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Q14202

- ZMYM3_HUMAN

UniProt

Q14202 - ZMYM3_HUMAN

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Protein

Zinc finger MYM-type protein 3

Gene
ZMYM3, DXS6673E, KIAA0385, ZNF261
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of cell morphology and cytoskeletal organization.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri332 – 36635MYM-type 1Add
BLAST
Zinc fingeri378 – 42245MYM-type 2Add
BLAST
Zinc fingeri429 – 46436MYM-type 3Add
BLAST
Zinc fingeri477 – 51135MYM-type 4Add
BLAST
Zinc fingeri521 – 55939MYM-type 5Add
BLAST
Zinc fingeri567 – 60438MYM-type 6Add
BLAST
Zinc fingeri612 – 64635MYM-type 7Add
BLAST
Zinc fingeri653 – 69240MYM-type 8Add
BLAST
Zinc fingeri699 – 73335MYM-type 9Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. cytoskeleton organization Source: UniProtKB
  2. multicellular organismal development Source: ProtInc
  3. regulation of cell morphogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger MYM-type protein 3
Alternative name(s):
Zinc finger protein 261
Gene namesi
Name:ZMYM3
Synonyms:DXS6673E, KIAA0385, ZNF261
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:13054. ZMYM3.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Organism-specific databases

PharmGKBiPA37632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13701370Zinc finger MYM-type protein 3PRO_0000191378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631Phosphoserine2 Publications
Modified residuei267 – 2671Phosphoserine2 Publications
Modified residuei464 – 4641Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14202.
PaxDbiQ14202.
PRIDEiQ14202.

PTM databases

PhosphoSiteiQ14202.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ14202.
BgeeiQ14202.
CleanExiHS_ZMYM3.
GenevestigatoriQ14202.

Organism-specific databases

HPAiHPA003211.

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.1 Publication

Protein-protein interaction databases

BioGridi114637. 18 interactions.
IntActiQ14202. 8 interactions.
MINTiMINT-7969582.
STRINGi9606.ENSP00000322845.

Structurei

3D structure databases

ProteinModelPortaliQ14202.
SMRiQ14202. Positions 308-340.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG86062.
HOGENOMiHOG000293258.
HOVERGENiHBG057545.
OrthoDBiEOG7JT6VN.
PhylomeDBiQ14202.
TreeFamiTF336988.

Family and domain databases

InterProiIPR021893. DUF3504.
IPR011017. TRASH_dom.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF12012. DUF3504. 1 hit.
PF06467. zf-FCS. 10 hits.
[Graphical view]
SMARTiSM00746. TRASH. 10 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14202-1) [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

MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PTRGWAPPGP     50
SPSSGALDLL DTPAGLEKDP GVLDGATELL GLGGLLYKAP SPPEVDHGPE 100
GTLAWDAGDQ TLEPGPGGQT PEVVPPDPGA GANSCSPEGL LEPLAPDSPI 150
TLQSPHIEEE ETTSIATARR GSPGQEEELP QGQPQSPNAP PSPSVGETLG 200
DGINSSQTKP GGSSPPAHPS LPGDGLTAKA SEKPPERKRS ERVRRAEPPK 250
PEVVDSTESI PVSDEDSDAM VDDPNDEDFV PFRPRRSPRM SLRSSVSQRA 300
GRSAVGTKMT CAHCRTPLQK GQTAYQRKGL PQLFCSSSCL TTFSKKPSGK 350
KTCTFCKKEI WNTKDSVVAQ TGSGGSFHEF CTSVCLSLYE AQQQRPIPQS 400
GDPADATRCS ICQKTGEVLH EVSNGSVVHR LCSDSCFSKF RANKGLKTNC 450
CDQCGAYIYT KTGSPGPELL FHEGQQKRFC NTTCLGAYKK KNTRVYPCVW 500
CKTLCKNFEM LSHVDRNGKT SLFCSLCCTT SYKVKQAGLT GPPRPCSFCR 550
RSLSDPCYYN KVDRTVYQFC SPSCWTKFQR TSPEGGIHLS CHYCHSLFSG 600
KPEVLDWQDQ VFQFCCRDCC EDFKRLRGVV SQCEHCRQEK LLHEKLRFSG 650
VEKSFCSEGC VLLYKQDFTK KLGLCCITCT YCSQTCQRGV TEQLDGSTWD 700
FCSEDCKSKY LLWYCKAARC HACKRQGKLL ETIHWRGQIR HFCNQQCLLR 750
FYSQQNQPNL DTQSGPESLL NSQSPESKPQ TPSQTKVENS NTVRTPEENG 800
NLGKIPVKTR SAPTAPTPPP PPPPATPRKN KAAMCKPLMQ NRGVSCKVEM 850
KSKGSQTEEW KPQVIVLPIP VPIFVPVPMH LYCQKVPVPF SMPIPVPVPM 900
FLPTTLESTD KIVETIEELK VKIPSNPLEA DILAMAEMIA EAEELDKASS 950
DLCDLVSNQS AEGLLEDCDL FGPARDDVLA MAVKMANVLD EPGQDLEADF 1000
PKNPLDINPS VDFLFDCGLV GPEDVSTEQD LPRTMRKGQK RLVLSESCSR 1050
DSMSSQPSCT GLNYSYGVNA WKCWVQSKYA NGETSKGDEL RFGPKPMRIK 1100
EDILACSAAE LNYGLAQFVR EITRPNGERY EPDSIYYLCL GIQQYLLENN 1150
RMVNIFTDLY YLTFVQELNK SLSTWQPTLL PNNTVFSRVE EEHLWECKQL 1200
GVYSPFVLLN TLMFFNTKFF GLQTAEEHMQ LSFTNVVRQS RKCTTPRGTT 1250
KVVSIRYYAP VRQRKGRDTG PGKRKREDEA PILEQRENRM NPLRCPVKFY 1300
EFYLSKCPES LRTRNDVFYL QPERSCIAES PLWYSVIPMD RSMLESMLNR 1350
ILAVREIYEE LGRPGEEDLD 1370
Length:1,370
Mass (Da):152,379
Last modified:December 1, 2000 - v2
Checksum:i088B5E01E7EE9C30
GO
Isoform 2 (identifier: Q14202-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     793-804: Missing.

Note: No experimental confirmation available.

Show »
Length:1,358
Mass (Da):151,084
Checksum:i8B636620F05DF82F
GO
Isoform 3 (identifier: Q14202-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:495
Mass (Da):52,485
Checksum:iAC0D49C9F3D9CC15
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei491 – 4955KNTRV → VGPRE in isoform 3. VSP_043262
Alternative sequencei496 – 1370875Missing in isoform 3. VSP_043263Add
BLAST
Alternative sequencei793 – 80412Missing in isoform 2. VSP_004492Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14409.1. [Q14202-1]
CCDS55443.1. [Q14202-3]
CCDS55444.1. [Q14202-2]
RefSeqiNP_001164633.1. NM_001171162.1. [Q14202-2]
NP_001164634.1. NM_001171163.1. [Q14202-3]
NP_005087.1. NM_005096.3. [Q14202-1]
NP_963893.1. NM_201599.2. [Q14202-1]
XP_005262366.1. XM_005262309.1. [Q14202-1]
XP_005262367.1. XM_005262310.1. [Q14202-2]
XP_006724778.1. XM_006724715.1. [Q14202-1]
UniGeneiHs.522684.

Genome annotation databases

EnsembliENST00000314425; ENSP00000322845; ENSG00000147130. [Q14202-1]
ENST00000353904; ENSP00000343909; ENSG00000147130. [Q14202-1]
ENST00000373981; ENSP00000363093; ENSG00000147130. [Q14202-3]
ENST00000373998; ENSP00000363110; ENSG00000147130. [Q14202-2]
GeneIDi9203.
KEGGihsa:9203.
UCSCiuc004dzh.2. human. [Q14202-1]
uc004dzj.2. human. [Q14202-2]
uc004dzl.4. human. [Q14202-3]

Polymorphism databases

DMDMi12644413.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14409.1. [Q14202-1 ]
CCDS55443.1. [Q14202-3 ]
CCDS55444.1. [Q14202-2 ]
RefSeqi NP_001164633.1. NM_001171162.1. [Q14202-2 ]
NP_001164634.1. NM_001171163.1. [Q14202-3 ]
NP_005087.1. NM_005096.3. [Q14202-1 ]
NP_963893.1. NM_201599.2. [Q14202-1 ]
XP_005262366.1. XM_005262309.1. [Q14202-1 ]
XP_005262367.1. XM_005262310.1. [Q14202-2 ]
XP_006724778.1. XM_006724715.1. [Q14202-1 ]
UniGenei Hs.522684.

3D structure databases

ProteinModelPortali Q14202.
SMRi Q14202. Positions 308-340.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114637. 18 interactions.
IntActi Q14202. 8 interactions.
MINTi MINT-7969582.
STRINGi 9606.ENSP00000322845.

PTM databases

PhosphoSitei Q14202.

Polymorphism databases

DMDMi 12644413.

Proteomic databases

MaxQBi Q14202.
PaxDbi Q14202.
PRIDEi Q14202.

Protocols and materials databases

DNASUi 9203.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314425 ; ENSP00000322845 ; ENSG00000147130 . [Q14202-1 ]
ENST00000353904 ; ENSP00000343909 ; ENSG00000147130 . [Q14202-1 ]
ENST00000373981 ; ENSP00000363093 ; ENSG00000147130 . [Q14202-3 ]
ENST00000373998 ; ENSP00000363110 ; ENSG00000147130 . [Q14202-2 ]
GeneIDi 9203.
KEGGi hsa:9203.
UCSCi uc004dzh.2. human. [Q14202-1 ]
uc004dzj.2. human. [Q14202-2 ]
uc004dzl.4. human. [Q14202-3 ]

Organism-specific databases

CTDi 9203.
GeneCardsi GC0XM070459.
HGNCi HGNC:13054. ZMYM3.
HPAi HPA003211.
MIMi 300061. gene.
neXtProti NX_Q14202.
PharmGKBi PA37632.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG86062.
HOGENOMi HOG000293258.
HOVERGENi HBG057545.
OrthoDBi EOG7JT6VN.
PhylomeDBi Q14202.
TreeFami TF336988.

Miscellaneous databases

GeneWikii ZMYM3.
GenomeRNAii 9203.
NextBioi 34497.
PROi Q14202.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14202.
Bgeei Q14202.
CleanExi HS_ZMYM3.
Genevestigatori Q14202.

Family and domain databases

InterProi IPR021893. DUF3504.
IPR011017. TRASH_dom.
IPR010507. Znf_MYM.
[Graphical view ]
Pfami PF12012. DUF3504. 1 hit.
PF06467. zf-FCS. 10 hits.
[Graphical view ]
SMARTi SM00746. TRASH. 10 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZMYM3_HUMAN
AccessioniPrimary (citable) accession number: Q14202
Secondary accession number(s): D3DVV3, O15089, Q96E26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: September 3, 2014
This is version 122 of the entry and version 2 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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi