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Q8TB72

- PUM2_HUMAN

UniProt

Q8TB72 - PUM2_HUMAN

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Protein

Pumilio homolog 2

Gene

PUM2

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. Its interactions and tissue specificity suggest that it may be required to support proliferation and self-renewal of stem cells by regulating the translation of key transcripts.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. stress granule assembly Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pumilio homolog 2
Short name:
Pumilio-2
Gene namesi
Name:PUM2
Synonyms:KIAA0235, PUMH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:14958. PUM2.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmic granule By similarity. Cytoplasmperinuclear region 1 Publication
Note: The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules (By similarity). Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells.By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic stress granule Source: UniProtKB
  3. nuclear membrane Source: HPA
  4. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10661066Pumilio homolog 2PRO_0000075919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Phosphoserine2 Publications
Modified residuei136 – 1361Phosphoserine3 Publications
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei182 – 1821Phosphoserine3 Publications
Modified residuei184 – 1841Phosphothreonine2 Publications
Modified residuei587 – 5871Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8TB72.
PaxDbiQ8TB72.
PRIDEiQ8TB72.

PTM databases

PhosphoSiteiQ8TB72.

Expressioni

Tissue specificityi

Expressed in male germ cells of adult testis (at protein level). Highly expressed in testis and ovary. Predominantly expressed in stem cells and germ cells. Expressed at lower level in brain, heart, kidney, liver, muscle, placenta, intestine and stomach Expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed in all fetal tissues tested.3 Publications

Inductioni

Down-regulated in keratinocytes upon UVB irradiation.1 Publication

Gene expression databases

BgeeiQ8TB72.
CleanExiHS_PUM2.
ExpressionAtlasiQ8TB72. baseline and differential.
GenevestigatoriQ8TB72.

Organism-specific databases

HPAiHPA030316.
HPA049670.

Interactioni

Subunit structurei

Homodimer; homodimerizes in vitro. Interacts with DAZ, DAZL and NANOS1 via its pumilio repeats. Interacts with NANOS3 (By similarity). Interacts with SNAPIN. Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Interacts with DDX20.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAZ1Q9NQZ35EBI-311190,EBI-997955
ORFQ9Q2G43EBI-311190,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi116949. 12 interactions.
IntActiQ8TB72. 6 interactions.
MINTiMINT-254513.
STRINGi9606.ENSP00000338173.

Structurei

Secondary structure

1
1066
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi709 – 7157Combined sources
Helixi724 – 7274Combined sources
Turni728 – 7303Combined sources
Helixi731 – 7355Combined sources
Helixi738 – 74811Combined sources
Helixi753 – 76513Combined sources
Helixi767 – 7715Combined sources
Turni774 – 7763Combined sources
Helixi777 – 78610Combined sources
Helixi789 – 79911Combined sources
Helixi803 – 8086Combined sources
Helixi812 – 82211Combined sources
Helixi828 – 8358Combined sources
Turni836 – 8394Combined sources
Helixi841 – 8466Combined sources
Helixi850 – 86011Combined sources
Helixi863 – 8664Combined sources
Helixi867 – 8726Combined sources
Turni873 – 8764Combined sources
Helixi877 – 8815Combined sources
Helixi886 – 89611Combined sources
Helixi899 – 91113Combined sources
Helixi913 – 9164Combined sources
Helixi922 – 93211Combined sources
Helixi935 – 94511Combined sources
Helixi949 – 9535Combined sources
Helixi958 – 96811Combined sources
Helixi971 – 98212Combined sources
Beta strandi987 – 9893Combined sources
Helixi991 – 9966Combined sources
Helixi1001 – 101111Combined sources
Helixi1014 – 102411Combined sources
Helixi1025 – 10273Combined sources
Helixi1028 – 10336Combined sources
Helixi1035 – 10373Combined sources
Helixi1040 – 10456Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q0QX-ray2.00A706-1056[»]
3Q0RX-ray2.00A706-1056[»]
3Q0SX-ray2.00A706-1056[»]
ProteinModelPortaliQ8TB72.
SMRiQ8TB72. Positions 706-1048.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TB72.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini706 – 1048343PUM-HDPROSITE-ProRule annotationAdd
BLAST
Repeati726 – 76136Pumilio 11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati762 – 79736Pumilio 21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati798 – 83538Pumilio 31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati836 – 87136Pumilio 41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati872 – 90736Pumilio 51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati908 – 94336Pumilio 61 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati944 – 97936Pumilio 71 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati983 – 102240Pumilio 81 PublicationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 260260Interaction with SNAPINAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi278 – 488211Ala-richAdd
BLAST
Compositional biasi359 – 40547Gln-richAdd
BLAST
Compositional biasi520 – 687168Ser-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 (PubMed:21397187).1 Publication

Sequence similaritiesi

Contains 1 PUM-HD domain.PROSITE-ProRule annotation
Contains 8 pumilio repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5099.
GeneTreeiENSGT00390000017241.
HOGENOMiHOG000238461.
HOVERGENiHBG049462.
InParanoidiQ8TB72.
KOiK17943.
OMAiSDERARC.
OrthoDBiEOG7T7GT5.
PhylomeDBiQ8TB72.
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.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TB72-1) [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
MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW
60 70 80 90 100
GASHHSMSQP IMVQRRSGQG FHGNSEVNAI LSPRSESGGL GVSMVEYVLS
110 120 130 140 150
SSPADKLDSR FRKGNFGTRD AETDGPEKGD QKGKASPFEE DQNRDLKQGD
160 170 180 190 200
DDDSKINGRG LPNGMDADCK DFNRTPGSRQ ASPTEVVERL GPNTNPSEGL
210 220 230 240 250
GPLPNPTANK PLVEEFSNPE TQNLDAMEQV GLESLQFDYP GNQVPMDSSG
260 270 280 290 300
ATVGLFDYNS QQQLFQRTNA LTVQQLTAAQ QQQYALAAAQ QPHIAGVFSA
310 320 330 340 350
GLAPAAFVPN PYIISAAPPG TDPYTAAGLA AAATLAGPAV VPPQYYGVPW
360 370 380 390 400
GVYPANLFQQ QAAAAANNTA SQQAASQAQP GQQQVLRAGA GQRPLTPNQG
410 420 430 440 450
QQGQQAESLA AAAAANPTLA FGQGLATGMP GYQVLAPTAY YDQTGALVVG
460 470 480 490 500
PGARTGLGAP VRLMAPTPVL ISSAAAQAAA AAAAGGTASS LTGSTNGLFR
510 520 530 540 550
PIGTQPPQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS HGPGQPGSTS
560 570 580 590 600
LGFGSGNSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS
610 620 630 640 650
SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL
660 670 680 690 700
HLGGLTNGSG RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS
710 720 730 740 750
DIMPSGRSRL LEDFRNNRFP NLQLRDLIGH IVEFSQDQHG SRFIQQKLER
760 770 780 790 800
ATPAERQMVF NEILQAAYQL MTDVFGNYVI QKFFEFGSLD QKLALATRIR
810 820 830 840 850
GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH VLKCVKDQNG
860 870 880 890 900
NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE
910 920 930 940 950
QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL
960 970 980 990 1000
ALSQHKFASN VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY
1010 1020 1030 1040 1050
ANYVVQKMID MAEPAQRKII MHKIRPHITT LRKYTYGKHI LAKLEKYYLK
1060
NSPDLGPIGG PPNGML
Length:1,066
Mass (Da):114,216
Last modified:February 2, 2004 - v2
Checksum:iCF6F9D7998CD5D9E
GO
Isoform 2 (identifier: Q8TB72-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     574-652: Missing.

Show »
Length:987
Mass (Da):106,215
Checksum:i99F119F5E3CFCCCF
GO
Isoform 3 (identifier: Q8TB72-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     829-830: Missing.

Show »
Length:1,064
Mass (Da):114,003
Checksum:i99BC2A2711306F18
GO
Isoform 4 (identifier: Q8TB72-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     829-830: Missing.

Note: No experimental confirmation available.

Show »
Length:1,008
Mass (Da):107,646
Checksum:i44DA760E31DD5F62
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti367 – 3671N → S.
Corresponds to variant rs34032508 [ dbSNP | Ensembl ].
VAR_057100

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5656Missing in isoform 4. 1 PublicationVSP_053705Add
BLAST
Alternative sequencei574 – 65279Missing in isoform 2. 1 PublicationVSP_009319Add
BLAST
Alternative sequencei829 – 8302Missing in isoform 3 and isoform 4. 4 PublicationsVSP_009320

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315591 mRNA. Translation: AAG31806.1.
D87078 mRNA. Translation: BAA19665.3.
AK093847 mRNA. Translation: BAG52772.1.
AK304198 mRNA. Translation: BAG65078.1.
AC007041 Genomic DNA. Translation: AAY15026.1.
CH471053 Genomic DNA. Translation: EAX00821.1.
CH471053 Genomic DNA. Translation: EAX00823.1.
BC024218 mRNA. Translation: AAH24218.2.
BC112046 mRNA. Translation: AAI12047.1.
BC112048 mRNA. Translation: AAI12049.1.
AF272350 mRNA. Translation: AAL36981.1.
CCDSiCCDS1698.1. [Q8TB72-3]
CCDS74487.1. [Q8TB72-4]
RefSeqiNP_001269681.1. NM_001282752.1. [Q8TB72-4]
NP_001269719.1. NM_001282790.1.
NP_001269720.1. NM_001282791.1.
NP_056132.1. NM_015317.2. [Q8TB72-3]
XP_005262664.1. XM_005262607.1. [Q8TB72-1]
XP_005262666.1. XM_005262609.1. [Q8TB72-2]
XP_006712035.1. XM_006711972.1. [Q8TB72-1]
XP_006712036.1. XM_006711973.1. [Q8TB72-1]
XP_006712037.1. XM_006711974.1. [Q8TB72-1]
UniGeneiHs.467824.

Genome annotation databases

EnsembliENST00000338086; ENSP00000338173; ENSG00000055917. [Q8TB72-3]
ENST00000361078; ENSP00000354370; ENSG00000055917. [Q8TB72-4]
ENST00000403432; ENSP00000385992; ENSG00000055917. [Q8TB72-3]
ENST00000440577; ENSP00000409905; ENSG00000055917.
GeneIDi23369.
KEGGihsa:23369.
UCSCiuc002rds.1. human. [Q8TB72-3]

Polymorphism databases

DMDMi41688714.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315591 mRNA. Translation: AAG31806.1 .
D87078 mRNA. Translation: BAA19665.3 .
AK093847 mRNA. Translation: BAG52772.1 .
AK304198 mRNA. Translation: BAG65078.1 .
AC007041 Genomic DNA. Translation: AAY15026.1 .
CH471053 Genomic DNA. Translation: EAX00821.1 .
CH471053 Genomic DNA. Translation: EAX00823.1 .
BC024218 mRNA. Translation: AAH24218.2 .
BC112046 mRNA. Translation: AAI12047.1 .
BC112048 mRNA. Translation: AAI12049.1 .
AF272350 mRNA. Translation: AAL36981.1 .
CCDSi CCDS1698.1. [Q8TB72-3 ]
CCDS74487.1. [Q8TB72-4 ]
RefSeqi NP_001269681.1. NM_001282752.1. [Q8TB72-4 ]
NP_001269719.1. NM_001282790.1.
NP_001269720.1. NM_001282791.1.
NP_056132.1. NM_015317.2. [Q8TB72-3 ]
XP_005262664.1. XM_005262607.1. [Q8TB72-1 ]
XP_005262666.1. XM_005262609.1. [Q8TB72-2 ]
XP_006712035.1. XM_006711972.1. [Q8TB72-1 ]
XP_006712036.1. XM_006711973.1. [Q8TB72-1 ]
XP_006712037.1. XM_006711974.1. [Q8TB72-1 ]
UniGenei Hs.467824.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3Q0Q X-ray 2.00 A 706-1056 [» ]
3Q0R X-ray 2.00 A 706-1056 [» ]
3Q0S X-ray 2.00 A 706-1056 [» ]
ProteinModelPortali Q8TB72.
SMRi Q8TB72. Positions 706-1048.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116949. 12 interactions.
IntActi Q8TB72. 6 interactions.
MINTi MINT-254513.
STRINGi 9606.ENSP00000338173.

PTM databases

PhosphoSitei Q8TB72.

Polymorphism databases

DMDMi 41688714.

Proteomic databases

MaxQBi Q8TB72.
PaxDbi Q8TB72.
PRIDEi Q8TB72.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338086 ; ENSP00000338173 ; ENSG00000055917 . [Q8TB72-3 ]
ENST00000361078 ; ENSP00000354370 ; ENSG00000055917 . [Q8TB72-4 ]
ENST00000403432 ; ENSP00000385992 ; ENSG00000055917 . [Q8TB72-3 ]
ENST00000440577 ; ENSP00000409905 ; ENSG00000055917 .
GeneIDi 23369.
KEGGi hsa:23369.
UCSCi uc002rds.1. human. [Q8TB72-3 ]

Organism-specific databases

CTDi 23369.
GeneCardsi GC02M020448.
HGNCi HGNC:14958. PUM2.
HPAi HPA030316.
HPA049670.
MIMi 607205. gene.
neXtProti NX_Q8TB72.
PharmGKBi PA34043.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5099.
GeneTreei ENSGT00390000017241.
HOGENOMi HOG000238461.
HOVERGENi HBG049462.
InParanoidi Q8TB72.
KOi K17943.
OMAi SDERARC.
OrthoDBi EOG7T7GT5.
PhylomeDBi Q8TB72.
TreeFami TF318160.

Miscellaneous databases

ChiTaRSi PUM2. human.
EvolutionaryTracei Q8TB72.
GeneWikii PUM2.
GenomeRNAii 23369.
NextBioi 35477241.
PROi Q8TB72.
SOURCEi Search...

Gene expression databases

Bgeei Q8TB72.
CleanExi HS_PUM2.
ExpressionAtlasi Q8TB72. baseline and differential.
Genevestigatori Q8TB72.

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 3), TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "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 3 AND 4).
    Tissue: Trachea.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 578-1066 (ISOFORM 1).
    Tissue: Lung and Placenta.
  8. "Human Pumilio-2 is expressed in embryonic stem cells and germ cells and interacts with DAZ (Deleted in AZoospermia) and DAZ-like proteins."
    Moore F.L., Jaruzelska J., Fox M.S., Urano J., Firpo M.T., Turek P.J., Dorfman D.M., Reijo Pera R.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:538-543(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-1066 (ISOFORM 2), TISSUE SPECIFICITY, RNA-BINDING, INTERACTION WITH DAZ AND DAZL.
  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. "Conservation of a Pumilio-Nanos complex from Drosophila germ plasm to human germ cells."
    Jaruzelska J., Kotecki M., Kusz K., Spik A., Firpo M., Reijo Pera R.A.
    Dev. Genes Evol. 213:120-126(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERACTION WITH NANOS1.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-178; SER-182; THR-184 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells."
    Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C., Kupryjanczyk J., Jaruzelska J.
    Mol. Hum. Reprod. 15:173-179(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SNAPIN AND NANOS1.
  16. "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 THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-136; SER-182 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within chromatoid body in human germ cells."
    Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A., Kupryjanczyk J., Jaruzelska J.
    Histochem. Cell Biol. 136:279-287(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX20.
  20. "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-136; SER-182 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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.
  22. "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 (2.0 ANGSTROMS) OF 706-1056 IN COMPLEX WITH CONSENSUS MRNA, FUNCTION, PUMILIO REPEATS.

Entry informationi

Entry nameiPUM2_HUMAN
AccessioniPrimary (citable) accession number: Q8TB72
Secondary accession number(s): B3KSL0
, B4E2B6, D6W527, O00234, Q53TV7, Q8WY43, Q9HAN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: November 26, 2014
This is version 122 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3