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Protein

Ankyrin repeat domain-containing protein 17

Gene

ANKRD17

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

Functioni

Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity).By similarity4 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • blood vessel maturation Source: Ensembl
  • defense response to bacterium Source: UniProtKB
  • innate immune response Source: UniProtKB
  • negative regulation of smooth muscle cell differentiation Source: Ensembl
  • positive regulation of cell cycle Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of MDA-5 signaling pathway Source: UniProtKB
  • positive regulation of RIG-I signaling pathway Source: UniProtKB
  • regulation of DNA replication Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin repeat domain-containing protein 17
Alternative name(s):
Gene trap ankyrin repeat protein
Serologically defined breast cancer antigen NY-BR-16
Gene namesi
Name:ANKRD17
Synonyms:GTAR, KIAA0697
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:23575. ANKRD17.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134943225.

Polymorphism and mutation databases

BioMutaiANKRD17.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26032603Ankyrin repeat domain-containing protein 17PRO_0000307917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei134 – 1341PhosphoserineBy similarity
Modified residuei803 – 8031PhosphoserineCombined sources
Modified residuei1457 – 14571PhosphoserineCombined sources
Modified residuei1635 – 16351PhosphoserineCombined sources
Modified residuei1683 – 16831PhosphothreonineBy similarity
Modified residuei1696 – 16961PhosphoserineCombined sources
Modified residuei1700 – 17001PhosphoserineCombined sources
Modified residuei1709 – 17091PhosphoserineCombined sources
Modified residuei2042 – 20421Phosphoserine1 Publication
Modified residuei2044 – 20441PhosphoserineBy similarity
Modified residuei2045 – 20451PhosphoserineCombined sources1 Publication
Modified residuei2047 – 20471PhosphoserineCombined sources
Modified residuei2059 – 20591PhosphoserineCombined sources
Modified residuei2067 – 20671PhosphoserineCombined sources
Modified residuei2401 – 24011PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDK2.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75179.
MaxQBiO75179.
PaxDbiO75179.
PRIDEiO75179.

PTM databases

iPTMnetiO75179.
PhosphoSiteiO75179.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Gene expression databases

BgeeiO75179.
CleanExiHS_ANKRD17.
ExpressionAtlasiO75179. baseline and differential.
GenevisibleiO75179. HS.

Organism-specific databases

HPAiHPA045024.

Interactioni

Subunit structurei

Interacts with VP1 capsid protein of enterovirus 71 (EV71). Interacts (via N-terminus) with NOD2. Interacts with CDK2, MCM3, MCM5, MCM7, CDC6 and PCNA. Interacts with MAVS and IFIH1. Interacts (via the second ankyrin repeat cluster) with DDX58.4 Publications

Protein-protein interaction databases

BioGridi117519. 39 interactions.
DIPiDIP-47290N.
IntActiO75179. 18 interactions.
STRINGi9606.ENSP00000351416.

Structurei

3D structure databases

ProteinModelPortaliO75179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati233 – 26230ANK 1Add
BLAST
Repeati266 – 29530ANK 2Add
BLAST
Repeati300 – 32930ANK 3Add
BLAST
Repeati333 – 36230ANK 4Add
BLAST
Repeati366 – 39530ANK 5Add
BLAST
Repeati400 – 42930ANK 6Add
BLAST
Repeati433 – 46230ANK 7Add
BLAST
Repeati466 – 49530ANK 8Add
BLAST
Repeati499 – 52830ANK 9Add
BLAST
Repeati533 – 56230ANK 10Add
BLAST
Repeati563 – 59230ANK 11Add
BLAST
Repeati596 – 62530ANK 12Add
BLAST
Repeati629 – 65830ANK 13Add
BLAST
Repeati663 – 69230ANK 14Add
BLAST
Repeati696 – 72530ANK 15Add
BLAST
Repeati1082 – 111130ANK 16Add
BLAST
Repeati1115 – 114430ANK 17Add
BLAST
Repeati1149 – 117830ANK 18Add
BLAST
Repeati1182 – 121130ANK 19Add
BLAST
Repeati1217 – 124630ANK 20Add
BLAST
Repeati1251 – 128030ANK 21Add
BLAST
Repeati1284 – 131330ANK 22Add
BLAST
Repeati1319 – 134830ANK 23Add
BLAST
Repeati1352 – 138130ANK 24Add
BLAST
Repeati1385 – 141430ANK 25Add
BLAST
Domaini1725 – 178965KHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1442 – 152685Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 11015Gly-richAdd
BLAST
Compositional biasi858 – 1008151Gln-richAdd
BLAST
Compositional biasi1603 – 170098Ser-richAdd
BLAST
Compositional biasi1950 – 2106157Ser-richAdd
BLAST
Compositional biasi1966 – 203368Thr-richAdd
BLAST

Sequence similaritiesi

Contains 25 ANK repeats.PROSITE-ProRule annotation
Contains 1 KH domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4369. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOVERGENiHBG071352.
InParanoidiO75179.
KOiK16726.
OMAiDCGTASP.
OrthoDBiEOG7MPRDH.
PhylomeDBiO75179.
TreeFamiTF328552.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
3.30.1370.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF12796. Ank_2. 10 hits.
PF00013. KH_1. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 25 hits.
SM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 3 hits.
SSF54791. SSF54791. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50084. KH_TYPE_1. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75179-1) [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
MEKATVPVAA ATAAEGEGSP PAVAAVAGPP AAAEVGGGVG GSSRARSASS
60 70 80 90 100
PRGMVRVCDL LLKKKPPQQQ HHKAKRNRTC RPPSSSESSS DSDNSGGGGG
110 120 130 140 150
GGGGGGGGGG TSSNNSEEEE DDDDEEEEVS EVESFILDQD DLENPMLETA
160 170 180 190 200
SKLLLSGTAD GADLRTVDPE TQARLEALLE AAGIGKLSTA DGKAFADPEV
210 220 230 240 250
LRRLTSSVSC ALDEAAAALT RMRAESTANA GQSDNRSLAE ACSEGDVNAV
260 270 280 290 300
RKLLIEGRSV NEHTEEGESL LCLACSAGYY ELAQVLLAMH ANVEDRGIKG
310 320 330 340 350
DITPLMAAAN GGHVKIVKLL LAHKADVNAQ SSTGNTALTY ACAGGYVDVV
360 370 380 390 400
KVLLESGASI EDHNENGHTP LMEAGSAGHV EVARLLLENG AGINTHSNEF
410 420 430 440 450
KESALTLACY KGHLEMVRFL LEAGADQEHK TDEMHTALME ACMDGHVEVA
460 470 480 490 500
RLLLDSGAQV NMPADSFESP LTLAACGGHV ELAALLIERG ASLEEVNDEG
510 520 530 540 550
YTPLMEAARE GHEEMVALLL GQGANINAQT EETQETALTL ACCGGFLEVA
560 570 580 590 600
DFLIKAGADI ELGCSTPLME AAQEGHLELV KYLLAAGANV HATTATGDTA
610 620 630 640 650
LTYACENGHT DVADVLLQAG ADLEHESEGG RTPLMKAARA GHVCTVQFLI
660 670 680 690 700
SKGANVNRTT ANNDHTVLSL ACAGGHLAVV ELLLAHGADP THRLKDGSTM
710 720 730 740 750
LIEAAKGGHT SVVCYLLDYP NNLLSAPPPD VTQLTPPSHD LNRAPRVPVQ
760 770 780 790 800
ALPMVVPPQE PDKPPANVAT TLPIRNKAAS KQKSSSHLPA NSQDVQGYIT
810 820 830 840 850
NQSPESIVEE AQGKLTELEQ RIKEAIEKNA QLQSLELAHA DQLTKEKIEE
860 870 880 890 900
LNKTREEQIQ KKQKILEELQ KVERELQLKT QQQLKKQYLE VKAQRIQLQQ
910 920 930 940 950
QQQQSCQHLG LLTPVGVGEQ LSEGDYARLQ QVDPVLLKDE PQQTAAQMGF
960 970 980 990 1000
APIQPLAMPQ ALPLAAGPLP PGSIANLTEL QGVIVGQPVL GQAQLAGLGQ
1010 1020 1030 1040 1050
GILTETQQGL MVASPAQTLN DTLDDIMAAV SGRASAMSNT PTHSIAASIS
1060 1070 1080 1090 1100
QPQTPTPSPI ISPSAMLPIY PAIDIDAQTE SNHDTALTLA CAGGHEELVQ
1110 1120 1130 1140 1150
TLLERGASIE HRDKKGFTPL ILAATAGHVG VVEILLDNGA DIEAQSERTK
1160 1170 1180 1190 1200
DTPLSLACSG GRQEVVELLL ARGANKEHRN VSDYTPLSLA ASGGYVNIIK
1210 1220 1230 1240 1250
ILLNAGAEIN SRTGSKLGIS PLMLAAMNGH TAAVKLLLDM GSDINAQIET
1260 1270 1280 1290 1300
NRNTALTLAC FQGRTEVVSL LLDRKANVEH RAKTGLTPLM EAASGGYAEV
1310 1320 1330 1340 1350
GRVLLDKGAD VNAPPVPSSR DTALTIAADK GHYKFCELLI GRGAHIDVRN
1360 1370 1380 1390 1400
KKGNTPLWLA ANGGHLDVVQ LLVQAGADVD AADNRKITPL MAAFRKGHVK
1410 1420 1430 1440 1450
VVRYLVKEVN QFPSDSECMR YIATITDKEM LKKCHLCMES IVQAKDRQAA
1460 1470 1480 1490 1500
EANKNASILL EELDLEKLRE ESRRLALAAK REKRKEKRRK KKEEQRRKLE
1510 1520 1530 1540 1550
EIEAKNKENF ELQAAQEKEK LKVEDEPEVL TEPPSATTTT TIGISATWTT
1560 1570 1580 1590 1600
LAGSHGKRNN TITTTSSKRK NRKNKITPEN VQIIFDDPLP ISYSQPEKVN
1610 1620 1630 1640 1650
GESKSSSTSE SGDSDNMRIS SCSDESSNSN SSRKSDNHSP AVVTTTVSSK
1660 1670 1680 1690 1700
KQPSVLVTFP KEERKSVSGK ASIKLSETIS EGTSNSLSTC TKSGPSPLSS
1710 1720 1730 1740 1750
PNGKLTVASP KRGQKREEGW KEVVRRSKKV SVPSTVISRV IGRGGCNINA
1760 1770 1780 1790 1800
IREFTGAHID IDKQKDKTGD RIITIRGGTE STRQATQLIN ALIKDPDKEI
1810 1820 1830 1840 1850
DELIPKNRLK SSSANSKIGS SAPTTTAANT SLMGIKMTTV ALSSTSQTAT
1860 1870 1880 1890 1900
ALTVPAISSA STHKTIKNPV NNVRPGFPVS LPLAYPPPQF AHALLAAQTF
1910 1920 1930 1940 1950
QQIRPPRLPM THFGGTFPPA QSTWGPFPVR PLSPARATNS PKPHMVPRHS
1960 1970 1980 1990 2000
NQNSSGSQVN SAGSLTSSPT TTTSSSASTV PGTSTNGSPS SPSVRRQLFV
2010 2020 2030 2040 2050
TVVKTSNATT TTVTTTASNN NTAPTNATYP MPTAKEHYPV SSPSSPSPPA
2060 2070 2080 2090 2100
QPGGVSRNSP LDCGSASPNK VASSSEQEAG SPPVVETTNT RPPNSSSSSG
2110 2120 2130 2140 2150
SSSAHSNQQQ PPGSVSQEPR PPLQQSQVPP PEVRMTVPPL ATSSAPVAVP
2160 2170 2180 2190 2200
STAPVTYPMP QTPMGCPQPT PKMETPAIRP PPHGTTAPHK NSASVQNSSV
2210 2220 2230 2240 2250
AVLSVNHIKR PHSVPSSVQL PSTLSTQSAC QNSVHPANKP IAPNFSAPLP
2260 2270 2280 2290 2300
FGPFSTLFEN SPTSAHAFWG GSVVSSQSTP ESMLSGKSSY LPNSDPLHQS
2310 2320 2330 2340 2350
DTSKAPGFRP PLQRPAPSPS GIVNMDSPYG SVTPSSTHLG NFASNISGGQ
2360 2370 2380 2390 2400
MYGPGAPLGG APAAANFNRQ HFSPLSLLTP CSSASNDSSA QSVSSGVRAP
2410 2420 2430 2440 2450
SPAPSSVPLG SEKPSNVSQD RKVPVPIGTE RSARIRQTGT SAPSVIGSNL
2460 2470 2480 2490 2500
STSVGHSGIW SFEGIGGNQD KVDWCNPGMG NPMIHRPMSD PGVFSQHQAM
2510 2520 2530 2540 2550
ERDSTGIVTP SGTFHQHVPA GYMDFPKVGG MPFSVYGNAM IPPVAPIPDG
2560 2570 2580 2590 2600
AGGPIFNGPH AADPSWNSLI KMVSSSTENN GPQTVWTGPW APHMNSVHMN

QLG
Length:2,603
Mass (Da):274,258
Last modified:October 23, 2007 - v3
Checksum:iBD2BF51889283483
GO
Isoform 2 (identifier: O75179-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1028-1028: Missing.

Show »
Length:2,602
Mass (Da):274,187
Checksum:iF446818E5B8ED6FB
GO
Isoform 3 (identifier: O75179-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1176-1187: KEHRNVSDYTPL → YRSTGMVLITHL
     1188-2603: Missing.

Note: No experimental confirmation available.
Show »
Length:1,187
Mass (Da):124,637
Checksum:iA0D3DD0135B33F07
GO
Isoform 4 (identifier: O75179-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     982-1010: GVIVGQPVLGQAQLAGLGQGILTETQQGL → VLSSLLQPCFLSTLPLILMHRLRVIMTRR
     1011-1603: Missing.

Note: No experimental confirmation available.
Show »
Length:2,010
Mass (Da):210,593
Checksum:iCAF01D3CC80C50E5
GO
Isoform 5 (identifier: O75179-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     742-751: NRAPRVPVQA → TDNIFPRLVC
     752-2603: Missing.

Note: No experimental confirmation available.
Show »
Length:751
Mass (Da):77,825
Checksum:i391CFA8C368A3895
GO
Isoform 6 (identifier: O75179-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     778-1028: Missing.

Note: Gene prediction based on EST data.
Show »
Length:2,352
Mass (Da):246,751
Checksum:i36D86547A481C76C
GO
Isoform 7 (identifier: O75179-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: MEKATVPVAA...DDDDEEEEVS → MVETAAEMEAYVLEDIL

Note: Gene prediction based on cDNA data.
Show »
Length:2,490
Mass (Da):263,556
Checksum:iC9D1FFCA1D5C4906
GO

Sequence cautioni

The sequence AAG48253.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAH04173.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB15260.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB15260.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041P → S in BAA31672 (PubMed:9734811).Curated
Sequence conflicti705 – 7051A → P in AAG48253 (PubMed:12747765).Curated
Sequence conflicti713 – 7131V → G in AAG48253 (PubMed:12747765).Curated
Sequence conflicti1137 – 11371D → G in BAB15260 (PubMed:14702039).Curated
Sequence conflicti1163 – 11631Q → P in AAG48253 (PubMed:12747765).Curated
Sequence conflicti1391 – 13911Missing in CAD38571 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2560 – 25601H → Y.
Corresponds to variant rs2306059 [ dbSNP | Ensembl ].
VAR_036711

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 130130MEKAT…EEEVS → MVETAAEMEAYVLEDIL in isoform 7. CuratedVSP_054757Add
BLAST
Alternative sequencei742 – 75110NRAPRVPVQA → TDNIFPRLVC in isoform 5. 1 PublicationVSP_028859
Alternative sequencei752 – 26031852Missing in isoform 5. 1 PublicationVSP_028860Add
BLAST
Alternative sequencei778 – 1028251Missing in isoform 6. CuratedVSP_047048Add
BLAST
Alternative sequencei982 – 101029GVIVG…TQQGL → VLSSLLQPCFLSTLPLILMH RLRVIMTRR in isoform 4. 1 PublicationVSP_028861Add
BLAST
Alternative sequencei1011 – 1603593Missing in isoform 4. 1 PublicationVSP_028862Add
BLAST
Alternative sequencei1028 – 10281Missing in isoform 2. 1 PublicationVSP_028863
Alternative sequencei1176 – 118712KEHRN…DYTPL → YRSTGMVLITHL in isoform 3. 1 PublicationVSP_028864Add
BLAST
Alternative sequencei1188 – 26031416Missing in isoform 3. 1 PublicationVSP_028865Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308285 mRNA. Translation: AAG48253.1. Frameshift.
AC053527 Genomic DNA. No translation available.
AC095053 Genomic DNA. No translation available.
AC105757 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05655.1.
BC004173 mRNA. Translation: AAH04173.1. Sequence problems.
BC007747 mRNA. Translation: AAH07747.2.
BC019963 mRNA. Translation: AAH19963.1.
BC043394 mRNA. Translation: AAH43394.1.
AB014597 mRNA. Translation: BAA31672.2.
AL831903 mRNA. Translation: CAD38571.2.
AK025859 mRNA. Translation: BAB15260.1. Sequence problems.
CCDSiCCDS34003.1. [O75179-6]
CCDS34004.1. [O75179-1]
CCDS68721.1. [O75179-7]
PIRiT00353.
RefSeqiNP_001273700.1. NM_001286771.2. [O75179-7]
NP_056389.1. NM_015574.1. [O75179-2]
NP_115593.3. NM_032217.4. [O75179-1]
NP_942592.1. NM_198889.2. [O75179-6]
UniGeneiHs.601206.
Hs.733994.
Hs.743705.

Genome annotation databases

EnsembliENST00000330838; ENSP00000332265; ENSG00000132466. [O75179-6]
ENST00000358602; ENSP00000351416; ENSG00000132466. [O75179-1]
ENST00000509867; ENSP00000427151; ENSG00000132466. [O75179-7]
GeneIDi26057.
KEGGihsa:26057.
UCSCiuc003hgo.5. human. [O75179-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308285 mRNA. Translation: AAG48253.1. Frameshift.
AC053527 Genomic DNA. No translation available.
AC095053 Genomic DNA. No translation available.
AC105757 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05655.1.
BC004173 mRNA. Translation: AAH04173.1. Sequence problems.
BC007747 mRNA. Translation: AAH07747.2.
BC019963 mRNA. Translation: AAH19963.1.
BC043394 mRNA. Translation: AAH43394.1.
AB014597 mRNA. Translation: BAA31672.2.
AL831903 mRNA. Translation: CAD38571.2.
AK025859 mRNA. Translation: BAB15260.1. Sequence problems.
CCDSiCCDS34003.1. [O75179-6]
CCDS34004.1. [O75179-1]
CCDS68721.1. [O75179-7]
PIRiT00353.
RefSeqiNP_001273700.1. NM_001286771.2. [O75179-7]
NP_056389.1. NM_015574.1. [O75179-2]
NP_115593.3. NM_032217.4. [O75179-1]
NP_942592.1. NM_198889.2. [O75179-6]
UniGeneiHs.601206.
Hs.733994.
Hs.743705.

3D structure databases

ProteinModelPortaliO75179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117519. 39 interactions.
DIPiDIP-47290N.
IntActiO75179. 18 interactions.
STRINGi9606.ENSP00000351416.

PTM databases

iPTMnetiO75179.
PhosphoSiteiO75179.

Polymorphism and mutation databases

BioMutaiANKRD17.

Proteomic databases

EPDiO75179.
MaxQBiO75179.
PaxDbiO75179.
PRIDEiO75179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330838; ENSP00000332265; ENSG00000132466. [O75179-6]
ENST00000358602; ENSP00000351416; ENSG00000132466. [O75179-1]
ENST00000509867; ENSP00000427151; ENSG00000132466. [O75179-7]
GeneIDi26057.
KEGGihsa:26057.
UCSCiuc003hgo.5. human. [O75179-1]

Organism-specific databases

CTDi26057.
GeneCardsiANKRD17.
HGNCiHGNC:23575. ANKRD17.
HPAiHPA045024.
MIMi615929. gene.
neXtProtiNX_O75179.
PharmGKBiPA134943225.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4369. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOVERGENiHBG071352.
InParanoidiO75179.
KOiK16726.
OMAiDCGTASP.
OrthoDBiEOG7MPRDH.
PhylomeDBiO75179.
TreeFamiTF328552.

Miscellaneous databases

ChiTaRSiANKRD17. human.
GeneWikiiANKRD17.
GenomeRNAii26057.
NextBioi35500543.
PROiO75179.
SOURCEiSearch...

Gene expression databases

BgeeiO75179.
CleanExiHS_ANKRD17.
ExpressionAtlasiO75179. baseline and differential.
GenevisibleiO75179. HS.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
3.30.1370.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF12796. Ank_2. 10 hits.
PF00013. KH_1. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 25 hits.
SM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 3 hits.
SSF54791. SSF54791. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50084. KH_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression."
    Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.
    Cancer Immun. 1:4-4(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Mammary gland.
  2. "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].
  3. 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 1 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-2603 (ISOFORM 4).
    Tissue: Lymph, Muscle, Placenta and Uterus.
  5. "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 117-2603 (ISOFORM 2).
    Tissue: Brain.
  6. "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.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1487 (ISOFORM 1).
    Tissue: Brain.
  8. "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] OF 1035-1492 (ISOFORM 1).
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2059, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "The VP1 structural protein of enterovirus 71 interacts with human ornithine decarboxylase and gene trap ankyrin repeat."
    Yeo W.M., Chow V.T.K.
    Microb. Pathog. 42:129-137(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VP1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803; SER-1700; SER-1709; SER-2045; SER-2047 AND SER-2401, 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. "Identification and functional analysis of a novel cyclin e/cdk2 substrate ankrd17."
    Deng M., Li F., Ballif B.A., Li S., Chen X., Guo L., Ye X.
    J. Biol. Chem. 284:7875-7888(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH CDK2; MCM3; MCM5; MCM7; CDC6 AND PCNA, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2042; SER-2045 AND SER-2401 BY CDK2, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  15. "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-19; SER-1709; SER-2047 AND SER-2401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-1457; SER-1709; SER-2047 AND SER-2067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-1635; SER-1696; SER-1709 AND SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Ankrd17 positively regulates RIG-I-like receptor (RLR)-mediated immune signaling."
    Wang Y., Tong X., Li G., Li J., Deng M., Ye X.
    Eur. J. Immunol. 42:1304-1315(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAVS; IFIH1; DDX58, SUBCELLULAR LOCATION, FUNCTION.
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and Nod2-mediated inflammatory responses."
    Menning M., Kufer T.A.
    FEBS Lett. 587:2137-2142(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOD2, FUNCTION.
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2045; SER-2047 AND SER-2059, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiANR17_HUMAN
AccessioniPrimary (citable) accession number: O75179
Secondary accession number(s): E7EUV3
, G5E964, Q6PJ85, Q6PK85, Q6PKA2, Q86XI3, Q8NDR5, Q96I86, Q9H288, Q9H6J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: May 11, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.