SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14671

- PUM1_HUMAN

UniProt

Q14671 - PUM1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pumilio homolog 1

Gene
PUM1, KIAA0099, PUMH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Sequence-specific RNA-binding protein that negatively regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE). Capable of deadenylation-dependent and -independent modes of repression. May be required to support proliferation and self-renewal of stem cells.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. membrane organization Source: Reactome
  2. post-Golgi vesicle-mediated transport Source: Reactome
  3. regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Pumilio homolog 1
Short name:
HsPUM
Short name:
Pumilio-1
Gene namesi
Name:PUM1
Synonyms:KIAA0099, PUMH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14957. PUM1.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1043 – 10442NY → SN: Changes the specificity for RNA; when associated with E-1047.
Mutagenesisi1047 – 10471Q → E: Changes the specificity for RNA; when associated with 1043-SN-1044. 1 Publication

Organism-specific databases

PharmGKBiPA34042.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11861185Pumilio homolog 1PRO_0000075917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei75 – 751Phosphoserine3 Publications
Modified residuei98 – 981Phosphoserine1 Publication
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei124 – 1241Phosphoserine By similarity
Modified residuei209 – 2091Phosphoserine4 Publications
Modified residuei709 – 7091Phosphoserine4 Publications
Modified residuei806 – 8061Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14671.
PaxDbiQ14671.
PRIDEiQ14671.

2D gel databases

UCD-2DPAGEQ14671.

PTM databases

PhosphoSiteiQ14671.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, muscle, intestine and stomach. Not expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed in all fetal tissues tested.1 Publication

Inductioni

Strongly down-regulated in keratinocytes upon UVB irradiation.1 Publication

Gene expression databases

ArrayExpressiQ14671.
BgeeiQ14671.
CleanExiHS_PUM1.
GenevestigatoriQ14671.

Organism-specific databases

HPAiHPA027424.

Interactioni

Subunit structurei

Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation.1 Publication

Protein-protein interaction databases

BioGridi115050. 21 interactions.
DIPiDIP-29082N.
IntActiQ14671. 12 interactions.
MINTiMINT-1199500.
STRINGi9606.ENSP00000391723.

Structurei

Secondary structure

1
1186
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi831 – 8377
Helixi846 – 8494
Turni850 – 8523
Helixi853 – 8575
Helixi860 – 87213
Helixi875 – 88511
Helixi886 – 8883
Helixi889 – 8935
Helixi898 – 90811
Helixi911 – 92111
Helixi925 – 9295
Helixi934 – 94411
Helixi947 – 9548
Helixi955 – 9573
Helixi961 – 9666
Helixi970 – 98011
Helixi983 – 9864
Helixi987 – 9926
Turni993 – 9964
Helixi997 – 10015
Helixi1006 – 101611
Helixi1019 – 103113
Helixi1033 – 10364
Helixi1042 – 105211
Helixi1055 – 106511
Turni1066 – 10683
Helixi1069 – 10735
Helixi1078 – 108811
Helixi1091 – 110313
Beta strandi1104 – 11063
Beta strandi1107 – 11093
Helixi1111 – 11166
Helixi1121 – 113111
Helixi1134 – 11429
Helixi1145 – 11473
Helixi1148 – 11514
Beta strandi1153 – 11553
Helixi1157 – 11648
Turni1165 – 11673

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IB2X-ray1.90A828-1176[»]
1M8WX-ray2.20A/B828-1176[»]
1M8XX-ray2.20A/B828-1176[»]
1M8YX-ray2.60A/B828-1176[»]
1M8ZX-ray1.90A828-1176[»]
2YJYX-ray2.60A/B828-1176[»]
3BSBX-ray2.80A/B828-1170[»]
3BSXX-ray2.32A/B828-1170[»]
3Q0LX-ray2.50A/B828-1176[»]
3Q0MX-ray2.70A/B828-1176[»]
3Q0NX-ray2.40A/B828-1176[»]
3Q0OX-ray2.80A/B828-1176[»]
3Q0PX-ray2.60A/B828-1176[»]
ProteinModelPortaliQ14671.
SMRiQ14671. Positions 792-1165.

Miscellaneous databases

EvolutionaryTraceiQ14671.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini828 – 1168341PUM-HDAdd
BLAST
Repeati848 – 88336Pumilio 1Add
BLAST
Repeati884 – 91936Pumilio 2Add
BLAST
Repeati920 – 95536Pumilio 3Add
BLAST
Repeati956 – 99136Pumilio 4Add
BLAST
Repeati992 – 102736Pumilio 5Add
BLAST
Repeati1028 – 106336Pumilio 6Add
BLAST
Repeati1064 – 109936Pumilio 7Add
BLAST
Repeati1103 – 114240Pumilio 8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi393 – 613221Ala-richAdd
BLAST
Compositional biasi475 – 52349Gln-richAdd
BLAST
Compositional biasi642 – 815174Ser-richAdd
BLAST

Domaini

The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half doughnut. RNA-binding occurs on the concave side of the surface (1 Publication).

Sequence similaritiesi

Contains 1 PUM-HD domain.
Contains 8 pumilio repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5099.
HOGENOMiHOG000238461.
HOVERGENiHBG049462.
KOiK17943.
PhylomeDBiQ14671.
TreeFamiTF318160.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamiPF00806. PUF. 8 hits.
[Graphical view]
SMARTiSM00025. Pumilio. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14671-1) [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

MSVACVLKRK AVLWQDSFSP HLKHHPQEPA NPNMPVVLTS GTGSQAQPQP     50
AANQALAAGT HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG 100
GGYNNSKHRW PTGDNIHAEH QVRSMDELNH DFQALALEGR AMGEQLLPGK 150
KFWETDESSK DGPKGIFLGD QWRDSAWGTS DHSVSQPIMV QRRPGQSFHV 200
NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF GPRDADSDEN 250
DKGEKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDA DVKDFSRTPG 300
NCQNSANEVD LLGPNQNGSE GLAQLTSTNG AKPVEDFSNM ESQSVPLDPM 350
EHVGMEPLQF DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT 400
AAQQQQYALA AAHQPHIGLA PAAFVPNPYI ISAAPPGTDP YTAGLAAAAT 450
LGPAVVPHQY YGVTPWGVYP ASLFQQQAAA AAAATNSANQ QTTPQAQQGQ 500
QQVLRGGASQ RPLTPNQNQQ GQQTDPLVAA AAVNSALAFG QGLAAGMPGY 550
PVLAPAAYYD QTGALVVNAG ARNGLGAPVR LVAPAPVIIS SSAAQAAVAA 600
AAASANGAAG GLAGTTNGPF RPLGTQQPQP QPQQQPNNNL ASSSFYGNNS 650
LNSNSQSSSL FSQGSAQPAN TSLGFGSSSS LGATLGSALG GFGTAVANSN 700
TGSGSRRDSL TGSSDLYKRT SSSLTPIGHS FYNGLSFSSS PGPVGMPLPS 750
QGPGHSQTPP PSLSSHGSSS SLNLGGLTNG SGRYISAAPG AEAKYRSASS 800
ASSLFSPSST LFSSSRLRYG MSDVMPSGRS RLLEDFRNNR YPNLQLREIA 850
GHIMEFSQDQ HGSRFIQLKL ERATPAERQL VFNEILQAAY QLMVDVFGNY 900
VIQKFFEFGS LEQKLALAER IRGHVLSLAL QMYGCRVIQK ALEFIPSDQQ 950
NEMVRELDGH VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFAL 1000
STHPYGCRVI QRILEHCLPD QTLPILEELH QHTEQLVQDQ YGNYVIQHVL 1050
EHGRPEDKSK IVAEIRGNVL VLSQHKFASN VVEKCVTHAS RTERAVLIDE 1100
VCTMNDGPHS ALYTMMKDQY ANYVVQKMID VAEPGQRKIV MHKIRPHIAT 1150
LRKYTYGKHI LAKLEKYYMK NGVDLGPICG PPNGII 1186
Length:1,186
Mass (Da):126,473
Last modified:February 2, 2004 - v3
Checksum:iE1E0D8B3B0181308
GO
Isoform 2 (identifier: Q14671-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     417-417: I → IA
     597-623: Missing.
     950-950: Q → QVI

Note: No experimental confirmation available.

Show »
Length:1,162
Mass (Da):124,420
Checksum:i84FF134AA644F074
GO
Isoform 3 (identifier: Q14671-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     950-950: Q → QVI

Note: No experimental confirmation available.

Show »
Length:1,188
Mass (Da):126,685
Checksum:i2CA1B7A40A641F4C
GO
Isoform 4 (identifier: Q14671-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPLPPPGPGPEPIPGCTAPTQSPVGRHVVGVKGVGGM
     145-240: Missing.
     417-417: I → IA

Note: No experimental confirmation available.

Show »
Length:1,127
Mass (Da):119,558
Checksum:i296596BFAD017D3F
GO

Sequence cautioni

The sequence BAA07895.3 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPLPPPGPGPEPIPGCTAPT QSPVGRHVVGVKGVGGM in isoform 4. VSP_053703
Alternative sequencei145 – 24096Missing in isoform 4. VSP_053704Add
BLAST
Alternative sequencei417 – 4171I → IA in isoform 2 and isoform 4. VSP_017059
Alternative sequencei597 – 62327Missing in isoform 2. VSP_017060Add
BLAST
Alternative sequencei950 – 9501Q → QVI in isoform 2 and isoform 3. VSP_017061

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161G → E in BAD96325. 1 Publication
Sequence conflicti469 – 4691Y → N in BAD96325. 1 Publication
Sequence conflicti893 – 8931M → N in BAA07895. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF315592 mRNA. Translation: AAG31807.1.
D43951 mRNA. Translation: BAA07895.3. Different initiation.
AL356320, AL445235 Genomic DNA. Translation: CAH71203.1.
AK291779 mRNA. Translation: BAF84468.1.
AK294477 mRNA. Translation: BAG57703.1.
AK222605 mRNA. Translation: BAD96325.1.
AL445235, AL356320 Genomic DNA. Translation: CAI22246.1.
CH471059 Genomic DNA. Translation: EAX07633.1.
CH471059 Genomic DNA. Translation: EAX07634.1.
BC013398 mRNA. Translation: AAH13398.1.
CCDSiCCDS338.1. [Q14671-1]
CCDS44099.1. [Q14671-3]
RefSeqiNP_001018494.1. NM_001020658.1. [Q14671-3]
NP_055491.1. NM_014676.2. [Q14671-1]
UniGeneiHs.281707.

Genome annotation databases

EnsembliENST00000257075; ENSP00000257075; ENSG00000134644. [Q14671-1]
ENST00000373742; ENSP00000362847; ENSG00000134644. [Q14671-4]
ENST00000426105; ENSP00000391723; ENSG00000134644. [Q14671-3]
ENST00000440538; ENSP00000401777; ENSG00000134644. [Q14671-2]
GeneIDi9698.
KEGGihsa:9698.
UCSCiuc001bsi.1. human. [Q14671-1]
uc001bsj.1. human. [Q14671-2]

Polymorphism databases

DMDMi41688619.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF315592 mRNA. Translation: AAG31807.1 .
D43951 mRNA. Translation: BAA07895.3 . Different initiation.
AL356320 , AL445235 Genomic DNA. Translation: CAH71203.1 .
AK291779 mRNA. Translation: BAF84468.1 .
AK294477 mRNA. Translation: BAG57703.1 .
AK222605 mRNA. Translation: BAD96325.1 .
AL445235 , AL356320 Genomic DNA. Translation: CAI22246.1 .
CH471059 Genomic DNA. Translation: EAX07633.1 .
CH471059 Genomic DNA. Translation: EAX07634.1 .
BC013398 mRNA. Translation: AAH13398.1 .
CCDSi CCDS338.1. [Q14671-1 ]
CCDS44099.1. [Q14671-3 ]
RefSeqi NP_001018494.1. NM_001020658.1. [Q14671-3 ]
NP_055491.1. NM_014676.2. [Q14671-1 ]
UniGenei Hs.281707.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IB2 X-ray 1.90 A 828-1176 [» ]
1M8W X-ray 2.20 A/B 828-1176 [» ]
1M8X X-ray 2.20 A/B 828-1176 [» ]
1M8Y X-ray 2.60 A/B 828-1176 [» ]
1M8Z X-ray 1.90 A 828-1176 [» ]
2YJY X-ray 2.60 A/B 828-1176 [» ]
3BSB X-ray 2.80 A/B 828-1170 [» ]
3BSX X-ray 2.32 A/B 828-1170 [» ]
3Q0L X-ray 2.50 A/B 828-1176 [» ]
3Q0M X-ray 2.70 A/B 828-1176 [» ]
3Q0N X-ray 2.40 A/B 828-1176 [» ]
3Q0O X-ray 2.80 A/B 828-1176 [» ]
3Q0P X-ray 2.60 A/B 828-1176 [» ]
ProteinModelPortali Q14671.
SMRi Q14671. Positions 792-1165.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115050. 21 interactions.
DIPi DIP-29082N.
IntActi Q14671. 12 interactions.
MINTi MINT-1199500.
STRINGi 9606.ENSP00000391723.

PTM databases

PhosphoSitei Q14671.

Polymorphism databases

DMDMi 41688619.

2D gel databases

UCD-2DPAGE Q14671.

Proteomic databases

MaxQBi Q14671.
PaxDbi Q14671.
PRIDEi Q14671.

Protocols and materials databases

DNASUi 9698.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257075 ; ENSP00000257075 ; ENSG00000134644 . [Q14671-1 ]
ENST00000373742 ; ENSP00000362847 ; ENSG00000134644 . [Q14671-4 ]
ENST00000426105 ; ENSP00000391723 ; ENSG00000134644 . [Q14671-3 ]
ENST00000440538 ; ENSP00000401777 ; ENSG00000134644 . [Q14671-2 ]
GeneIDi 9698.
KEGGi hsa:9698.
UCSCi uc001bsi.1. human. [Q14671-1 ]
uc001bsj.1. human. [Q14671-2 ]

Organism-specific databases

CTDi 9698.
GeneCardsi GC01M031405.
HGNCi HGNC:14957. PUM1.
HPAi HPA027424.
MIMi 607204. gene.
neXtProti NX_Q14671.
PharmGKBi PA34042.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5099.
HOGENOMi HOG000238461.
HOVERGENi HBG049462.
KOi K17943.
PhylomeDBi Q14671.
TreeFami TF318160.

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSi PUM1. human.
EvolutionaryTracei Q14671.
GeneWikii PUM1.
GenomeRNAii 9698.
NextBioi 35471694.
PROi Q14671.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14671.
Bgeei Q14671.
CleanExi HS_PUM1.
Genevestigatori Q14671.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view ]
Pfami PF00806. PUF. 8 hits.
[Graphical view ]
SMARTi SM00025. Pumilio. 8 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and comparative sequence analysis of PUM1 and PUM2 genes, human members of the Pumilio family of RNA-binding proteins."
    Spassov D.S., Jurecic R.
    Gene 299:195-204(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Bone marrow.
  3. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Coronary artery.
  5. "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] (ISOFORMS 1 AND 4).
    Tissue: Amygdala and Placenta.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Muscle.
  9. "Genome-wide comparison of human keratinocyte and squamous cell carcinoma responses to UVB irradiation: implications for skin and epithelial cancer."
    Dazard J.-E., Gal H., Amariglio N., Rechavi G., Domany E., Givol D.
    Oncogene 22:2993-3006(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  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 SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(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 SER-19; SER-75; SER-209 AND SER-709, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-209; SER-709 AND SER-806, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-98; SER-106; SER-209 AND SER-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 SER-75 AND SER-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Human Pumilio proteins recruit multiple deadenylases to efficiently repress messenger RNAs."
    Van Etten J., Schagat T.L., Hrit J., Weidmann C.A., Brumbaugh J., Coon J.J., Goldstrohm A.C.
    J. Biol. Chem. 287:36370-36383(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH A DEADENYLASE COMPLEX.
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "Crystal structure of a Pumilio homology domain."
    Wang X., Zamore P.D., Hall T.M.T.
    Mol. Cell 7:855-865(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 828-1166.
  20. "Modular recognition of RNA by a human pumilio-homology domain."
    Wang X., McLachlan J., Zamore P.D., Hall T.M.T.
    Cell 110:501-512(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 828-1176 IN COMPLEX WITH RNA, MUTAGENESIS OF 1043-ASN-TYR-1044 AND GLN-1047.
  21. "Alternate modes of cognate RNA recognition by human PUMILIO proteins."
    Lu G., Hall T.M.
    Structure 19:361-367(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 828-1176 IN COMPLEX WITH CONSENSUS MRNA, FUNCTION, PUMILIO REPEATS.

Entry informationi

Entry nameiPUM1_HUMAN
AccessioniPrimary (citable) accession number: Q14671
Secondary accession number(s): A8K6W4
, B4DG92, D3DPN3, E9PCJ0, Q53HH5, Q5VXY7, Q9HAN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: September 3, 2014
This is version 132 of the entry and version 3 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 1
    Human chromosome 1: 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

Similar proteinsi