Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O75400 (PR40A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length957 AA.
Sequence statusComplete.
Protein existenceEvidence 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 6 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:

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 957957Pre-mRNA-processing factor 40 homolog A
PRO_0000076085

Regions

Domain140 – 17334WW 1
Domain181 – 21434WW 2
Domain393 – 44755FF 1
Domain460 – 51455FF 2
Domain527 – 58761FF 3
Domain607 – 66761FF 4
Domain672 – 72756FF 5
Domain742 – 79958FF 6

Amino acid modifications

Modified residue1511Phosphoserine Ref.15
Modified residue1961N6-acetyllysine Ref.14
Modified residue3731Phosphothreonine Ref.10 Ref.15 Ref.18
Modified residue8831Phosphoserine Ref.10 Ref.18
Modified residue8851Phosphoserine Ref.10
Modified residue8881Phosphoserine Ref.10 Ref.18
Modified residue9321Phosphothreonine Ref.12
Modified residue9331Phosphoserine Ref.12 Ref.15 Ref.18
Modified residue9351Phosphoserine Ref.12
Modified residue9381Phosphoserine Ref.10 Ref.12 Ref.15 Ref.18

Natural variations

Alternative sequence11M → MCSGSGRRRSSLSPTM in isoform 2 and isoform 5.
VSP_040781
Alternative sequence14 – 5542Missing in isoform 2 and isoform 5.
VSP_008047
Alternative sequence127 – 1282PG → LN in isoform 5.
VSP_040782
Alternative sequence129 – 957829Missing in isoform 5.
VSP_040783
Alternative sequence220 – 23718Missing in isoform 3.
VSP_008048

Experimental info

Sequence conflict372 – 3732FT → LL in AAB93495. Ref.5
Sequence conflict4331K → N in AAC27501. Ref.3
Sequence conflict4331K → N in AAC27506. Ref.3
Sequence conflict7871S → P in BAA91277. Ref.1

Secondary structure

.......................................... 957
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 22, 2003. Version 2.
Checksum: 8874D0C1CE1FCDAF

FASTA957108,805
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 6AFC2E30F4FAEB47
Show »

FASTA930105,927
Isoform 3 [UniParc].

Checksum: 05527BF2FC5C9449
Show »

FASTA939106,907
Isoform 5 [UniParc].

Checksum: 2C254F75EDA2059D
Show »

FASTA10110,697

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
RefSeqNP_060362.3. NM_017892.3.
UniGeneHs.643580.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UZCNMR-A381-450[»]
1YWINMR-A142-173[»]
1YWJNMR-A142-173[»]
1ZR7NMR-A146-173[»]
2CQNNMR-A743-806[»]
2DYFNMR-A146-173[»]
2KZGNMR-A381-450[»]
2L5FNMR-A133-220[»]
2L9VNMR-A390-438[»]
2LKSNMR-A391-439[»]
ProteinModelPortalO75400.
SMRO75400. Positions 133-222, 382-450, 452-674, 743-806.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120792. 136 interactions.
IntActO75400. 69 interactions.
MINTMINT-1180299.
STRING9606.ENSP00000402094.

PTM databases

PhosphoSiteO75400.

Proteomic databases

PaxDbO75400.
PRIDEO75400.

Protocols and materials databases

DNASU55660.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000410080; ENSP00000386458; ENSG00000196504. [O75400-2]
GeneID55660.
KEGGhsa:55660.
UCSCuc002tyh.4. human. [O75400-2]
uc002tyi.2. human. [O75400-1]

Organism-specific databases

CTD55660.
GeneCardsGC02M153508.
HGNCHGNC:16463. PRPF40A.
HPAHPA038272.
HPA038273.
MIM612941. gene.
neXtProtNX_O75400.
PharmGKBPA28195.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5104.
HOVERGENHBG059634.
KOK12821.
OMAMMGHPGM.
OrthoDBEOG77Q4X2.
PhylomeDBO75400.
TreeFamTF318732.

Enzyme and pathway databases

SignaLinkO75400.

Gene expression databases

ArrayExpressO75400.
BgeeO75400.
CleanExHS_PRPF40A.
GenevestigatorO75400.

Family and domain databases

Gene3D1.10.10.440. 4 hits.
InterProIPR002713. FF_domain.
IPR001202. WW_dom.
[Graphical view]
PfamPF01846. FF. 5 hits.
PF00397. WW. 2 hits.
[Graphical view]
SMARTSM00441. FF. 5 hits.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF51045. SSF51045. 2 hits.
SSF81698. SSF81698. 5 hits.
PROSITEPS51676. FF. 6 hits.
PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRPF40A. human.
EvolutionaryTraceO75400.
GeneWikiPRPF40A.
GenomeRNAi55660.
NextBio60391.
PMAP-CutDBO75400.
PROO75400.
SOURCESearch...

Entry information

Entry namePR40A_HUMAN
AccessionPrimary (citable) accession number: O75400
Secondary accession number(s): O43856 expand/collapse secondary AC list , O75404, Q8TBQ1, Q9H782, Q9NWU9, Q9P0Q2, Q9Y5A8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM