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O75400

- PR40A_HUMAN

UniProt

O75400 - PR40A_HUMAN

Protein

Pre-mRNA-processing factor 40 homolog A

Gene

PRPF40A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (22 Aug 2003)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. cell migration Source: UniProtKB
    4. cytoskeleton organization Source: UniProtKB
    5. mRNA processing Source: UniProtKB-KW
    6. regulation of cell shape Source: UniProtKB
    7. regulation of cytokinesis Source: UniProtKB
    8. RNA splicing Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, mRNA processing, mRNA splicing

    Enzyme and pathway databases

    SignaLinkiO75400.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:PRPF40A
    Synonyms:FBP11, FLAF1, FNBP3, HIP10, HYPA
    ORF Names:HSPC225
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:16463. PRPF40A.

    Subcellular locationi

    Nucleus speckle By similarity. Nucleus matrix 1 Publication
    Note: Colocalizes with AKAP8L in the nuclear matrix.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. membrane Source: UniProtKB
    3. nuclear matrix Source: UniProtKB
    4. nuclear speck Source: UniProtKB-SubCell
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28195.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 957957Pre-mRNA-processing factor 40 homolog APRO_0000076085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei151 – 1511Phosphoserine1 Publication
    Modified residuei196 – 1961N6-acetyllysine1 Publication
    Modified residuei373 – 3731Phosphothreonine3 Publications
    Modified residuei883 – 8831Phosphoserine2 Publications
    Modified residuei885 – 8851Phosphoserine1 Publication
    Modified residuei888 – 8881Phosphoserine2 Publications
    Modified residuei932 – 9321Phosphothreonine1 Publication
    Modified residuei933 – 9331Phosphoserine3 Publications
    Modified residuei935 – 9351Phosphoserine1 Publication
    Modified residuei938 – 9381Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75400.
    PaxDbiO75400.
    PRIDEiO75400.

    PTM databases

    PhosphoSiteiO75400.

    Miscellaneous databases

    PMAP-CutDBO75400.

    Expressioni

    Tissue specificityi

    Expressed in the brain cortex (at protein level). Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiO75400.
    BgeeiO75400.
    CleanExiHS_PRPF40A.
    GenevestigatoriO75400.

    Organism-specific databases

    HPAiHPA038272.
    HPA038273.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHD3Q128732EBI-473291,EBI-523590
    HTTP4285815EBI-473291,EBI-466029
    NKAPQ8N5F72EBI-473291,EBI-721539
    SF3A1Q154592EBI-473291,EBI-1054743

    Protein-protein interaction databases

    BioGridi120792. 143 interactions.
    IntActiO75400. 69 interactions.
    MINTiMINT-1180299.
    STRINGi9606.ENSP00000402094.

    Structurei

    Secondary structure

    1
    957
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi136 – 1383
    Turni142 – 1454
    Beta strandi146 – 1516
    Turni152 – 1543
    Beta strandi155 – 1606
    Turni161 – 1644
    Beta strandi165 – 1695
    Helixi172 – 1743
    Helixi177 – 1837
    Beta strandi186 – 1916
    Beta strandi197 – 2015
    Turni202 – 2054
    Beta strandi206 – 2094
    Helixi213 – 2164
    Beta strandi218 – 2203
    Helixi393 – 40614
    Beta strandi411 – 4133
    Helixi415 – 4239
    Helixi426 – 4305
    Helixi434 – 44714
    Helixi743 – 75513
    Helixi767 – 7748
    Helixi778 – 7814
    Helixi786 – 80419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO75400.
    SMRiO75400. Positions 133-222, 382-450, 743-806.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75400.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini140 – 17334WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini181 – 21434WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini393 – 44755FF 1Add
    BLAST
    Domaini460 – 51455FF 2Add
    BLAST
    Domaini527 – 58761FF 3Add
    BLAST
    Domaini607 – 66761FF 4Add
    BLAST
    Domaini672 – 72756FF 5Add
    BLAST
    Domaini742 – 79958FF 6Add
    BLAST

    Domaini

    The WW domains are essential for localization to nuclear speckles.By similarity

    Sequence similaritiesi

    Belongs to the PRPF40 family.Curated
    Contains 6 FF domains.Curated
    Contains 2 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5104.
    HOVERGENiHBG059634.
    KOiK12821.
    OMAiERGGLMM.
    OrthoDBiEOG77Q4X2.
    PhylomeDBiO75400.
    TreeFamiTF318732.

    Family and domain databases

    Gene3Di1.10.10.440. 4 hits.
    InterProiIPR002713. FF_domain.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF01846. FF. 5 hits.
    PF00397. WW. 2 hits.
    [Graphical view]
    SMARTiSM00441. FF. 5 hits.
    SM00456. WW. 2 hits.
    [Graphical view]
    SUPFAMiSSF51045. SSF51045. 2 hits.
    SSF81698. SSF81698. 5 hits.
    PROSITEiPS51676. FF. 6 hits.
    PS01159. WW_DOMAIN_1. 2 hits.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75400-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRPGTGAERG GLMVSEMESH PPSQGPGDGE RRLSGSSLCS GSWVSADGFL    50
    RRRPSMGHPG MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM 100
    PGMMSSVMPG MMMSHMSQAS MQPALPPGVN SMDVAAGTAS GAKSMWTEHK 150
    SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ LLSKCPWKEY KSDSGKPYYY 200
    NSQTKESRWA KPKELEDLEG YQNTIVAGSL ITKSNLHAMI KAEESSKQEE 250
    CTTTSTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA AAAANANAST 300
    SASNTVSGTV PVVPEPEVTS IVATVVDNEN TVTISTEEQA QLTSTPAIQD 350
    QSVEVSSNTG EETSKQETVA DFTPKKEEEE SQPAKKTYTW NTKEEAKQAF 400
    KELLKEKRVP SNASWEQAMK MIINDPRYSA LAKLSEKKQA FNAYKVQTEK 450
    EEKEEARSKY KEAKESFQRF LENHEKMTST TRYKKAEQMF GEMEVWNAIS 500
    ERDRLEIYED VLFFLSKKEK EQAKQLRKRN WEALKNILDN MANVTYSTTW 550
    SEAQQYLMDN PTFAEDEELQ NMDKEDALIC FEEHIRALEK EEEEEKQKSL 600
    LRERRRQRKN RESFQIFLDE LHEHGQLHSM SSWMELYPTI SSDIRFTNML 650
    GQPGSTALDL FKFYVEDLKA RYHDEKKIIK DILKDKGFVV EVNTTFEDFV 700
    AIISSTKRST TLDAGNIKLA FNSLLEKAEA REREREKEEA RKMKRKESAF 750
    KSMLKQAAPP IELDAVWEDI RERFVKEPAF EDITLESERK RIFKDFMHVL 800
    EHECQHHHSK NKKHSKKSKK HHRKRSRSRS GSDSDDDDSH SKKKRQRSES 850
    RSASEHSSSA ESERSYKKSK KHKKKSKKRR HKSDSPESDA EREKDKKEKD 900
    RESEKDRTRQ RSESKHKSPK KKTGKDSGNW DTSGSELSEG ELEKRRRTLL 950
    EQLDDDQ 957
    Length:957
    Mass (Da):108,805
    Last modified:August 22, 2003 - v2
    Checksum:i8874D0C1CE1FCDAF
    GO
    Isoform 2 (identifier: O75400-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:930
    Mass (Da):105,927
    Checksum:i6AFC2E30F4FAEB47
    GO
    Isoform 3 (identifier: O75400-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:939
    Mass (Da):106,907
    Checksum:i05527BF2FC5C9449
    GO
    Isoform 5 (identifier: O75400-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:101
    Mass (Da):10,697
    Checksum:i2C254F75EDA2059D
    GO

    Sequence cautioni

    The sequence AAH11788.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 409.
    The sequence BAB15016.1 differs from that shown. Reason:
    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 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 BAA91277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti372 – 3732FT → LL in AAB93495. 1 PublicationCurated
    Sequence conflicti433 – 4331K → N in AAC27501. (PubMed:9700202)Curated
    Sequence conflicti433 – 4331K → N in AAC27506. (PubMed:9700202)Curated
    Sequence conflicti787 – 7871S → P in BAA91277. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MCSGSGRRRSSLSPTM in isoform 2 and isoform 5. 3 PublicationsVSP_040781
    Alternative sequencei14 – 5542Missing in isoform 2 and isoform 5. 3 PublicationsVSP_008047Add
    BLAST
    Alternative sequencei127 – 1282PG → LN in isoform 5. 1 PublicationVSP_040782
    Alternative sequencei129 – 957829Missing in isoform 5. 1 PublicationVSP_040783Add
    BLAST
    Alternative sequencei220 – 23718Missing in isoform 3. 1 PublicationVSP_008048Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS46430.1. [O75400-2]
    RefSeqiNP_060362.3. NM_017892.3. [O75400-2]
    UniGeneiHs.643580.

    Genome annotation databases

    EnsembliENST00000410080; ENSP00000386458; ENSG00000196504. [O75400-2]
    GeneIDi55660.
    KEGGihsa:55660.
    UCSCiuc002tyh.4. human. [O75400-2]
    uc002tyi.2. human. [O75400-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS46430.1. [O75400-2 ]
    RefSeqi NP_060362.3. NM_017892.3. [O75400-2 ]
    UniGenei Hs.643580.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali O75400.
    SMRi O75400. Positions 133-222, 382-450, 743-806.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120792. 143 interactions.
    IntActi O75400. 69 interactions.
    MINTi MINT-1180299.
    STRINGi 9606.ENSP00000402094.

    PTM databases

    PhosphoSitei O75400.

    Proteomic databases

    MaxQBi O75400.
    PaxDbi O75400.
    PRIDEi O75400.

    Protocols and materials databases

    DNASUi 55660.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000410080 ; ENSP00000386458 ; ENSG00000196504 . [O75400-2 ]
    GeneIDi 55660.
    KEGGi hsa:55660.
    UCSCi uc002tyh.4. human. [O75400-2 ]
    uc002tyi.2. human. [O75400-1 ]

    Organism-specific databases

    CTDi 55660.
    GeneCardsi GC02M153508.
    HGNCi HGNC:16463. PRPF40A.
    HPAi HPA038272.
    HPA038273.
    MIMi 612941. gene.
    neXtProti NX_O75400.
    PharmGKBi PA28195.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5104.
    HOVERGENi HBG059634.
    KOi K12821.
    OMAi ERGGLMM.
    OrthoDBi EOG77Q4X2.
    PhylomeDBi O75400.
    TreeFami TF318732.

    Enzyme and pathway databases

    SignaLinki O75400.

    Miscellaneous databases

    ChiTaRSi PRPF40A. human.
    EvolutionaryTracei O75400.
    GeneWikii PRPF40A.
    GenomeRNAii 55660.
    NextBioi 60391.
    PMAP-CutDB O75400.
    PROi O75400.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75400.
    Bgeei O75400.
    CleanExi HS_PRPF40A.
    Genevestigatori O75400.

    Family and domain databases

    Gene3Di 1.10.10.440. 4 hits.
    InterProi IPR002713. FF_domain.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF01846. FF. 5 hits.
    PF00397. WW. 2 hits.
    [Graphical view ]
    SMARTi SM00441. FF. 5 hits.
    SM00456. WW. 2 hits.
    [Graphical view ]
    SUPFAMi SSF51045. SSF51045. 2 hits.
    SSF81698. SSF81698. 5 hits.
    PROSITEi PS51676. FF. 6 hits.
    PS01159. WW_DOMAIN_1. 2 hits.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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, 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. 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. 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.

    Entry informationi

    Entry nameiPR40A_HUMAN
    AccessioniPrimary (citable) accession number: O75400
    Secondary accession number(s): O43856
    , O75404, Q8TBQ1, Q9H782, Q9NWU9, Q9P0Q2, Q9Y5A8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: August 22, 2003
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3