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Q14202 (ZMYM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger MYM-type protein 3
Alternative name(s):
Zinc finger protein 261
Gene names
Name:ZMYM3
Synonyms:DXS6673E, KIAA0385, ZNF261
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the regulation of cell morphology and cytoskeletal organization. Ref.12

Subunit structure

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. Ref.7

Subcellular location

Nucleus By similarity.

Tissue specificity

Most abundant in brain, moderate in muscle and heart, low in other tissues except placenta.

Involvement in disease

A chromosomal aberration involving ZMYM3 may be a cause of X-linked mental retardation in Xq13.1. Translocation t(X;13)(q13.1;?).

Sequence similarities

Contains 9 MYM-type zinc fingers.

Sequence caution

The sequence BAA20839.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14202-1)

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: Q14202-2)

The sequence of this isoform differs from the canonical sequence as follows:
     793-804: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q14202-3)

The sequence of this isoform differs from the canonical sequence as follows:
     491-495: KNTRV → VGPRE
     496-1370: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13701370Zinc finger MYM-type protein 3
PRO_0000191378

Regions

Zinc finger332 – 36635MYM-type 1
Zinc finger378 – 42245MYM-type 2
Zinc finger429 – 46436MYM-type 3
Zinc finger477 – 51135MYM-type 4
Zinc finger521 – 55939MYM-type 5
Zinc finger567 – 60438MYM-type 6
Zinc finger612 – 64635MYM-type 7
Zinc finger653 – 69240MYM-type 8
Zinc finger699 – 73335MYM-type 9

Amino acid modifications

Modified residue2631Phosphoserine Ref.8 Ref.9
Modified residue2671Phosphoserine Ref.8 Ref.9
Modified residue4641Phosphoserine Ref.9

Natural variations

Alternative sequence491 – 4955KNTRV → VGPRE in isoform 3.
VSP_043262
Alternative sequence496 – 1370875Missing in isoform 3.
VSP_043263
Alternative sequence793 – 80412Missing in isoform 2.
VSP_004492

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 088B5E01E7EE9C30

FASTA1,370152,379
        10         20         30         40         50         60 
MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PTRGWAPPGP SPSSGALDLL 

        70         80         90        100        110        120 
DTPAGLEKDP GVLDGATELL GLGGLLYKAP SPPEVDHGPE GTLAWDAGDQ TLEPGPGGQT 

       130        140        150        160        170        180 
PEVVPPDPGA GANSCSPEGL LEPLAPDSPI TLQSPHIEEE ETTSIATARR GSPGQEEELP 

       190        200        210        220        230        240 
QGQPQSPNAP PSPSVGETLG DGINSSQTKP GGSSPPAHPS LPGDGLTAKA SEKPPERKRS 

       250        260        270        280        290        300 
ERVRRAEPPK PEVVDSTESI PVSDEDSDAM VDDPNDEDFV PFRPRRSPRM SLRSSVSQRA 

       310        320        330        340        350        360 
GRSAVGTKMT CAHCRTPLQK GQTAYQRKGL PQLFCSSSCL TTFSKKPSGK KTCTFCKKEI 

       370        380        390        400        410        420 
WNTKDSVVAQ TGSGGSFHEF CTSVCLSLYE AQQQRPIPQS GDPADATRCS ICQKTGEVLH 

       430        440        450        460        470        480 
EVSNGSVVHR LCSDSCFSKF RANKGLKTNC CDQCGAYIYT KTGSPGPELL FHEGQQKRFC 

       490        500        510        520        530        540 
NTTCLGAYKK KNTRVYPCVW CKTLCKNFEM LSHVDRNGKT SLFCSLCCTT SYKVKQAGLT 

       550        560        570        580        590        600 
GPPRPCSFCR RSLSDPCYYN KVDRTVYQFC SPSCWTKFQR TSPEGGIHLS CHYCHSLFSG 

       610        620        630        640        650        660 
KPEVLDWQDQ VFQFCCRDCC EDFKRLRGVV SQCEHCRQEK LLHEKLRFSG VEKSFCSEGC 

       670        680        690        700        710        720 
VLLYKQDFTK KLGLCCITCT YCSQTCQRGV TEQLDGSTWD FCSEDCKSKY LLWYCKAARC 

       730        740        750        760        770        780 
HACKRQGKLL ETIHWRGQIR HFCNQQCLLR FYSQQNQPNL DTQSGPESLL NSQSPESKPQ 

       790        800        810        820        830        840 
TPSQTKVENS NTVRTPEENG NLGKIPVKTR SAPTAPTPPP PPPPATPRKN KAAMCKPLMQ 

       850        860        870        880        890        900 
NRGVSCKVEM KSKGSQTEEW KPQVIVLPIP VPIFVPVPMH LYCQKVPVPF SMPIPVPVPM 

       910        920        930        940        950        960 
FLPTTLESTD KIVETIEELK VKIPSNPLEA DILAMAEMIA EAEELDKASS DLCDLVSNQS 

       970        980        990       1000       1010       1020 
AEGLLEDCDL FGPARDDVLA MAVKMANVLD EPGQDLEADF PKNPLDINPS VDFLFDCGLV 

      1030       1040       1050       1060       1070       1080 
GPEDVSTEQD LPRTMRKGQK RLVLSESCSR DSMSSQPSCT GLNYSYGVNA WKCWVQSKYA 

      1090       1100       1110       1120       1130       1140 
NGETSKGDEL RFGPKPMRIK EDILACSAAE LNYGLAQFVR EITRPNGERY EPDSIYYLCL 

      1150       1160       1170       1180       1190       1200 
GIQQYLLENN RMVNIFTDLY YLTFVQELNK SLSTWQPTLL PNNTVFSRVE EEHLWECKQL 

      1210       1220       1230       1240       1250       1260 
GVYSPFVLLN TLMFFNTKFF GLQTAEEHMQ LSFTNVVRQS RKCTTPRGTT KVVSIRYYAP 

      1270       1280       1290       1300       1310       1320 
VRQRKGRDTG PGKRKREDEA PILEQRENRM NPLRCPVKFY EFYLSKCPES LRTRNDVFYL 

      1330       1340       1350       1360       1370 
QPERSCIAES PLWYSVIPMD RSMLESMLNR ILAVREIYEE LGRPGEEDLD 

« Hide

Isoform 2 [UniParc].

Checksum: 8B636620F05DF82F
Show »

FASTA1,358151,084
Isoform 3 [UniParc].

Checksum: AC0D49C9F3D9CC15
Show »

FASTA49552,485

References

« Hide 'large scale' references
[1]"Cloning and characterization of DXS6673E, a candidate gene for X-linked mental retardation in Xq13.1."
van der Maarel S.M., Scholten I.H.G.M., Huber I., Phillippe C., Suijkerbuijk R.F., Gilgenkrantz S., Kere J., Cremers F.P.M., Ropers H.-H.
Hum. Mol. Genet. 5:887-897(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal brain.
[2]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 3).
Tissue: Lymph and Muscle.
[7]"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes."
Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.
J. Biol. Chem. 278:7234-7239(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A; RCOR1; PHF21A; ZMYM2; ZNF217; KIAA0182 AND GTF2I.
[8]"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-263 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-267 AND SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95808 mRNA. Translation: CAA65075.1.
AB002383 mRNA. Translation: BAA20839.2. Different initiation.
BT007095 mRNA. Translation: AAP35759.1.
AL590762 Genomic DNA. No translation available.
CH471132 Genomic DNA. Translation: EAX05302.1.
CH471132 Genomic DNA. Translation: EAX05303.1.
BC069057 mRNA. Translation: AAH69057.1.
BC013009 mRNA. Translation: AAH13009.1.
RefSeqNP_001164633.1. NM_001171162.1.
NP_001164634.1. NM_001171163.1.
NP_005087.1. NM_005096.3.
NP_963893.1. NM_201599.2.
XP_005262366.1. XM_005262309.1.
XP_005262367.1. XM_005262310.1.
UniGeneHs.522684.

3D structure databases

ProteinModelPortalQ14202.
SMRQ14202. Positions 308-340, 348-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114637. 18 interactions.
IntActQ14202. 8 interactions.
MINTMINT-7969582.
STRING9606.ENSP00000322845.

PTM databases

PhosphoSiteQ14202.

Polymorphism databases

DMDM12644413.

Proteomic databases

PaxDbQ14202.
PRIDEQ14202.

Protocols and materials databases

DNASU9203.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314425; ENSP00000322845; ENSG00000147130. [Q14202-1]
ENST00000353904; ENSP00000343909; ENSG00000147130. [Q14202-1]
ENST00000373981; ENSP00000363093; ENSG00000147130. [Q14202-3]
ENST00000373998; ENSP00000363110; ENSG00000147130. [Q14202-2]
GeneID9203.
KEGGhsa:9203.
UCSCuc004dzh.2. human. [Q14202-1]
uc004dzj.2. human. [Q14202-2]
uc004dzl.4. human. [Q14202-3]

Organism-specific databases

CTD9203.
GeneCardsGC0XM070459.
HGNCHGNC:13054. ZMYM3.
HPAHPA003211.
MIM300061. gene.
neXtProtNX_Q14202.
PharmGKBPA37632.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86062.
HOGENOMHOG000293258.
HOVERGENHBG057545.
OrthoDBEOG7JT6VN.
PhylomeDBQ14202.
TreeFamTF336988.

Gene expression databases

ArrayExpressQ14202.
BgeeQ14202.
CleanExHS_ZMYM3.
GenevestigatorQ14202.

Family and domain databases

InterProIPR021893. DUF3504.
IPR011017. TRASH_dom.
IPR010507. Znf_MYM.
[Graphical view]
PfamPF12012. DUF3504. 1 hit.
PF06467. zf-FCS. 10 hits.
[Graphical view]
SMARTSM00746. TRASH. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiZMYM3.
GenomeRNAi9203.
NextBio34497.
PROQ14202.
SOURCESearch...

Entry information

Entry nameZMYM3_HUMAN
AccessionPrimary (citable) accession number: Q14202
Secondary accession number(s): D3DVV3, O15089, Q96E26
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: March 19, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM