Q8TB72 (PUM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pumilio homolog 2
Short name=Pumilio-2

Gene names

Name:	PUM2
Synonyms:	KIAA0235, PUMH2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1066 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. 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.
Subunit structure	Homodimer; homodimerizes in vitro. Interacts with DAZ, DAZL and NANOS1 via its pumilio repeats. Binds to a RNA consensus sequence, that is related to the Nanos Response Element (NRE), a 16 bp sequence found in the 3'-UTR of the Drosophila hb mRNA. Also binds to the NRE. Interacts with NANOS3 By similarity. Interacts with SNAPIN. Ref.8 Ref.10 Ref.17
Subcellular location	Cytoplasm Probable. Cytoplasmic granule By similarity. Cytoplasm › perinuclear region. 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. Co-localizes with NANOS3 in the stress granules By similarity. Co-localizes with NANOS1 and SNAPIN in the perinuclear region of germ cells. Ref.17
Tissue specificity	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. Ref.1 Ref.8 Ref.17
Induction	Down-regulated in keratinocytes upon UVB irradiation. Ref.9
Domain	The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs By similarity.
Sequence similarities	Contains 1 PUM-HD domain. Contains 8 pumilio repeats.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic stress granule Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.17. Source: UniProtKB
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DAZ1	Q9NQZ3	5	EBI-311190,EBI-997955

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TB72-1)

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.

Isoform 2 (identifier: Q8TB72-2)

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

Isoform 3 (identifier: Q8TB72-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1066

1066

Pumilio homolog 2

PRO_0000075919

Regions

Domain

706 – 1048

343

PUM-HD

Repeat

726 – 761

36

Pumilio 1

Repeat

762 – 797

36

Pumilio 2

Repeat

798 – 835

38

Pumilio 3

Repeat

836 – 871

36

Pumilio 4

Repeat

872 – 907

36

Pumilio 5

Repeat

908 – 943

36

Pumilio 6

Repeat

944 – 979

36

Pumilio 7

Repeat

983 – 1022

40

Pumilio 8

Region

1 – 260

260

Interaction with SNAPIN

Compositional bias

278 – 488

211

Ala-rich

Compositional bias

359 – 405

47

Gln-rich

Compositional bias

520 – 687

168

Ser-rich

Amino acid modifications

Modified residue

82

1

Phosphoserine Ref.13 Ref.14 Ref.18

Modified residue

136

1

Phosphoserine Ref.12 Ref.14 Ref.16 Ref.18

Modified residue

178

1

Phosphoserine Ref.14

Modified residue

182

1

Phosphoserine Ref.11 Ref.14 Ref.15 Ref.16 Ref.18

Modified residue

184

1

Phosphothreonine Ref.14 Ref.18

Modified residue

587

1

Phosphoserine Ref.14

Modified residue

672

1

N6-acetyllysine Ref.19

Natural variations

Alternative sequence

574 – 652

79

Missing in isoform 2.

VSP_009319

Alternative sequence

829 – 830

2

Missing in isoform 3.

VSP_009320

Natural variant

367

1

N → S.
Corresponds to variant rs34032508 [ dbSNP | Ensembl ].

VAR_057100

Secondary structure

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1066

Helix Strand Turn

Details...

Helix

709 – 715

7

Helix

724 – 727

4

Helix

731 – 735

5

Helix

742 – 748

7

Helix

753 – 765

13

Helix

767 – 771

5

Helix

778 – 785

8

Helix

789 – 799

11

Helix

803 – 808

6

Helix

814 – 822

9

Helix

828 – 835

8

Helix

841 – 846

6

Helix

852 – 860

9

Helix

863 – 866

4

Helix

867 – 872

6

Helix

877 – 881

5

Helix

888 – 896

9

Helix

899 – 911

13

Helix

913 – 916

4

Helix

924 – 931

8

Helix

935 – 945

11

Helix

949 – 953

5

Helix

958 – 968

11

Helix

971 – 982

12

Helix

991 – 996

6

Helix

1001 – 1011

11

Helix

1014 – 1024

11

Helix

1025 – 1027

3

Helix

1028 – 1033

6

Helix

1040 – 1045

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 2, 2004. Version 2. Checksum: CF6F9D7998CD5D9E	FASTA	1,066	114,216
	10 20 30 40 50 60 MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GASHHSMSQP 70 80 90 100 110 120 IMVQRRSGQG FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGNFGTRD 130 140 150 160 170 180 AETDGPEKGD QKGKASPFEE DQNRDLKQGD DDDSKINGRG LPNGMDADCK DFNRTPGSRQ 190 200 210 220 230 240 ASPTEVVERL GPNTNPSEGL GPLPNPTANK PLVEEFSNPE TQNLDAMEQV GLESLQFDYP 250 260 270 280 290 300 GNQVPMDSSG ATVGLFDYNS QQQLFQRTNA LTVQQLTAAQ QQQYALAAAQ QPHIAGVFSA 310 320 330 340 350 360 GLAPAAFVPN PYIISAAPPG TDPYTAAGLA AAATLAGPAV VPPQYYGVPW GVYPANLFQQ 370 380 390 400 410 420 QAAAAANNTA SQQAASQAQP GQQQVLRAGA GQRPLTPNQG QQGQQAESLA AAAAANPTLA 430 440 450 460 470 480 FGQGLATGMP GYQVLAPTAY YDQTGALVVG PGARTGLGAP VRLMAPTPVL ISSAAAQAAA 490 500 510 520 530 540 AAAAGGTASS LTGSTNGLFR PIGTQPPQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS 550 560 570 580 590 600 HGPGQPGSTS LGFGSGNSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS 610 620 630 640 650 660 SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL HLGGLTNGSG 670 680 690 700 710 720 RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS DIMPSGRSRL LEDFRNNRFP 730 740 750 760 770 780 NLQLRDLIGH IVEFSQDQHG SRFIQQKLER ATPAERQMVF NEILQAAYQL MTDVFGNYVI 790 800 810 820 830 840 QKFFEFGSLD QKLALATRIR GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH 850 860 870 880 890 900 VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE 910 920 930 940 950 960 QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL ALSQHKFASN 970 980 990 1000 1010 1020 VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY ANYVVQKMID MAEPAQRKII 1030 1040 1050 1060 MHKIRPHITT LRKYTYGKHI LAKLEKYYLK NSPDLGPIGG PPNGML
	Isoform 2 [UniParc]. Checksum: 99F119F5E3CFCCCF	FASTA	987	106,215
	10 20 30 40 50 60 MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GASHHSMSQP 70 80 90 100 110 120 IMVQRRSGQG FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGNFGTRD 130 140 150 160 170 180 AETDGPEKGD QKGKASPFEE DQNRDLKQGD DDDSKINGRG LPNGMDADCK DFNRTPGSRQ 190 200 210 220 230 240 ASPTEVVERL GPNTNPSEGL GPLPNPTANK PLVEEFSNPE TQNLDAMEQV GLESLQFDYP 250 260 270 280 290 300 GNQVPMDSSG ATVGLFDYNS QQQLFQRTNA LTVQQLTAAQ QQQYALAAAQ QPHIAGVFSA 310 320 330 340 350 360 GLAPAAFVPN PYIISAAPPG TDPYTAAGLA AAATLAGPAV VPPQYYGVPW GVYPANLFQQ 370 380 390 400 410 420 QAAAAANNTA SQQAASQAQP GQQQVLRAGA GQRPLTPNQG QQGQQAESLA AAAAANPTLA 430 440 450 460 470 480 FGQGLATGMP GYQVLAPTAY YDQTGALVVG PGARTGLGAP VRLMAPTPVL ISSAAAQAAA 490 500 510 520 530 540 AAAAGGTASS LTGSTNGLFR PIGTQPPQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS 550 560 570 580 590 600 HGPGQPGSTS LGFGSGNSLG AAIGSALSGF GSSGGLTNGS GRYISAAPGA EAKYRSASST 610 620 630 640 650 660 SSLFSSSSQL FPPSRLRYNR SDIMPSGRSR LLEDFRNNRF PNLQLRDLIG HIVEFSQDQH 670 680 690 700 710 720 GSRFIQQKLE RATPAERQMV FNEILQAAYQ LMTDVFGNYV IQKFFEFGSL DQKLALATRI 730 740 750 760 770 780 RGHVLPLALQ MYGCRVIQKA LESISSDQQV ISEMVKELDG HVLKCVKDQN GNHVVQKCIE 790 800 810 820 830 840 CVQPQSLQFI IDAFKGQVFV LSTHPYGCRV IQRILEHCTA EQTLPILEEL HQHTEQLVQD 850 860 870 880 890 900 QYGNYVIQHV LEHGRPEDKS KIVSEIRGKV LALSQHKFAS NVVEKCVTHA SRAERALLID 910 920 930 940 950 960 EVCCQNDGPH SALYTMMKDQ YANYVVQKMI DMAEPAQRKI IMHKIRPHIT TLRKYTYGKH 970 980 ILAKLEKYYL KNSPDLGPIG GPPNGML
	Isoform 3 [UniParc]. Checksum: 99BC2A2711306F18	FASTA	1,064	114,003
	10 20 30 40 50 60 MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GASHHSMSQP 70 80 90 100 110 120 IMVQRRSGQG FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGNFGTRD 130 140 150 160 170 180 AETDGPEKGD QKGKASPFEE DQNRDLKQGD DDDSKINGRG LPNGMDADCK DFNRTPGSRQ 190 200 210 220 230 240 ASPTEVVERL GPNTNPSEGL GPLPNPTANK PLVEEFSNPE TQNLDAMEQV GLESLQFDYP 250 260 270 280 290 300 GNQVPMDSSG ATVGLFDYNS QQQLFQRTNA LTVQQLTAAQ QQQYALAAAQ QPHIAGVFSA 310 320 330 340 350 360 GLAPAAFVPN PYIISAAPPG TDPYTAAGLA AAATLAGPAV VPPQYYGVPW GVYPANLFQQ 370 380 390 400 410 420 QAAAAANNTA SQQAASQAQP GQQQVLRAGA GQRPLTPNQG QQGQQAESLA AAAAANPTLA 430 440 450 460 470 480 FGQGLATGMP GYQVLAPTAY YDQTGALVVG PGARTGLGAP VRLMAPTPVL ISSAAAQAAA 490 500 510 520 530 540 AAAAGGTASS LTGSTNGLFR PIGTQPPQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS 550 560 570 580 590 600 HGPGQPGSTS LGFGSGNSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS 610 620 630 640 650 660 SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL HLGGLTNGSG 670 680 690 700 710 720 RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS DIMPSGRSRL LEDFRNNRFP 730 740 750 760 770 780 NLQLRDLIGH IVEFSQDQHG SRFIQQKLER ATPAERQMVF NEILQAAYQL MTDVFGNYVI 790 800 810 820 830 840 QKFFEFGSLD QKLALATRIR GHVLPLALQM YGCRVIQKAL ESISSDQQSE MVKELDGHVL 850 860 870 880 890 900 KCVKDQNGNH VVQKCIECVQ PQSLQFIIDA FKGQVFVLST HPYGCRVIQR ILEHCTAEQT 910 920 930 940 950 960 LPILEELHQH TEQLVQDQYG NYVIQHVLEH GRPEDKSKIV SEIRGKVLAL SQHKFASNVV 970 980 990 1000 1010 1020 EKCVTHASRA ERALLIDEVC CQNDGPHSAL YTMMKDQYAN YVVQKMIDMA EPAQRKIIMH 1030 1040 1050 1060 KIRPHITTLR KYTYGKHILA KLEKYYLKNS PDLGPIGGPP NGML

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 12459267] [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: 9039502] [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: 12168954] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 12511597] [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: 12771951] [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: 12690449] [Abstract] Cited for: HOMODIMERIZATION, INTERACTION WITH NANOS1.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-136; SER-178; SER-182; THR-184 AND SER-587, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-182, MASS SPECTROMETRY.
[17]	"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: 19168546] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SNAPIN AND NANOS1.
[18]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-136; SER-182 AND THR-184, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-672, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF315591 mRNA. Translation: AAG31806.1.
D87078 mRNA. Translation: BAA19665.3.
AC007041 Genomic DNA. Translation: AAY15026.1.
AK093847 mRNA. Translation: BAG52772.1.
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.

IPI

IPI00022184.
IPI00398749.
IPI00398750.

RefSeq

NP_056132.1. NM_015317.1.

UniGene

Hs.467824.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q8TB72.

SMR

Q8TB72. Positions 706-1048.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8TB72. 4 interactions.

MINT

MINT-254513.

STRING

Q8TB72.

PTM databases

PhosphoSite

Q8TB72.

Polymorphism databases

DMDM

41688714.

Proteomic databases

PRIDE

Q8TB72.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361078; ENSP00000354370; ENSG00000055917.

GeneID

23369.

KEGG

hsa:23369.

UCSC

uc002rdr.1. human.
uc002rds.1. human.

Organism-specific databases

CTD

23369.

GeneCards

GC02M020448.

HGNC

HGNC:14958. PUM2.

HPA

HPA030316.

MIM

607205. gene.

neXtProt

NX_Q8TB72.

PharmGKB

PA34043.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10855.

GeneTree

ENSGT00390000017241.

HOGENOM

HBG445218.

HOVERGEN

HBG049462.

InParanoid

Q8TB72.

OMA

HITSIPR.

PhylomeDB

Q8TB72.

Gene expression databases

ArrayExpress

Q8TB72.

Bgee

Q8TB72.

CleanEx

HS_PUM2.

Genevestigator

Q8TB72.

GermOnline

ENSG00000055917. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

Pfam

PF00806. PUF. 8 hits.
[Graphical view]

SMART

SM00025. Pumilio. 8 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

45440.

SOURCE

Search...

Entry information

Entry name

PUM2_HUMAN

Accession

Primary (citable) accession number: Q8TB72
Secondary accession number(s): B3KSL0 , D6W527, O00234, Q53TV7, Q8WY43, Q9HAN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 2, 2004
Last sequence update:	February 2, 2004
Last modified:	January 25, 2012
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.