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Protein

Zinc finger MYM-type protein 3

Gene

ZMYM3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

BgeeiQ14202.
CleanExiHS_ZMYM3.
ExpressionAtlasiQ14202. baseline and differential.
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. 24 interactions.
IntActiQ14202. 8 interactions.
MINTiMINT-7969582.
STRINGi9606.ENSP00000322845.

Structurei

3D structure databases

ProteinModelPortaliQ14202.
SMRiQ14202. Positions 308-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 9 MYM-type zinc fingers.Curated

Zinc finger

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

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG86062.
GeneTreeiENSGT00550000074408.
HOGENOMiHOG000293258.
HOVERGENiHBG057545.
InParanoidiQ14202.
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

        10         20         30         40         50
MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PTRGWAPPGP
60 70 80 90 100
SPSSGALDLL DTPAGLEKDP GVLDGATELL GLGGLLYKAP SPPEVDHGPE
110 120 130 140 150
GTLAWDAGDQ TLEPGPGGQT PEVVPPDPGA GANSCSPEGL LEPLAPDSPI
160 170 180 190 200
TLQSPHIEEE ETTSIATARR GSPGQEEELP QGQPQSPNAP PSPSVGETLG
210 220 230 240 250
DGINSSQTKP GGSSPPAHPS LPGDGLTAKA SEKPPERKRS ERVRRAEPPK
260 270 280 290 300
PEVVDSTESI PVSDEDSDAM VDDPNDEDFV PFRPRRSPRM SLRSSVSQRA
310 320 330 340 350
GRSAVGTKMT CAHCRTPLQK GQTAYQRKGL PQLFCSSSCL TTFSKKPSGK
360 370 380 390 400
KTCTFCKKEI WNTKDSVVAQ TGSGGSFHEF CTSVCLSLYE AQQQRPIPQS
410 420 430 440 450
GDPADATRCS ICQKTGEVLH EVSNGSVVHR LCSDSCFSKF RANKGLKTNC
460 470 480 490 500
CDQCGAYIYT KTGSPGPELL FHEGQQKRFC NTTCLGAYKK KNTRVYPCVW
510 520 530 540 550
CKTLCKNFEM LSHVDRNGKT SLFCSLCCTT SYKVKQAGLT GPPRPCSFCR
560 570 580 590 600
RSLSDPCYYN KVDRTVYQFC SPSCWTKFQR TSPEGGIHLS CHYCHSLFSG
610 620 630 640 650
KPEVLDWQDQ VFQFCCRDCC EDFKRLRGVV SQCEHCRQEK LLHEKLRFSG
660 670 680 690 700
VEKSFCSEGC VLLYKQDFTK KLGLCCITCT YCSQTCQRGV TEQLDGSTWD
710 720 730 740 750
FCSEDCKSKY LLWYCKAARC HACKRQGKLL ETIHWRGQIR HFCNQQCLLR
760 770 780 790 800
FYSQQNQPNL DTQSGPESLL NSQSPESKPQ TPSQTKVENS NTVRTPEENG
810 820 830 840 850
NLGKIPVKTR SAPTAPTPPP PPPPATPRKN KAAMCKPLMQ NRGVSCKVEM
860 870 880 890 900
KSKGSQTEEW KPQVIVLPIP VPIFVPVPMH LYCQKVPVPF SMPIPVPVPM
910 920 930 940 950
FLPTTLESTD KIVETIEELK VKIPSNPLEA DILAMAEMIA EAEELDKASS
960 970 980 990 1000
DLCDLVSNQS AEGLLEDCDL FGPARDDVLA MAVKMANVLD EPGQDLEADF
1010 1020 1030 1040 1050
PKNPLDINPS VDFLFDCGLV GPEDVSTEQD LPRTMRKGQK RLVLSESCSR
1060 1070 1080 1090 1100
DSMSSQPSCT GLNYSYGVNA WKCWVQSKYA NGETSKGDEL RFGPKPMRIK
1110 1120 1130 1140 1150
EDILACSAAE LNYGLAQFVR EITRPNGERY EPDSIYYLCL GIQQYLLENN
1160 1170 1180 1190 1200
RMVNIFTDLY YLTFVQELNK SLSTWQPTLL PNNTVFSRVE EEHLWECKQL
1210 1220 1230 1240 1250
GVYSPFVLLN TLMFFNTKFF GLQTAEEHMQ LSFTNVVRQS RKCTTPRGTT
1260 1270 1280 1290 1300
KVVSIRYYAP VRQRKGRDTG PGKRKREDEA PILEQRENRM NPLRCPVKFY
1310 1320 1330 1340 1350
EFYLSKCPES LRTRNDVFYL QPERSCIAES PLWYSVIPMD RSMLESMLNR
1360 1370
ILAVREIYEE LGRPGEEDLD
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. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei491 – 4955KNTRV → VGPRE in isoform 3. 2 PublicationsVSP_043262
Alternative sequencei496 – 1370875Missing in isoform 3. 2 PublicationsVSP_043263Add
BLAST
Alternative sequencei793 – 80412Missing in isoform 2. 1 PublicationVSP_004492Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ14202.
SMRiQ14202. Positions 308-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114637. 24 interactions.
IntActiQ14202. 8 interactions.
MINTiMINT-7969582.
STRINGi9606.ENSP00000322845.

PTM databases

PhosphoSiteiQ14202.

Polymorphism databases

DMDMi12644413.

Proteomic databases

MaxQBiQ14202.
PaxDbiQ14202.
PRIDEiQ14202.

Protocols and materials databases

DNASUi9203.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314425; ENSP00000322845; 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]

Organism-specific databases

CTDi9203.
GeneCardsiGC0XM070459.
HGNCiHGNC:13054. ZMYM3.
HPAiHPA003211.
MIMi300061. gene.
neXtProtiNX_Q14202.
PharmGKBiPA37632.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG86062.
GeneTreeiENSGT00550000074408.
HOGENOMiHOG000293258.
HOVERGENiHBG057545.
InParanoidiQ14202.
OrthoDBiEOG7JT6VN.
PhylomeDBiQ14202.
TreeFamiTF336988.

Miscellaneous databases

GeneWikiiZMYM3.
GenomeRNAii9203.
NextBioi34497.
PROiQ14202.
SOURCEiSearch...

Gene expression databases

BgeeiQ14202.
CleanExiHS_ZMYM3.
ExpressionAtlasiQ14202. baseline and differential.
GenevestigatoriQ14202.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 125 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

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 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.