER-883; SER-888; SER-933 AND SER-938, MASS SPECTROMETRY.
[19]	"Solution structure of the FF domain of human formin-binding protein 3." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 743-806.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AC012443 Genomic DNA. No translation available.
AC079344 Genomic DNA. No translation available.
AK000592 mRNA. Translation: BAA91277.1. Different initiation.
AK024810 mRNA. Translation: BAB15016.1. Sequence problems.
AF049523 mRNA. Translation: AAC27501.1. Different initiation.
AF049524 mRNA. Translation: AAC27502.1. Different initiation.
AF049528 mRNA. Translation: AAC27506.1. Different initiation.
BC011788 mRNA. Translation: AAH11788.1. Sequence problems.
BC027178 mRNA. Translation: AAH27178.1.
U70667 mRNA. Translation: AAB93495.1.
AF155096 mRNA. Translation: AAD42862.1. Frameshift.
AF151059 mRNA. Translation: AAF36145.1. Frameshift.

IPI

IPI00337385.
IPI00337386.
IPI00337387.
IPI00915929.

RefSeq

NP_060362.3. NM_017892.3.

UniGene

Hs.643580.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UZC	NMR	-	A	381-450	[»]
1YWI	NMR	-	A	142-173	[»]
1YWJ	NMR	-	A	142-173	[»]
1ZR7	NMR	-	A	146-173	[»]
2CQN	NMR	-	A	743-806	[»]
2DYF	NMR	-	A	146-173	[»]
2KZG	NMR	-	A	381-450	[»]
2L5F	NMR	-	A	133-220	[»]
2L9V	NMR	-	A	390-438	[»]
2LKS	NMR	-	A	391-439	[»]

ProteinModelPortal

O75400.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75400. 12 interactions.

MINT

MINT-1180299.

STRING

9606.ENSP00000402094.

PTM databases

PhosphoSite

O75400.

Proteomic databases

PaxDb

O75400.

PRIDE

O75400.

Protocols and materials databases

DNASU

55660.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000410080; ENSP00000386458; ENSG00000196504.

GeneID

55660.

KEGG

hsa:55660.

UCSC

uc002tyi.2. human.

Organism-specific databases

CTD

55660.

GeneCards

GC02M153508.

HGNC

HGNC:16463. PRPF40A.

HPA

HPA038273.

MIM

612941. gene.

neXtProt

NX_O75400.

PharmGKB

PA28195.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5104.

HOVERGEN

HBG059634.

KO

K12821.

Gene expression databases

ArrayExpress

O75400.

Bgee

O75400.

CleanEx

HS_PRPF40A.

Genevestigator

O75400.

GermOnline

ENSG00000196504. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.440. 4 hits.

InterPro

IPR002713. FF_domain.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF01846. FF. 5 hits.
PF00397. WW. 2 hits.
[Graphical view]

SMART

SM00441. FF. 5 hits.
SM00456. WW. 2 hits.
[Graphical view]

SUPFAM

SSF81698. FF. 4 hits.
SSF51045. WW_Rsp5_WWP. 2 hits.

PROSITE

PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PRPF40A. human.

EvolutionaryTrace

O75400.

GenomeRNAi

55660.

NextBio

60391.

PMAP-CutDB

O75400.

SOURCE

Search...

Entry information

Entry name

PR40A_HUMAN

Accession

Primary (citable) accession number: O75400
Secondary accession number(s): O43856 , O75404, Q8TBQ1, Q9H782, Q9NWU9, Q9P0Q2, Q9Y5A8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	August 22, 2003
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 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.