Q86Z02 (HIPK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Homeodomain-interacting protein kinase 1
EC=2.7.11.1

Alternative name(s):
Nuclear body-associated kinase 2

Gene names

Name:	HIPK1
Synonyms:	KIAA0630, MYAK, NBAK2

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	1210 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation. Ref.7 Ref.9 Ref.10 Ref.11 Ref.13
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with Nkx1-2, Nkx2-5, MYB, PARK7, DAXX and p53/TP53. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF. This complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Subcellular location	Nucleus. Cytoplasm. Note: Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation. Ref.10 Ref.11 Ref.12 Ref.13
Tissue specificity	Ubiquitously expressed with highest levels in skeletal muscle and heart. Overexpressed in breast cancer cell lines. Isoform 2 is highly expressed in testis. Ref.8 Ref.9
Post-translational modification	Autophosphorylated. Phosphorylated and activated by JNK1. Ref.7 Degraded by PARK7 at the protein level. Sumoylated. When conjugated it is directed to nuclear speckles. SENP1-mediated desumoylation is mediated by TNF in response to stress stimuli, triggering transient translocation from nucleus to cytoplasm. Ref.10 Ref.12
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	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	anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara apoptotic process Inferred from direct assay Ref.10. Source: UniProtKB definitive hemopoiesis Inferred from sequence or structural similarity PubMed 20231426. 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 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 Inferred from electronic annotation. Source: Compara iris morphogenesis Inferred from electronic annotation. Source: Compara lens induction in camera-type eye Inferred from electronic annotation. Source: Compara neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of angiogenesis Inferred from sequence or structural similarity PubMed 16917507. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW regulation of tumor necrosis factor-mediated signaling pathway Inferred from direct assay Ref.10. Source: UniProtKB retina layer formation Inferred from electronic annotation. Source: Compara smoothened signaling pathway Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TP53	P04637	2	EBI-692891,EBI-366083

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86Z02-1)

Also known as: HIPK1-alpha;

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: Q86Z02-2)

Also known as: HIPK1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1049-1075: NQQSSAAPTSQERSSNPAPRRQQAFVA → VSAMGYCLLFGPCTVVTFWRTLLLAGC
     1076-1210: Missing.

Isoform 3 (identifier: Q86Z02-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-374: Missing.

Isoform 4 (identifier: Q86Z02-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-394: Missing.
     395-399: ASEYD → MVLMF

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1210	1210	Homeodomain-interacting protein kinase 1		PRO_0000085993
Regions
	Domain	190 – 518	329	Protein kinase
	Nucleotide binding	196 – 204	9	ATP Probable
	Region	844 – 847	4	Nuclear localization signal 1 (NLS1) By similarity
	Region	885 – 1093	209	Interaction with TP53
	Region	891 – 998	108	Required for localization to nuclear speckles By similarity
	Region	902 – 926	25	SUMO interaction motifs (SIM); required for nuclear localization and kinase activity By similarity
Sites
	Active site	315	1	Proton acceptor Probable
	Binding site	219	1	ATP Probable
Amino acid modifications
	Modified residue	352	1	Phosphotyrosine By similarity
	Modified residue	872	1	Phosphoserine Ref.14
	Cross-link	25		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.10
	Cross-link	1203		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Natural variations
	Alternative sequence	1 – 394	394	Missing in isoform 4.		VSP_013127
	Alternative sequence	1 – 374	374	Missing in isoform 3.		VSP_013128
	Alternative sequence	395 – 399	5	ASEYD → MVLMF in isoform 4.		VSP_013129
	Alternative sequence	1049 – 1075	27	NQQSS…QAFVA → VSAMGYCLLFGPCTVVTFWR TLLLAGC in isoform 2.		VSP_013130
	Alternative sequence	1076 – 1210	135	Missing in isoform 2.		VSP_013131
	Natural variant	6	1	Q → R. Corresponds to variant rs35324789 [ dbSNP | Ensembl ].		VAR_051626
	Natural variant	310	1	G → C. Ref.15		VAR_040546
	Natural variant	1165	1	L → V. Ref.15		VAR_046047
Experimental info
	Mutagenesis	25	1	K → R: Reduced sumoylation and cytoplasmic subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-317; R-440; R-556 and R-1203. Ref.10
	Mutagenesis	219	1	K → A: Loss of kinase activity. Ref.13
	Mutagenesis	315	1	D → N: Loss of kinase activity and impaired MAP3K5-JNK inactivation. Ref.10
	Mutagenesis	317	1	K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-440; R-556 and R-1203. Ref.10
	Mutagenesis	440	1	K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-556 and R-1203. Ref.10
	Mutagenesis	556	1	K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-1203. Ref.10
	Mutagenesis	1203	1	K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-556. Ref.10
	Sequence conflict	721	1	P → Q in AAH33012. Ref.4
	Sequence conflict	747	1	Missing in BAA31605. Ref.6
	Sequence conflict	799	1	H → Y in CAD38689. Ref.5
	Sequence conflict	1054	1	A → V in AAH36057. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (HIPK1-alpha) [UniParc]. Last modified June 1, 2003. Version 1. Checksum: DB0BBFA6DF152909	FASTA	1,210	130,843
	10 20 30 40 50 60 MASQLQVFSP PSVSSSAFCS AKKLKIEPSG WDVSGQSSND KYYTHSKTLP ATQGQANSSH 70 80 90 100 110 120 QVANFNIPAY DQGLLLPAPA VEHIVVTAAD SSGSAATSTF QSSQTLTHRS NVSLLEPYQK 130 140 150 160 170 180 CGLKRKSEEV DSNGSVQIIE EHPPLMLQNR TVVGAAATTT TVTTKSSSSS GEGDYQLVQH 190 200 210 220 230 240 EILCSMTNSY EVLEFLGRGT FGQVAKCWKR STKEIVAIKI LKNHPSYARQ GQIEVSILSR 250 260 270 280 290 300 LSSENADEYN FVRSYECFQH KNHTCLVFEM LEQNLYDFLK QNKFSPLPLK YIRPILQQVA 310 320 330 340 350 360 TALMKLKSLG LIHADLKPEN IMLVDPVRQP YRVKVIDFGS ASHVSKAVCS TYLQSRYYRA 370 380 390 400 410 420 PEIILGLPFC EAIDMWSLGC VIAELFLGWP LYPGASEYDQ IRYISQTQGL PAEYLLSAGT 430 440 450 460 470 480 KTTRFFNRDP NLGYPLWRLK TPEEHELETG IKSKEARKYI FNCLDDMAQV NMSTDLEGTD 490 500 510 520 530 540 MLAEKADRRE YIDLLKKMLT IDADKRITPL KTLNHQFVTM THLLDFPHSN HVKSCFQNME 550 560 570 580 590 600 ICKRRVHMYD TVSQIKSPFT THVAPNTSTN LTMSFSNQLN TVHNQASVLA SSSTAAAATL 610 620 630 640 650 660 SLANSDVSLL NYQSALYPSS AAPVPGVAQQ GVSLQPGTTQ ICTQTDPFQQ TFIVCPPAFQ 670 680 690 700 710 720 TGLQATTKHS GFPVRMDNAV PIVPQAPAAQ PLQIQSGVLT QGSCTPLMVA TLHPQVATIT 730 740 750 760 770 780 PQYAVPFTLS CAAGRPALVE QTAAVLQAWP GGTQQILLPS TWQQLPGVAL HNSVQPTAMI 790 800 810 820 830 840 PEAMGSGQQL ADWRNAHSHG NQYSTIMQQP SLLTNHVTLA TAQPLNVGVA HVVRQQQSSS 850 860 870 880 890 900 LPSKKNKQSA PVSSKSSLDV LPSQVYSLVG SSPLRTTSSY NSLVPVQDQH QPIIIPDTPS 910 920 930 940 950 960 PPVSVITIRS DTDEEEDNKY KPSSSGLKPR SNVISYVTVN DSPDSDSSLS SPYSTDTLSA 970 980 990 1000 1010 1020 LRGNSGSVLE GPGRVVADGT GTRTIIVPPL KTQLGDCTVA TQASGLLSNK TKPVASVSGQ 1030 1040 1050 1060 1070 1080 SSGCCITPTG YRAQRGGTSA AQPLNLSQNQ QSSAAPTSQE RSSNPAPRRQ QAFVAPLSQA 1090 1100 1110 1120 1130 1140 PYTFQHGSPL HSTGHPHLAP APAHLPSQAH LYTYAAPTSA AALGSTSSIA HLFSPQGSSR 1150 1160 1170 1180 1190 1200 HAAAYTTHPS TLVHQVPVSV GPSLLTSASV APAQYQHQFA TQSYIGSSRG STIYTGYPLS 1210 PTKISQYSYL
	Isoform 2 (HIPK1-beta) [UniParc]. Checksum: DC4EE791F0EEC369	FASTA	1,075	116,731
	10 20 30 40 50 60 MASQLQVFSP PSVSSSAFCS AKKLKIEPSG WDVSGQSSND KYYTHSKTLP ATQGQANSSH 70 80 90 100 110 120 QVANFNIPAY DQGLLLPAPA VEHIVVTAAD SSGSAATSTF QSSQTLTHRS NVSLLEPYQK 130 140 150 160 170 180 CGLKRKSEEV DSNGSVQIIE EHPPLMLQNR TVVGAAATTT TVTTKSSSSS GEGDYQLVQH 190 200 210 220 230 240 EILCSMTNSY EVLEFLGRGT FGQVAKCWKR STKEIVAIKI LKNHPSYARQ GQIEVSILSR 250 260 270 280 290 300 LSSENADEYN FVRSYECFQH KNHTCLVFEM LEQNLYDFLK QNKFSPLPLK YIRPILQQVA 310 320 330 340 350 360 TALMKLKSLG LIHADLKPEN IMLVDPVRQP YRVKVIDFGS ASHVSKAVCS TYLQSRYYRA 370 380 390 400 410 420 PEIILGLPFC EAIDMWSLGC VIAELFLGWP LYPGASEYDQ IRYISQTQGL PAEYLLSAGT 430 440 450 460 470 480 KTTRFFNRDP NLGYPLWRLK TPEEHELETG IKSKEARKYI FNCLDDMAQV NMSTDLEGTD 490 500 510 520 530 540 MLAEKADRRE YIDLLKKMLT IDADKRITPL KTLNHQFVTM THLLDFPHSN HVKSCFQNME 550 560 570 580 590 600 ICKRRVHMYD TVSQIKSPFT THVAPNTSTN LTMSFSNQLN TVHNQASVLA SSSTAAAATL 610 620 630 640 650 660 SLANSDVSLL NYQSALYPSS AAPVPGVAQQ GVSLQPGTTQ ICTQTDPFQQ TFIVCPPAFQ 670 680 690 700 710 720 TGLQATTKHS GFPVRMDNAV PIVPQAPAAQ PLQIQSGVLT QGSCTPLMVA TLHPQVATIT 730 740 750 760 770 780 PQYAVPFTLS CAAGRPALVE QTAAVLQAWP GGTQQILLPS TWQQLPGVAL HNSVQPTAMI 790 800 810 820 830 840 PEAMGSGQQL ADWRNAHSHG NQYSTIMQQP SLLTNHVTLA TAQPLNVGVA HVVRQQQSSS 850 860 870 880 890 900 LPSKKNKQSA PVSSKSSLDV LPSQVYSLVG SSPLRTTSSY NSLVPVQDQH QPIIIPDTPS 910 920 930 940 950 960 PPVSVITIRS DTDEEEDNKY KPSSSGLKPR SNVISYVTVN DSPDSDSSLS SPYSTDTLSA 970 980 990 1000 1010 1020 LRGNSGSVLE GPGRVVADGT GTRTIIVPPL KTQLGDCTVA TQASGLLSNK TKPVASVSGQ 1030 1040 1050 1060 1070 SSGCCITPTG YRAQRGGTSA AQPLNLSQVS AMGYCLLFGP CTVVTFWRTL LLAGC
	Isoform 3 [UniParc]. Checksum: ED30D5EDCA8D4918	FASTA	836	89,481
	10 20 30 40 50 60 MWSLGCVIAE LFLGWPLYPG ASEYDQIRYI SQTQGLPAEY LLSAGTKTTR FFNRDPNLGY 70 80 90 100 110 120 PLWRLKTPEE HELETGIKSK EARKYIFNCL DDMAQVNMST DLEGTDMLAE KADRREYIDL 130 140 150 160 170 180 LKKMLTIDAD KRITPLKTLN HQFVTMTHLL DFPHSNHVKS CFQNMEICKR RVHMYDTVSQ 190 200 210 220 230 240 IKSPFTTHVA PNTSTNLTMS FSNQLNTVHN QASVLASSST AAAATLSLAN SDVSLLNYQS 250 260 270 280 290 300 ALYPSSAAPV PGVAQQGVSL QPGTTQICTQ TDPFQQTFIV CPPAFQTGLQ ATTKHSGFPV 310 320 330 340 350 360 RMDNAVPIVP QAPAAQPLQI QSGVLTQGSC TPLMVATLHP QVATITPQYA VPFTLSCAAG 370 380 390 400 410 420 RPALVEQTAA VLQAWPGGTQ QILLPSTWQQ LPGVALHNSV QPTAMIPEAM GSGQQLADWR 430 440 450 460 470 480 NAHSHGNQYS TIMQQPSLLT NHVTLATAQP LNVGVAHVVR QQQSSSLPSK KNKQSAPVSS 490 500 510 520 530 540 KSSLDVLPSQ VYSLVGSSPL RTTSSYNSLV PVQDQHQPII IPDTPSPPVS VITIRSDTDE 550 560 570 580 590 600 EEDNKYKPSS SGLKPRSNVI SYVTVNDSPD SDSSLSSPYS TDTLSALRGN SGSVLEGPGR 610 620 630 640 650 660 VVADGTGTRT IIVPPLKTQL GDCTVATQAS GLLSNKTKPV ASVSGQSSGC CITPTGYRAQ 670 680 690 700 710 720 RGGTSAAQPL NLSQNQQSSA APTSQERSSN PAPRRQQAFV APLSQAPYTF QHGSPLHSTG 730 740 750 760 770 780 HPHLAPAPAH LPSQAHLYTY AAPTSAAALG STSSIAHLFS PQGSSRHAAA YTTHPSTLVH 790 800 810 820 830 QVPVSVGPSL LTSASVAPAQ YQHQFATQSY IGSSRGSTIY TGYPLSPTKI SQYSYL
	Isoform 4 [UniParc]. Checksum: 97A2176C8995F038	FASTA	816	87,302
	10 20 30 40 50 60 MVLMFQIRYI SQTQGLPAEY LLSAGTKTTR FFNRDPNLGY PLWRLKTPEE HELETGIKSK 70 80 90 100 110 120 EARKYIFNCL DDMAQVNMST DLEGTDMLAE KADRREYIDL LKKMLTIDAD KRITPLKTLN 130 140 150 160 170 180 HQFVTMTHLL DFPHSNHVKS CFQNMEICKR RVHMYDTVSQ IKSPFTTHVA PNTSTNLTMS 190 200 210 220 230 240 FSNQLNTVHN QASVLASSST AAAATLSLAN SDVSLLNYQS ALYPSSAAPV PGVAQQGVSL 250 260 270 280 290 300 QPGTTQICTQ TDPFQQTFIV CPPAFQTGLQ ATTKHSGFPV RMDNAVPIVP QAPAAQPLQI 310 320 330 340 350 360 QSGVLTQGSC TPLMVATLHP QVATITPQYA VPFTLSCAAG RPALVEQTAA VLQAWPGGTQ 370 380 390 400 410 420 QILLPSTWQQ LPGVALHNSV QPTAMIPEAM GSGQQLADWR NAHSHGNQYS TIMQQPSLLT 430 440 450 460 470 480 NHVTLATAQP LNVGVAHVVR QQQSSSLPSK KNKQSAPVSS KSSLDVLPSQ VYSLVGSSPL 490 500 510 520 530 540 RTTSSYNSLV PVQDQHQPII IPDTPSPPVS VITIRSDTDE EEDNKYKPSS SGLKPRSNVI 550 560 570 580 590 600 SYVTVNDSPD SDSSLSSPYS TDTLSALRGN SGSVLEGPGR VVADGTGTRT IIVPPLKTQL 610 620 630 640 650 660 GDCTVATQAS GLLSNKTKPV ASVSGQSSGC CITPTGYRAQ RGGTSAAQPL NLSQNQQSSA 670 680 690 700 710 720 APTSQERSSN PAPRRQQAFV APLSQAPYTF QHGSPLHSTG HPHLAPAPAH LPSQAHLYTY 730 740 750 760 770 780 AAPTSAAALG STSSIAHLFS PQGSSRHAAA YTTHPSTLVH QVPVSVGPSL LTSASVAPAQ 790 800 810 YQHQFATQSY IGSSRGSTIY TGYPLSPTKI SQYSYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of human HIPK1." Miyata Y. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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].
[3]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). Tissue: Testis.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1210 (ISOFORM 1). Tissue: Testis.
[6]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 720-1210 (ISOFORMS 1/3/4). Tissue: Brain.
[7]	"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization." Song J.J., Lee Y.J. J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY JNK1.
[8]	"Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity." Ecsedy J.A., Michaelson J.S., Leder P. Mol. Cell. Biol. 23:950-960(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH DAXX.
[9]	"Characterization of cells and gene-targeted mice deficient for the p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1)." Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A., Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W., Mak T.W., Thukral S.K. Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TP53, TISSUE SPECIFICITY, FUNCTION.
[10]	"Tumor necrosis factor alpha-induced desumoylation and cytoplasmic translocation of homeodomain-interacting protein kinase 1 are critical for apoptosis signal-regulating kinase 1-JNK/p38 activation." Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W. J. Biol. Chem. 280:15061-15070(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DAB2IP AND MAP3K5, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-25 AND LYS-1203, DESUMOYLATION MEDIATED BY TNF, MUTAGENESIS OF LYS-25; ASP-315; LYS-317; LYS-440; LYS-556 AND LYS-1203.
[11]	"DJ-1 interacts with HIPK1 and affects H2O2-induced cell death." Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H. Free Radic. Res. 40:155-165(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ANTI-OXIDATIVE STRESS, INTERACTION WITH PARK7, SUBCELLULAR LOCATION, DEGRADATION BY PARK7.
[12]	"SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis." Li X., Luo Y., Yu L., Lin Y., Luo D., Zhang H., He Y., Kim Y.-O., Kim Y., Tang S., Min W. Cell Death Differ. 15:739-750(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DESUMOYLATION BY SENP1, SUBCELLULAR LOCATION.
[13]	"HIPK1 interacts with c-Myb and modulates its activity through phosphorylation." Matre V., Nordgaard O., Alm-Kristiansen A.H., Ledsaak M., Gabrielsen O.S. Biochem. Biophys. Res. Commun. 388:150-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS MYB KINASE, INTERACTION WITH MYB, MUTAGENESIS OF LYS-219, SUBCELLULAR LOCATION.
[14]	"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-872, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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] CYS-310 AND VAL-1165.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB089957 mRNA. Translation: BAC57075.1. AL731797 Genomic DNA. Translation: CAI22792.1. AL731797 Genomic DNA. Translation: CAI22793.1. AL731797 Genomic DNA. Translation: CAI22795.1. AL137856 Genomic DNA. No translation available. CH471122 Genomic DNA. Translation: EAW56590.1. BC028408 mRNA. Translation: AAH28408.1. BC033012 mRNA. Translation: AAH33012.1. BC036057 mRNA. Translation: AAH36057.1. AL833829 mRNA. Translation: CAD38689.1. AB014530 mRNA. Translation: BAA31605.1.
IPI	IPI00178582. IPI00302302. IPI00383559. IPI00942467.
RefSeq	NP_689909.2. NM_152696.3. NP_852003.1. NM_181358.2. NP_938009.1. NM_198268.2. NP_938010.1. NM_198269.2.
UniGene	Hs.532363.
3D structure databases
ProteinModelPortal	Q86Z02.
SMR	Q86Z02. Positions 188-517.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86Z02. 6 interactions.
MINT	MINT-1187651.
PTM databases
PhosphoSite	Q86Z02.
Polymorphism databases
DMDM	34395641.
Proteomic databases
PaxDb	Q86Z02.
PRIDE	Q86Z02.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000340480; ENSP00000340956; ENSG00000163349. ENST00000369553; ENSP00000358566; ENSG00000163349. ENST00000369558; ENSP00000358571; ENSG00000163349. ENST00000369559; ENSP00000358572; ENSG00000163349. ENST00000406344; ENSP00000384960; ENSG00000163349. ENST00000443627; ENSP00000409673; ENSG00000163349.
GeneID	204851.
KEGG	hsa:204851.
UCSC	uc001eel.3. human. uc001eem.3. human. uc001eep.3. human.
Organism-specific databases
CTD	204851.
GeneCards	GC01P114471.
HGNC	HGNC:19006. HIPK1.
HPA	HPA016664.
MIM	608003. gene.
neXtProt	NX_Q86Z02.
PharmGKB	PA134897980.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG051908.
InParanoid	Q86Z02.
KO	K08826.
OrthoDB	EOG4K9BBD.
PhylomeDB	Q86Z02.
Gene expression databases
ArrayExpress	Q86Z02.
Bgee	Q86Z02.
CleanEx	HS_HIPK1.
Genevestigator	Q86Z02.
GermOnline	ENSG00000163349. 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	Q86Z02.
ChEMBL	CHEMBL5427.
ChiTaRS	HIPK1. human.
GenomeRNAi	204851.
NextBio	90482.
SOURCE	Search...

Entry information

Entry name

HIPK1_HUMAN

Accession

Primary (citable) accession number: Q86Z02
Secondary accession number(s): A6NJ34 , O75125, Q5SQL2, Q5SQL4, Q5SQL5, Q8IYD7, Q8NDN5, Q8NEB6, Q8TBZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 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.