Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc finger MYM-type protein 2

Gene

Zmym2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May function as a transcription factor.Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri351 – 38535MYM-type 1Add
BLAST
Zinc fingeri397 – 43741MYM-type 2Add
BLAST
Zinc fingeri444 – 47936MYM-type 3Add
BLAST
Zinc fingeri490 – 51829MYM-type 4Add
BLAST
Zinc fingeri558 – 59639MYM-type 5Add
BLAST
Zinc fingeri604 – 65148MYM-type 6Add
BLAST
Zinc fingeri659 – 69335MYM-type 7Add
BLAST
Zinc fingeri700 – 73940MYM-type 8Add
BLAST
Zinc fingeri746 – 78035MYM-type 9Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger MYM-type protein 2
Alternative name(s):
Zinc finger protein 198
Gene namesi
Name:Zmym2
Synonyms:Zfp198, Znf198
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1923257. Zmym2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13761376Zinc finger MYM-type protein 2PRO_0000191383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki88 – 88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki98 – 98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki104 – 104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki253 – 253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei305 – 3051PhosphoserineBy similarity
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki440 – 440Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki512 – 512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki528 – 528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki531 – 531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki575 – 575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki648 – 648Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki699 – 699Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei837 – 8371PhosphoserineBy similarity
Modified residuei1063 – 10631PhosphoserineCombined sources
Modified residuei1375 – 13751PhosphothreonineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9CU65.
MaxQBiQ9CU65.
PaxDbiQ9CU65.
PRIDEiQ9CU65.

PTM databases

iPTMnetiQ9CU65.
PhosphoSiteiQ9CU65.

Expressioni

Gene expression databases

BgeeiQ9CU65.
CleanExiMM_ZMYM2.
GenevisibleiQ9CU65. MM.

Interactioni

Subunit structurei

May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi217903. 9 interactions.
DIPiDIP-29928N.
IntActiQ9CU65. 2 interactions.
STRINGi10090.ENSMUSP00000022511.

Structurei

3D structure databases

ProteinModelPortaliQ9CU65.
SMRiQ9CU65. Positions 316-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 9 MYM-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri351 – 38535MYM-type 1Add
BLAST
Zinc fingeri397 – 43741MYM-type 2Add
BLAST
Zinc fingeri444 – 47936MYM-type 3Add
BLAST
Zinc fingeri490 – 51829MYM-type 4Add
BLAST
Zinc fingeri558 – 59639MYM-type 5Add
BLAST
Zinc fingeri604 – 65148MYM-type 6Add
BLAST
Zinc fingeri659 – 69335MYM-type 7Add
BLAST
Zinc fingeri700 – 73940MYM-type 8Add
BLAST
Zinc fingeri746 – 78035MYM-type 9Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IE8I. Eukaryota.
ENOG410XQR6. LUCA.
GeneTreeiENSGT00550000074408.
HOGENOMiHOG000293258.
HOVERGENiHBG057545.
InParanoidiQ9CU65.
OMAiAYGVNAW.
OrthoDBiEOG7JT6VN.
PhylomeDBiQ9CU65.
TreeFamiTF336988.

Family and domain databases

InterProiIPR021893. DUF3504.
IPR011017. TRASH_dom.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF12012. DUF3504. 1 hit.
PF06467. zf-FCS. 8 hits.
[Graphical view]
SMARTiSM00746. TRASH. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CU65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTSSVGTLE LTDQTPVLLG STAMATSLTN VGNSFSGPPN PLVSRSSKFQ
60 70 80 90 100
NSSVEDDDDV VFIEPVQPPP SSAPLVADQR PITFTSSKNE ELQGNDPKIL
110 120 130 140 150
PSSKELAPQK GSVSETIVID DEEDMETNQG QEKSSSNFIE RRPSETKNRT
160 170 180 190 200
NDVDFSSSTF SRSKVNAGVS NSGITTEPDS EIQIANVTTL ETGVSSVSDG
210 220 230 240 250
QLESTDGRDM NLMITHVTSL HNTSLGDGSN GLQSSNFGVN IQTYTPSLTS
260 270 280 290 300
QTKAGVGPFN PGRMNVAGDV FQNGESAPHH NPDSWISQSA SFPRNQKQQG
310 320 330 340 350
VDSLSPVASL PKQIFQPSNQ QPTKPVKVTC ANCKKPLQKG QTAYQRKGSA
360 370 380 390 400
HLFCSTTCLS SFSHKPAPKK LCVMCKKDIT TMKGTIVAQV DSSESFQEFC
410 420 430 440 450
STSCLSLYED KQSPAKGALN KSRCTICGKL TEIRHEVSFK NMTHKLCSDH
460 470 480 490 500
CFNRYRMANG LIMNCCEQCG EYLPSKGAGN NVLVVDGQQK RFCCQSCVTE
510 520 530 540 550
YKQVGSHPSF LKEVRDHMQD SFLMQPEKYG KLTTCTGCRT QCRFFDMTQC
560 570 580 590 600
IGPNGYMEPY CSTACMNSHK TKYAKSQSLG IICHFCKRNS LPQYQATMPD
610 620 630 640 650
GKLYNFCNSS CVAKFQALSM QSSPNGQFVA PSDIQLKCNY CKNSFCSKPE
660 670 680 690 700
ILEWENKVHQ FCSKTCSDDY KKLHCIVTYC EYCQEEKTLH ETVNFSGVKR
710 720 730 740 750
PFCSEGCKLL YKQDFARRLG LRCVTCNYCS QLCKKGATKE LDGVVRDFCS
760 770 780 790 800
EDCCKKFQEW YYKAARCDCC KSQGTLKERV QWRGEMKHFC DQHCLLRFYC
810 820 830 840 850
QQNEPNMTTQ KGPENLHYDQ GCQTSRTKMT GSAPPPSPTP NKEMKNKAIL
860 870 880 890 900
CKPLTMTKAT YCKPHMQTKS CQTDENWKTE YVPVPIPVPV YVPVPMHMYS
910 920 930 940 950
QNIPVPTTVP VPVPVPVFLP APLDSSEKIP ATVEDLKSKV SSDPLDSELL
960 970 980 990 1000
TMTDMMTEEE GKAEASNINS VIIETDIIGS DLTKNSDPDI QSNMPDVPYE
1010 1020 1030 1040 1050
PDLDIEIDFP RAAEELDMEN EFLLPPVFGE EYEEQPRPRS KKKGTKRKAV
1060 1070 1080 1090 1100
SGYQSHDDSS DNSECSFPFK YTYGVNAWKH WVKTRQLDED LLVLDELKSS
1110 1120 1130 1140 1150
KSVKLKEDLL SHTTAELNYG LAHFVNEIRR PNGENYAPDS IYYLCLGIQE
1160 1170 1180 1190 1200
YLCGSNRKDN IFIDPGYQMF EQELNKILRS WQPSILPDGS IFSRVEEDYL
1210 1220 1230 1240 1250
WRIKQLGSHS PVALLNTLFY FNTKYFGLKT VEQHLRLSFG TVFRHWKKNP
1260 1270 1280 1290 1300
LTMENKACLR YQVSSLCGTD NEDKIATGKR KHEDDEPVFE QVENTANPSR
1310 1320 1330 1340 1350
CPVKMFECYL SKSPQNLNQR MDVFYLQPEC SSSTDSPVWY TSTSLDRNTL
1360 1370
ENMLVRVLLV KDIYDKDNYE LDEDTD
Length:1,376
Mass (Da):154,642
Last modified:January 9, 2007 - v3
Checksum:i1D4955422F0646B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017929 mRNA. Translation: BAB31008.1.
AK135499 mRNA. Translation: BAE22556.1.
AK137708 mRNA. Translation: BAE23471.1.
AK137720 mRNA. Translation: BAE23475.1.
BC043450 mRNA. Translation: AAH43450.1.
BC141403 mRNA. Translation: AAI41404.1.
CCDSiCCDS49506.1.
RefSeqiNP_083774.2. NM_029498.3.
XP_006519728.1. XM_006519665.2.
UniGeneiMm.31417.
Mm.486624.

Genome annotation databases

EnsembliENSMUST00000022511; ENSMUSP00000022511; ENSMUSG00000021945.
GeneIDi76007.
KEGGimmu:76007.
UCSCiuc007ucs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017929 mRNA. Translation: BAB31008.1.
AK135499 mRNA. Translation: BAE22556.1.
AK137708 mRNA. Translation: BAE23471.1.
AK137720 mRNA. Translation: BAE23475.1.
BC043450 mRNA. Translation: AAH43450.1.
BC141403 mRNA. Translation: AAI41404.1.
CCDSiCCDS49506.1.
RefSeqiNP_083774.2. NM_029498.3.
XP_006519728.1. XM_006519665.2.
UniGeneiMm.31417.
Mm.486624.

3D structure databases

ProteinModelPortaliQ9CU65.
SMRiQ9CU65. Positions 316-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217903. 9 interactions.
DIPiDIP-29928N.
IntActiQ9CU65. 2 interactions.
STRINGi10090.ENSMUSP00000022511.

PTM databases

iPTMnetiQ9CU65.
PhosphoSiteiQ9CU65.

Proteomic databases

EPDiQ9CU65.
MaxQBiQ9CU65.
PaxDbiQ9CU65.
PRIDEiQ9CU65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022511; ENSMUSP00000022511; ENSMUSG00000021945.
GeneIDi76007.
KEGGimmu:76007.
UCSCiuc007ucs.1. mouse.

Organism-specific databases

CTDi7750.
MGIiMGI:1923257. Zmym2.

Phylogenomic databases

eggNOGiENOG410IE8I. Eukaryota.
ENOG410XQR6. LUCA.
GeneTreeiENSGT00550000074408.
HOGENOMiHOG000293258.
HOVERGENiHBG057545.
InParanoidiQ9CU65.
OMAiAYGVNAW.
OrthoDBiEOG7JT6VN.
PhylomeDBiQ9CU65.
TreeFamiTF336988.

Miscellaneous databases

ChiTaRSiZmym2. mouse.
PROiQ9CU65.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CU65.
CleanExiMM_ZMYM2.
GenevisibleiQ9CU65. MM.

Family and domain databases

InterProiIPR021893. DUF3504.
IPR011017. TRASH_dom.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF12012. DUF3504. 1 hit.
PF06467. zf-FCS. 8 hits.
[Graphical view]
SMARTiSM00746. TRASH. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Muellerian duct and Thymus.
  2. "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].
    Tissue: Brain and Eye.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1063 AND THR-1375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Spleen and Testis.

Entry informationi

Entry nameiZMYM2_MOUSE
AccessioniPrimary (citable) accession number: Q9CU65
Secondary accession number(s): B2RUS2
, Q3UUZ8, Q3UXK7, Q80XP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: January 9, 2007
Last modified: June 8, 2016
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.