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O75400

- PR40A_HUMAN

UniProt

O75400 - PR40A_HUMAN

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Protein
Pre-mRNA-processing factor 40 homolog A
Gene
PRPF40A, FBP11, FLAF1, FNBP3, HIP10, HYPA, HSPC225
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

GO - Molecular functioni

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

GO - Biological processi

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

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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nuclear matrix Source: UniProtKB
  3. nuclear speck Source: UniProtKB-SubCell
  4. nucleus Source: HPA
Complete GO annotation...

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 A
PRO_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.2 Publications

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

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.

Miscellaneous databases

EvolutionaryTraceiO75400.

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

Belongs to the PRPF40 family.
Contains 6 FF domains.
Contains 2 WW domains.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MCSGSGRRRSSLSPTM in isoform 2 and isoform 5.
VSP_040781
Alternative sequencei14 – 5542Missing in isoform 2 and isoform 5.
VSP_008047Add
BLAST
Alternative sequencei127 – 1282PG → LN in isoform 5.
VSP_040782
Alternative sequencei129 – 957829Missing in isoform 5.
VSP_040783Add
BLAST
Alternative sequencei220 – 23718Missing in isoform 3.
VSP_008048Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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