Q9H2X6 (HIPK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Homeodomain-interacting protein kinase 2
Short name=hHIPk2
EC=2.7.11.1

Gene names

Name:

HIPK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1198 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.20 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 Ref.37
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with CREB1, SIAH1, WSB1, CBX4, TRADD, p53/TP53, TP73, TP63, CREBBP, DAXX, P53DINP1, SKI, SMAD1, SMAD2 and SMAD3, but not SMAD4. Interacts with ATF1, PML, RUNX1, EP300, NKX1-2, NKX2-5, SPN/CD43, UBE2I, HMGA1, CTBP1, AXIN1, NLK, MYB, POU4F1, POU4F2, POU4F3, UBE2I, UBL1 and ZBTB4. Probably part of a complex consisting of p53/TP53, HIPK2 and AXIN1. Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.16 Ref.19 Ref.21 Ref.24 Ref.25 Ref.29 Ref.30 Ref.31
Subcellular location	Nucleus › PML body. Cytoplasm. Note: Concentrated in PML/POD/ND10 nuclear bodies. Small amounts are cytoplasmic. Ref.1 Ref.7 Ref.9 Ref.10 Ref.12 Ref.31 Ref.32
Tissue specificity	Highly expressed in heart, muscle and kidney. Weakly expressed in a ubiquitous way. Down-regulated in several thyroid and breast tumors. Ref.1 Ref.6
Induction	Unstable in unstressed cells but stabilized upon DNA damage. Induced by UV irradiation and other genotoxic agents (adriamycin ADR, cisplatin CDDP, etoposide, IR, roscovitin), thus triggering p53/TP53 apoptotic response. Consistutively negatively regulated by SIAH1 and WSB1 through proteasomal degradation. This negative regulation is impaired upon genotoxic stress. Repressed upon hypoxia (often associated with tumors), through MDM2- (an E3 ubiquitin ligases) mediated proteasomal degradation, thus inactivating p53/TP53 apoptotic response. This hypoxia repression is reversed by zinc. The stabilization mediated by DNA damage requires the damage checkpoint kinases ATM and ATR. Ref.9 Ref.21 Ref.26 Ref.33 Ref.36
Post-translational modification	Phosphorylated on tyrosines By similarity. Autophosphorylated. Ref.9 Sumoylated. When conjugated it is directed to nuclear speckles. Desumoylated by SENP1 By similarity. Sumoylation on Lys-32 is promoted by the E3 SUMO-protein ligase CBX4. Ref.14 Ref.16 Ref.31 Ref.32 Ubiquitinated by FBXO3, WSB1 and SIAH1, leading to rapid proteasome-dependent degradation. The degradation mediated by FBXO3, but not ubiquitination, is prevented in the presence of PML. The degradation mediated by WSB1 and SIAH1 is reversibly reduced upon DNA damage. Ref.19 Ref.20 Ref.21 Cleaved at Asp-923 and Asp-984 by CASP6 in a p53/TP53-dependent manner. The cleaved form lacks the autoinhibitory C-terminal domain (AID), resulting in a hyperactive kinase, which potentiates p53/TP53 Ser-46 phosphorylation and subsequent activation of the cell death machinery. Ref.15
Miscellaneous	Interesting targets for cancer therapy. HIPK2 deregulation would end up in a multifactorial response leading to tumor chemoresistance by affecting p53/TP53 activity on one hand and to angiogenesis and cell proliferation by affecting HIF1A activity on the other hand. May provide important insights in the process of tumor progression, and may also serve as the crucial point in the diagnostic and therapeutical aspects of cancer. Tumor treatment may potential be improved by zinc supplementation in combination with chemotherapy to address hypoxia (Ref.36).
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. HIPK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis DNA damage Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from direct assay PubMed 14647468. Source: BHF-UCL PML body organization Traceable author statement Ref.33. Source: UniProtKB SMAD protein signal transduction Inferred from direct assay Ref.13. Source: UniProtKB adult walking behavior Inferred from electronic annotation. Source: Compara anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara cellular response to hypoxia Traceable author statement Ref.33. Source: UniProtKB embryonic camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara embryonic retina morphogenesis in camera-type eye Inferred from electronic annotation. Source: Compara erythrocyte differentiation Inferred from sequence or structural similarity PubMed 20231426. Source: UniProtKB eye development Inferred from sequence or structural similarity PubMed 20579985. Source: UniProtKB intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Traceable author statement Ref.33. Source: UniProtKB iris morphogenesis Inferred from electronic annotation. Source: Compara lens induction in camera-type eye Inferred from electronic annotation. Source: Compara negative regulation of BMP signaling pathway Inferred from mutant phenotype Ref.13. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara neuron differentiation Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from sequence or structural similarity. Source: BHF-UCL peptidyl-threonine phosphorylation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of DNA binding Inferred from electronic annotation. Source: Compara positive regulation of JNK cascade Inferred from mutant phenotype Ref.11. Source: UniProtKB positive regulation of angiogenesis Inferred from direct assay Ref.22. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of protein binding Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype Ref.11. Source: UniProtKB regulation of cell cycle Traceable author statement Ref.33. Source: UniProtKB retina layer formation Inferred from electronic annotation. Source: Compara smoothened signaling pathway Inferred from electronic annotation. Source: Compara transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara virus-host interaction Non-traceable author statement PubMed 14990717. Source: UniProtKB voluntary musculoskeletal movement Inferred from electronic annotation. Source: Compara
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell centrosome Inferred from direct assay. Source: HPA cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nuclear body Inferred from direct assay Ref.13. Source: UniProtKB nuclear membrane Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II activating transcription factor binding Inferred from sequence or structural similarity. Source: BHF-UCL RNA polymerase II transcription coactivator activity Inferred from electronic annotation. Source: Compara protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: BHF-UCL transcription corepressor activity Inferred from direct assay Ref.13. Source: UniProtKB virion binding Inferred from physical interaction PubMed 14990717. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9H2X6-1)

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: Q9H2X6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     808-907: Missing.
     989-1018: VNTSHHSSSYKSKSSSNVTSTSGHSSGSSS → GNLGPGQGRNLSLESGFPAFLLLEMLLYGS
     1019-1198: Missing.

Isoform 3 (identifier: Q9H2X6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     595-621: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1198	1198	Homeodomain-interacting protein kinase 2		PRO_0000085995
Regions
	Domain	199 – 527	329	Protein kinase
	Nucleotide binding	205 – 213	9	ATP Probable
	Region	97 – 230	134	Transcriptional corepression By similarity
	Region	189 – 520	332	Interaction with DAXX
	Region	539 – 844	306	Interaction with SKI and SMAD1
	Region	752 – 897	146	Interaction with POU4F1 By similarity
	Region	774 – 876	103	Interaction with CTBP1 By similarity
	Region	787 – 897	111	Interaction with HMGA1 By similarity
	Region	802 – 805	4	Nuclear localization signal 1 (NLS1)
	Region	832 – 835	4	Nuclear localization signal 2 (NLS2)
	Region	846 – 941	96	Interaction with TP53 and TP73
	Region	873 – 980	108	Required for localization to nuclear speckles By similarity
	Region	873 – 907	35	Interaction with UBE2I By similarity
	Region	884 – 908	25	SUMO interaction motifs (SIM); required for nuclear localization and kinase activity
	Region	935 – 1049	115	Interaction with AXIN1 By similarity
	Region	984 – 1198	215	Autoinhibitory domain (AID)
	Compositional bias	1088 – 1094	7	Poly-Ala
Sites
	Active site	324	1	Proton acceptor Probable
	Binding site	228	1	ATP Probable
	Site	923 – 924	2	Cleavage; by CASP6
	Site	984 – 985	2	Cleavage; by CASP6
Amino acid modifications
	Modified residue	361	1	Phosphotyrosine By similarity
	Cross-link	32		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16
	Cross-link	1191		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	595 – 621	27	Missing in isoform 3.		VSP_004804
	Alternative sequence	808 – 907	100	Missing in isoform 2.		VSP_004805
	Alternative sequence	989 – 1018	30	VNTSH…SGSSS → GNLGPGQGRNLSLESGFPAF LLLEMLLYGS in isoform 2.		VSP_004806
	Alternative sequence	1019 – 1198	180	Missing in isoform 2.		VSP_004807
	Natural variant	792	1	R → Q. Ref.38		VAR_040547
	Natural variant	1027	1	R → Q. Ref.38		VAR_040548
Experimental info
	Mutagenesis	228	1	K → A: Locates in the nucleoplasm, no effect on interaction with RANBP9, but loss of kinase activity toward PML, RUNX1 and EP300. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.18 Ref.24
	Mutagenesis	228	1	K → R: Abolishes enzymatic activity, no effect on interaction with TP53 and TP73 or on BMP-induced transcriptional activation. Enhances BMP-induced transcriptional activation; when associated with 359-AAF-361. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.18 Ref.24
	Mutagenesis	359 – 361	3	STY → AAF: Enhances BMP-induced transcriptional activation; when associated with R-228. Ref.13
	Mutagenesis	803	1	K → A: Impaired nuclear localization; when associated with A-805. Ref.31
	Mutagenesis	805	1	K → A: Impaired nuclear localization; when associated with A-803. Ref.31
	Mutagenesis	833	1	R → A: Impaired nuclear localization. Ref.31
	Mutagenesis	835	1	K → E: Impaired nuclear localization. Ref.31
	Mutagenesis	885 – 892	8	VSVITISS → KFMHFHRM: Loss of SUMO and CBX4 interaction, and impaired nuclear and PML-nuclear bodies localization. Ref.31
	Mutagenesis	885 – 888	4	VSVI → KSAK: Loss of SUMO interaction, and impaired nuclear and PML-nuclear bodies localization. Ref.32
	Mutagenesis	892 – 895	4	SDTD → ADTA: Loss of SUMO interaction, and impaired nuclear and PML-nuclear bodies localization. Ref.32
	Mutagenesis	893 – 899	7	DTDEEEE → NFNQQQQ: Loss of SUMO and CBX4 interaction, and impaired nuclear and PML-nuclear bodies localization. Ref.31
	Sequence conflict	33	1	I → V in AAG41236. Ref.1
	Sequence conflict	59	1	L → P in AAG41236. Ref.1
	Sequence conflict	64	1	T → S in AAG41236. Ref.1
	Sequence conflict	169	1	S → F in AAG35710. Ref.4
	Sequence conflict	187	1	V → S in AAG35710. Ref.4
	Sequence conflict	202	1	L → S in AAG35710. Ref.4
	Sequence conflict	233	1	H → R in AAG41236. Ref.1
	Sequence conflict	471	1	N → I in AAL37371. Ref.2
	Sequence conflict	669	1	P → S in AAG35710. Ref.4
	Sequence conflict	711	1	T → N in AAG35710. Ref.4
	Sequence conflict	717 – 719	3	PPA → SPT in AAG35710. Ref.4
	Sequence conflict	724	1	T → D in AAG35710. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 6022D5710E8D2D93	FASTA	1,198	130,966
	10 20 30 40 50 60 MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKIEPSSNWD MTGYGSHSKV YSQSKNIPLS 70 80 90 100 110 120 QPATTTVSTS LPVPNPSLPY EQTIVFPGST GHIVVTSASS TSVTGQVLGG PHNLMRRSTV 130 140 150 160 170 180 SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH PPMIQNNASG ATVATATTST ATSKNSGSNS 190 200 210 220 230 240 EGDYQLVQHE VLCSMTNTYE VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG 250 260 270 280 290 300 QIEVSILARL STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY 310 320 330 340 350 360 IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA SHVSKAVCST 370 380 390 400 410 420 YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL YPGASEYDQI RYISQTQGLP 430 440 450 460 470 480 AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT PDDHEAETGI KSKEARKYIF NCLDDMAQVN 490 500 510 520 530 540 MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRITPIE TLNHPFVTMT HLLDFPHSTH 550 560 570 580 590 600 VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQAPSSTS 610 620 630 640 650 660 ATISLANPEV SILNYPSTLY QPSAASMAAV AQRSMPLQTG TAQICARPDP FQQALIVCPP 670 680 690 700 710 720 GFQGLQASPS KHAGYSVRME NAVPIVTQAP GAQPLQIQPG LLAQQAWPSG TQQILLPPAW 730 740 750 760 770 780 QQLTGVATHT SVQHATVIPE TMAGTQQLAD WRNTHAHGSH YNPIMQQPAL LTGHVTLPAA 790 800 810 820 830 840 QPLNVGVAHV MRQQPTSTTS SRKSKQHQSS VRNVSTCEVS SSQAISSPQR SKRVKENTPP 850 860 870 880 890 900 RCAMVHSSPA CSTSVTCGWG DVASSTTRER QRQTIVIPDT PSPTVSVITI SSDTDEEEEQ 910 920 930 940 950 960 KHAPTSTVSK QRKNVISCVT VHDSPYSDSS SNTSPYSVQQ RAGHNNANAF DTKGSLENHC 970 980 990 1000 1010 1020 TGNPRTIIVP PLKTQASEVL VECDSLVPVN TSHHSSSYKS KSSSNVTSTS GHSSGSSSGA 1030 1040 1050 1060 1070 1080 ITYRQQRPGP HFQQQQPLNL SQAQQHITTD RTGSHRRQQA YITPTMAQAP YSFPHNSPSH 1090 1100 1110 1120 1130 1140 GTVHPHLAAA AAAAHLPTQP HLYTYTAPAA LGSTGTVAHL VASQGSARHT VQHTAYPASI 1150 1160 1170 1180 1190 VHQVPVSMGP RVLPSPTIHP SQYPAQFAHQ TYISASPAST VYTGYPLSPA KVNQYPYI
	Isoform 2 [UniParc]. Checksum: BA34005E15CFC5CD	FASTA	918	101,013
	10 20 30 40 50 60 MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKIEPSSNWD MTGYGSHSKV YSQSKNIPLS 70 80 90 100 110 120 QPATTTVSTS LPVPNPSLPY EQTIVFPGST GHIVVTSASS TSVTGQVLGG PHNLMRRSTV 130 140 150 160 170 180 SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH PPMIQNNASG ATVATATTST ATSKNSGSNS 190 200 210 220 230 240 EGDYQLVQHE VLCSMTNTYE VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG 250 260 270 280 290 300 QIEVSILARL STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY 310 320 330 340 350 360 IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA SHVSKAVCST 370 380 390 400 410 420 YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL YPGASEYDQI RYISQTQGLP 430 440 450 460 470 480 AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT PDDHEAETGI KSKEARKYIF NCLDDMAQVN 490 500 510 520 530 540 MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRITPIE TLNHPFVTMT HLLDFPHSTH 550 560 570 580 590 600 VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQAPSSTS 610 620 630 640 650 660 ATISLANPEV SILNYPSTLY QPSAASMAAV AQRSMPLQTG TAQICARPDP FQQALIVCPP 670 680 690 700 710 720 GFQGLQASPS KHAGYSVRME NAVPIVTQAP GAQPLQIQPG LLAQQAWPSG TQQILLPPAW 730 740 750 760 770 780 QQLTGVATHT SVQHATVIPE TMAGTQQLAD WRNTHAHGSH YNPIMQQPAL LTGHVTLPAA 790 800 810 820 830 840 QPLNVGVAHV MRQQPTSTTS SRKSKQHVSK QRKNVISCVT VHDSPYSDSS SNTSPYSVQQ 850 860 870 880 890 900 RAGHNNANAF DTKGSLENHC TGNPRTIIVP PLKTQASEVL VECDSLVPGN LGPGQGRNLS 910 LESGFPAFLL LEMLLYGS
	Isoform 3 [UniParc]. Checksum: C38A3241948C7D66	FASTA	1,171	128,158
	10 20 30 40 50 60 MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKIEPSSNWD MTGYGSHSKV YSQSKNIPLS 70 80 90 100 110 120 QPATTTVSTS LPVPNPSLPY EQTIVFPGST GHIVVTSASS TSVTGQVLGG PHNLMRRSTV 130 140 150 160 170 180 SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH PPMIQNNASG ATVATATTST ATSKNSGSNS 190 200 210 220 230 240 EGDYQLVQHE VLCSMTNTYE VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG 250 260 270 280 290 300 QIEVSILARL STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY 310 320 330 340 350 360 IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA SHVSKAVCST 370 380 390 400 410 420 YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL YPGASEYDQI RYISQTQGLP 430 440 450 460 470 480 AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT PDDHEAETGI KSKEARKYIF NCLDDMAQVN 490 500 510 520 530 540 MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRITPIE TLNHPFVTMT HLLDFPHSTH 550 560 570 580 590 600 VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQPSAASM 610 620 630 640 650 660 AAVAQRSMPL QTGTAQICAR PDPFQQALIV CPPGFQGLQA SPSKHAGYSV RMENAVPIVT 670 680 690 700 710 720 QAPGAQPLQI QPGLLAQQAW PSGTQQILLP PAWQQLTGVA THTSVQHATV IPETMAGTQQ 730 740 750 760 770 780 LADWRNTHAH GSHYNPIMQQ PALLTGHVTL PAAQPLNVGV AHVMRQQPTS TTSSRKSKQH 790 800 810 820 830 840 QSSVRNVSTC EVSSSQAISS PQRSKRVKEN TPPRCAMVHS SPACSTSVTC GWGDVASSTT 850 860 870 880 890 900 RERQRQTIVI PDTPSPTVSV ITISSDTDEE EEQKHAPTST VSKQRKNVIS CVTVHDSPYS 910 920 930 940 950 960 DSSSNTSPYS VQQRAGHNNA NAFDTKGSLE NHCTGNPRTI IVPPLKTQAS EVLVECDSLV 970 980 990 1000 1010 1020 PVNTSHHSSS YKSKSSSNVT STSGHSSGSS SGAITYRQQR PGPHFQQQQP LNLSQAQQHI 1030 1040 1050 1060 1070 1080 TTDRTGSHRR QQAYITPTMA QAPYSFPHNS PSHGTVHPHL AAAAAAAHLP TQPHLYTYTA 1090 1100 1110 1120 1130 1140 PAALGSTGTV AHLVASQGSA RHTVQHTAYP ASIVHQVPVS MGPRVLPSPT IHPSQYPAQF 1150 1160 1170 AHQTYISASP ASTVYTGYPL SPAKVNQYPY I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of cDNAs for the protein kinase HIPK2." Wang Y., Hofmann T.G., Runkel L., Haaf T., Schaller H., Debatin K.-M., Hug H. Biochim. Biophys. Acta 1518:168-172(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-228. Tissue: Liver and Testis.
[2]	"Sequencing of hHIPk2, a human homolog of mouse homeodomain interacting protein kinase 2." Stukart G.C., Dias-Neto E. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Frontal cortex.
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Pierantoni G.M., Benvenuto G., Chiariotti L., Fusco A. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1198 (ISOFORM 2).
[5]	"The serine/threonine kinase HIPK2 interacts with TRADD, but not with CD95 or TNF-R1 in 293T cells." Li X., Wang Y., Debatin K.-M., Hug H. Biochem. Biophys. Res. Commun. 277:513-517(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRADD.
[6]	"The homeodomain-interacting protein kinase 2 gene is expressed late in embryogenesis and preferentially in retina, muscle, and neural tissues." Pierantoni G.M., Bulfone A., Pentimalli F., Fedele M., Iuliano R., Santoro M., Chiariotti L., Ballabio A., Fusco A. Biochem. Biophys. Res. Commun. 290:942-947(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"HIPK2 associates with RanBPM." Wang Y., Marion Schneider E., Li X., Duttenhoefer I., Debatin K.-M., Hug H. Biochem. Biophys. Res. Commun. 297:148-153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RANBP9, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-228.
[8]	"Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo." Kim E.-J., Park J.-S., Um S.-J. J. Biol. Chem. 277:32020-32028(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TP73; TP53 AND TP63, MUTAGENESIS OF LYS-228, FUNCTION.
[9]	"Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2." Hofmann T.G., Moeller A., Sirma H., Zentgraf H., Taya Y., Droege W., Will H., Schmitz M.L. Nat. Cell Biol. 4:1-10(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH TP53 AND CREBBP, MUTAGENESIS OF LYS-228, FUNCTION, INDUCTION.
[10]	"PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains." Moeller A., Sirma H., Hofmann T.G., Rueffer S., Klimczak E., Droege W., Will H., Schmitz M.L. Cancer Res. 63:4310-4314(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-228.
[11]	"HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells." Hofmann T.G., Stollberg N., Schmitz M.L., Will H. Cancer Res. 63:8271-8277(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DAXX, MUTAGENESIS OF LYS-228.
[12]	"TP53INP1s and homeodomain-interacting protein kinase-2 (HIPK2) are partners in regulating p53 activity." Tomasini R., Samir A.A., Carrier A., Isnardon D., Cecchinelli B., Soddu S., Malissen B., Dagorn J.-C., Iovanna J.L., Dusetti N.J. J. Biol. Chem. 278:37722-37729(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH P53DINP1.
[13]	"Requirement of the co-repressor homeodomain-interacting protein kinase 2 for ski-mediated inhibition of bone morphogenetic protein-induced transcriptional activation." Harada J., Kokura K., Kanei-Ishii C., Nomura T., Khan M.M., Kim Y., Ishii S. J. Biol. Chem. 278:38998-39005(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SKI; SMAD1; SMAD2 AND SMAD3, MUTAGENESIS OF LYS-228 AND 359-SER--TYR-361.
[14]	"Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1." Kim Y.H., Sung K.S., Lee S.-J., Kim Y.-O., Choi C.Y., Kim Y. FEBS Lett. 579:6272-6278(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DESUMOYLATION.
[15]	"Autoregulatory control of the p53 response by caspase-mediated processing of HIPK2." Gresko E., Roscic A., Ritterhoff S., Vichalkovski A., del Sal G., Schmitz M.L. EMBO J. 25:1883-1894(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY CASP6 AT ASP-923 AND ASP-984.
[16]	"Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2." Roscic A., Moeller A., Calzado M.A., Renner F., Wimmer V.C., Gresko E., Luedi K.S., Schmitz M.L. Mol. Cell 24:77-89(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBX4, SUMOYLATION AT LYS-32, FUNCTION.
[17]	"Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA binding affinity." Zhang Q., Wang Y. J. Proteome Res. 6:4711-4719(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS HMGA1 KINASE.
[18]	"PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2: implications for leukemogenesis." Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y. Blood 112:3777-3787(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS RUNX1 AND EP300 KINASE, MUTAGENESIS OF LYS-228.
[19]	"Ubiquitination and degradation of homeodomain-interacting protein kinase 2 by WD40 repeat/SOCS box protein WSB-1." Choi D.W., Seo Y.-M., Kim E.-A., Sung K.S., Ahn J.W., Park S.-J., Lee S.-R., Choi C.Y. J. Biol. Chem. 283:4682-4689(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WSB1, UBIQUITINATION BY WSB1.
[20]	"PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation." Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I. Mol. Cell. Biol. 28:7126-7138(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, UBIQUITINATION BY FBXO3.
[21]	"Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR." Winter M., Sombroek D., Dauth I., Moehlenbrink J., Scheuermann K., Crone J., Hofmann T.G. Nat. Cell Biol. 10:812-824(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY DNA DAMAGE, INTERACTION WITH SIAH1, UBIQUITINATION BY SIAH1.
[22]	"Transcriptional regulation of hypoxia-inducible factor 1alpha by HIPK2 suggests a novel mechanism to restrain tumor growth." Nardinocchi L., Puca R., Guidolin D., Belloni A.S., Bossi G., Michiels C., Sacchi A., Onisto M., D'Orazi G. Biochim. Biophys. Acta 1793:368-377(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS HIF1A TRANSCRIPTION REGULATOR AND ANGIOGENESIS PROMOTER.
[23]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"PML tumor suppressor is regulated by HIPK2-mediated phosphorylation in response to DNA damage." Gresko E., Ritterhoff S., Sevilla-Perez J., Roscic A., Froebius K., Kotevic I., Vichalkovski A., Hess D., Hemmings B.A., Schmitz M.L. Oncogene 28:698-708(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PML KINASE, INTERACTION WITH PML, MUTAGENESIS OF LYS-228.
[25]	"The human protein kinase HIPK2 phosphorylates and downregulates the methyl-binding transcription factor ZBTB4." Yamada D., Perez-Torrado R., Filion G., Caly M., Jammart B., Devignot V., Sasai N., Ravassard P., Mallet J., Sastre-Garau X., Schmitz M.L., Defossez P.A. Oncogene 28:2535-2544(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS ZBTB4 KINASE, INTERACTION WITH ZBTB4.
[26]	"Targeting hypoxia in cancer cells by restoring homeodomain interacting protein-kinase 2 and p53 activity and suppressing HIF-1alpha." Nardinocchi L., Puca R., Sacchi A., Rechavi G., Givol D., D'Orazi G. PLoS ONE 4:E6819-E6819(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY ZINC DURING HYPOXIA.
[27]	"Pancreatic and duodenal homeobox 1 (PDX1) phosphorylation at serine-269 is HIPK2-dependent and affects PDX1 subnuclear localization." An R., da Silva Xavier G., Semplici F., Vakhshouri S., Hao H.X., Rutter J., Pagano M.A., Meggio F., Pinna L.A., Rutter G.A. Biochem. Biophys. Res. Commun. 399:155-161(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PDX1 KINASE.
[28]	"Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin for phosphorylation and proteasomal degradation." Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y. Biochem. Biophys. Res. Commun. 394:966-971(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS CTNNB1 KINASE.
[29]	"Transcriptional regulation of ferritin and antioxidant genes by HIPK2 under genotoxic stress." Hailemariam K., Iwasaki K., Huang B.W., Sakamoto K., Tsuji Y. J. Cell Sci. 123:3863-3871(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS ATF1 KINASE, INTERACTION WITH ATF1.
[30]	"Regulation of genotoxic stress response by homeodomain-interacting protein kinase 2 through phosphorylation of cyclic AMP response element-binding protein at serine 271." Sakamoto K., Huang B.-W., Iwasaki K., Hailemariam K., Ninomiya-Tsuji J., Tsuji Y. Mol. Biol. Cell 21:2966-2974(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS CREB1 KINASE, INTERACTION WITH CREB1.
[31]	"Control of nuclear HIPK2 localization and function by a SUMO interaction motif." de la Vega L., Froebius K., Moreno R., Calzado M.A., Geng H., Schmitz M.L. Biochim. Biophys. Acta 1813:283-297(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SUMOYLATION, NUCLEAR LOCALIZATION SIGNALS, MUTAGENESIS OF LYS-803; LYS-805; ARG-833; LYS-835; 885-VAL--SER-892 AND 893-ASP--GLU-899, INTERACTION WITH CBX4.
[32]	"Role of the SUMO-interacting motif in HIPK2 targeting to the PML nuclear bodies and regulation of p53." Sung K.S., Lee Y.A., Kim E.T., Lee S.R., Ahn J.H., Choi C.Y. Exp. Cell Res. 317:1060-1070(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SUMOYLATION, FUNCTION, MUTAGENESIS OF 885-VAL--ILE-888 AND 892-SER--ASP-895.
[33]	"How cells switch HIPK2 on and off." Sombroek D., Hofmann T.G. Cell Death Differ. 16:187-194(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON DNA DAMAGE SIGNALING, INDUCTION BY GENOTOXIC AGENTS, STABILIZATION BY DNA DAMAGE.
[34]	"Apoptosis and autophagy: Regulation of apoptosis by DNA damage signalling - roles of p53, p73 and HIPK2." Bitomsky N., Hofmann T.G. FEBS J. 276:6074-6083(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[35]	"HIPK2-a therapeutical target to be (re)activated for tumor suppression: role in p53 activation and HIF-1? inhibition." Nardinocchi L., Puca R., Givol D., D'Orazi G. Cell Cycle 9:1270-1275(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW AS HYPOXIA AND TP53 REGULATOR.
[36]	"Regulation of p53 activity by HIPK2: molecular mechanisms and therapeutical implications in human cancer cells." Puca R., Nardinocchi L., Givol D., D'Orazi G. Oncogene 29:4378-4387(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW AS TP53 REGULATOR, INDUCTION BY GENOTOXIC AGENTS AND HYPOXIA.
[37]	"DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation." Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A. J. Biol. Chem. 287:30789-30799(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[38]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-792 AND GLN-1027.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF208291 mRNA. Translation: AAG41236.1. AF326592 mRNA. Translation: AAL37371.1. AC005531 Genomic DNA. Translation: AAS00368.1. AC073184 Genomic DNA. No translation available. AC006021 Genomic DNA. No translation available. AC141932 Genomic DNA. No translation available. AF207702 mRNA. Translation: AAG35710.1.
IPI	IPI00215949. IPI00215950. IPI00289892.
RefSeq	NP_001106710.1. NM_001113239.2. NP_073577.3. NM_022740.4.
UniGene	Hs.731417.
3D structure databases
ProteinModelPortal	Q9H2X6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H2X6. 9 interactions.
MINT	MINT-234689.
STRING	9606.ENSP00000263551.
PTM databases
PhosphoSite	Q9H2X6.
Polymorphism databases
DMDM	21431782.
Proteomic databases
PaxDb	Q9H2X6.
PRIDE	Q9H2X6.
Protocols and materials databases
DNASU	28996.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000406875; ENSP00000385571; ENSG00000064393. ENST00000428878; ENSP00000413724; ENSG00000064393.
GeneID	28996.
KEGG	hsa:28996.
UCSC	uc003vvd.4. human. uc003vvf.4. human.
Organism-specific databases
CTD	28996.
GeneCards	GC07M139246.
HGNC	HGNC:14402. HIPK2.
HPA	HPA007611.
MIM	606868. gene.
neXtProt	NX_Q9H2X6.
PharmGKB	PA29291.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000231785.
HOVERGEN	HBG051908.
InParanoid	Q9H2X6.
KO	K08826.
OMA	MIQNNAS.
OrthoDB	EOG4CVG63.
PhylomeDB	Q9H2X6.
Enzyme and pathway databases
BRENDA	2.7.11.1. 2681.
Gene expression databases
ArrayExpress	Q9H2X6.
Bgee	Q9H2X6.
CleanEx	HS_HIPK2.
Genevestigator	Q9H2X6.
GermOnline	ENSG00000064393. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9H2X6.
ChEMBL	CHEMBL4576.
ChiTaRS	HIPK2. human.
GenomeRNAi	28996.
NextBio	51926.
PMAP-CutDB	Q9H2X6.
SOURCE	Search...

Entry information

Entry name

HIPK2_HUMAN

Accession

Primary (citable) accession number: Q9H2X6
Secondary accession number(s): Q75MR7, Q8WWI4, Q9H2Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	June 6, 2002
Last modified:	May 1, 2013
This is version 133 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.