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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

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.By similarity1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

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
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 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. 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 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

BgeeiO75400.
CleanExiHS_PRPF40A.
ExpressionAtlasiO75400. baseline and differential.
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. 155 interactions.
IntActiO75400. 70 interactions.
MINTiMINT-1180299.
STRINGi9606.ENSP00000402094.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00740000115182.
HOVERGENiHBG059634.
InParanoidiO75400.
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

        10         20         30         40         50
MRPGTGAERG GLMVSEMESH PPSQGPGDGE RRLSGSSLCS GSWVSADGFL
60 70 80 90 100
RRRPSMGHPG MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM
110 120 130 140 150
PGMMSSVMPG MMMSHMSQAS MQPALPPGVN SMDVAAGTAS GAKSMWTEHK
160 170 180 190 200
SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ LLSKCPWKEY KSDSGKPYYY
210 220 230 240 250
NSQTKESRWA KPKELEDLEG YQNTIVAGSL ITKSNLHAMI KAEESSKQEE
260 270 280 290 300
CTTTSTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA AAAANANAST
310 320 330 340 350
SASNTVSGTV PVVPEPEVTS IVATVVDNEN TVTISTEEQA QLTSTPAIQD
360 370 380 390 400
QSVEVSSNTG EETSKQETVA DFTPKKEEEE SQPAKKTYTW NTKEEAKQAF
410 420 430 440 450
KELLKEKRVP SNASWEQAMK MIINDPRYSA LAKLSEKKQA FNAYKVQTEK
460 470 480 490 500
EEKEEARSKY KEAKESFQRF LENHEKMTST TRYKKAEQMF GEMEVWNAIS
510 520 530 540 550
ERDRLEIYED VLFFLSKKEK EQAKQLRKRN WEALKNILDN MANVTYSTTW
560 570 580 590 600
SEAQQYLMDN PTFAEDEELQ NMDKEDALIC FEEHIRALEK EEEEEKQKSL
610 620 630 640 650
LRERRRQRKN RESFQIFLDE LHEHGQLHSM SSWMELYPTI SSDIRFTNML
660 670 680 690 700
GQPGSTALDL FKFYVEDLKA RYHDEKKIIK DILKDKGFVV EVNTTFEDFV
710 720 730 740 750
AIISSTKRST TLDAGNIKLA FNSLLEKAEA REREREKEEA RKMKRKESAF
760 770 780 790 800
KSMLKQAAPP IELDAVWEDI RERFVKEPAF EDITLESERK RIFKDFMHVL
810 820 830 840 850
EHECQHHHSK NKKHSKKSKK HHRKRSRSRS GSDSDDDDSH SKKKRQRSES
860 870 880 890 900
RSASEHSSSA ESERSYKKSK KHKKKSKKRR HKSDSPESDA EREKDKKEKD
910 920 930 940 950
RESEKDRTRQ RSESKHKSPK KKTGKDSGNW DTSGSELSEG ELEKRRRTLL

EQLDDDQ
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 AAC27501.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC27502.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC27506.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAD42862.1 differs from that shown. Reason: Frameshift at position 953. Curated
The sequence AAF36145.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAH11788.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 409.Curated
The sequence BAA91277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15016.1 differs from that shown. Reason: Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 155 interactions.
IntActi O75400. 70 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.
GeneTreei ENSGT00740000115182.
HOVERGENi HBG059634.
InParanoidi O75400.
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

Bgeei O75400.
CleanExi HS_PRPF40A.
ExpressionAtlasi O75400. baseline and differential.
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: November 26, 2014
This is version 147 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