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Protein

Zinc finger MYM-type protein 4

Gene

ZMYM4

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 fingeri362 – 40241MYM-type 1Add
BLAST
Zinc fingeri414 – 45744MYM-type 2Add
BLAST
Zinc fingeri464 – 49936MYM-type 3Add
BLAST
Zinc fingeri510 – 54435MYM-type 4Add
BLAST
Zinc fingeri554 – 59239MYM-type 5Add
BLAST
Zinc fingeri600 – 63132MYM-type 6Add
BLAST
Zinc fingeri708 – 74235MYM-type 7Add
BLAST
Zinc fingeri749 – 78840MYM-type 8Add
BLAST
Zinc fingeri795 – 82935MYM-type 9Add
BLAST

GO - Molecular functioni

GO - Biological processi

  • cytoskeleton organization Source: UniProtKB
  • multicellular organism development Source: ProtInc
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger MYM-type protein 4
Alternative name(s):
Zinc finger protein 262
Gene namesi
Name:ZMYM4
Synonyms:KIAA0425, ZNF262
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:13055. ZMYM4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37633.

Polymorphism and mutation databases

BioMutaiZMYM4.
DMDMi74762280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 15481547Zinc finger MYM-type protein 4PRO_0000299017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei107 – 1071PhosphothreonineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei122 – 1221PhosphoserineCombined sources
Cross-linki149 – 149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei162 – 1621PhosphoserineCombined sources
Cross-linki250 – 250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki273 – 273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki430 – 430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1030 – 10301PhosphoserineCombined sources
Modified residuei1181 – 11811PhosphoserineCombined sources
Modified residuei1256 – 12561PhosphoserineCombined sources
Modified residuei1539 – 15391PhosphoserineCombined sources
Modified residuei1542 – 15421PhosphoserineCombined sources
Modified residuei1547 – 15471PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5VZL5.
MaxQBiQ5VZL5.
PaxDbiQ5VZL5.
PRIDEiQ5VZL5.

PTM databases

iPTMnetiQ5VZL5.
PhosphoSiteiQ5VZL5.

Miscellaneous databases

PMAP-CutDBQ5VZL5.

Expressioni

Tissue specificityi

Expressed at higher level in heart, skeletal muscle, kidney and liver.1 Publication

Gene expression databases

BgeeiQ5VZL5.
CleanExiHS_ZMYM4.
ExpressionAtlasiQ5VZL5. baseline and differential.
GenevisibleiQ5VZL5. HS.

Organism-specific databases

HPAiHPA051301.
HPA054802.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CTCFP497113EBI-2514659,EBI-932887
FHL2Q141923EBI-2514659,EBI-701903
ROR2A1L4F53EBI-2514659,EBI-10172778
RUNX1T1Q06455-43EBI-2514659,EBI-10224192
UBQLN1Q9UMX03EBI-2514659,EBI-741480
UBQLN1Q9UMX0-23EBI-2514659,EBI-10173939

Protein-protein interaction databases

BioGridi114636. 34 interactions.
IntActiQ5VZL5. 20 interactions.
STRINGi9606.ENSP00000322915.

Structurei

3D structure databases

ProteinModelPortaliQ5VZL5.
SMRiQ5VZL5. Positions 338-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 9 MYM-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri362 – 40241MYM-type 1Add
BLAST
Zinc fingeri414 – 45744MYM-type 2Add
BLAST
Zinc fingeri464 – 49936MYM-type 3Add
BLAST
Zinc fingeri510 – 54435MYM-type 4Add
BLAST
Zinc fingeri554 – 59239MYM-type 5Add
BLAST
Zinc fingeri600 – 63132MYM-type 6Add
BLAST
Zinc fingeri708 – 74235MYM-type 7Add
BLAST
Zinc fingeri749 – 78840MYM-type 8Add
BLAST
Zinc fingeri795 – 82935MYM-type 9Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IE8I. Eukaryota.
ENOG410XQR6. LUCA.
GeneTreeiENSGT00550000074408.
HOVERGENiHBG106731.
InParanoidiQ5VZL5.
OMAiDNIFTEP.
OrthoDBiEOG75J0M6.
PhylomeDBiQ5VZL5.
TreeFamiTF336988.

Family and domain databases

InterProiIPR021893. DUF3504.
IPR011017. TRASH_dom.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF12012. DUF3504. 1 hit.
PF06467. zf-FCS. 5 hits.
[Graphical view]
SMARTiSM00746. TRASH. 10 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5VZL5-1) [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
MAEREVESGP RKRFEQKSGA VFDEIVENCG GIMDTEMSED IDHNLTPTLD
60 70 80 90 100
SMSYGMPNQT GSENSLLDED DYFLNSGDLA GIPVVGSDNE DEQDFSSKDN
110 120 130 140 150
LVSSIHTDDS LEVERRVTQH ESDNENEIQI QNKLKKDFPK QFDQVSVFKS
160 170 180 190 200
IRKDFSLVRE NSKETFSGKE KNRDLTYERE KRLDKPHKDL DSRLKSSFFD
210 220 230 240 250
KAANQVEETL HTHLPQTPET NFRDSSYPFA NKESIGSELG NSFASNIRIK
260 270 280 290 300
EEPLDDEYDK AMAPQQGLLD KIKDEPDNAQ EYSHGQQQKT QEGELKISAV
310 320 330 340 350
FSVSGSPLAP QLTTGFQPSL ASSGMNKMLP SVPATAVRVS CSGCKKILQK
360 370 380 390 400
GQTAYQRKGS TQLFCSTLCL TGYTVPPARP PPPLTKKTCS SCSKDILNPK
410 420 430 440 450
DVISAQFENT TTSKDFCSQS CLSTYELKKK PIVTINTNSI STKCSMCQKN
460 470 480 490 500
AVIRHEVNYQ NVVHKLCSDA CFSKFRSANN LTMNCCENCG GYCYSGSGQC
510 520 530 540 550
HMLQIEGQSK KFCSSSCITA YKQKSAKITP CALCKSLRSS AEMIENTNSL
560 570 580 590 600
GKTELFCSVN CLSAYRVKMV TSAGVQVQCN SCKTSAIPQY HLAMSDGSIR
610 620 630 640 650
NFCSYSCVVA FQNLFNKPTG MNSSVVPLSQ GQVIVSIPTG STVSAGGGST
660 670 680 690 700
SAVSPTSISS SAAAGLQRLA AQSQHVGFAR SVVKLKCQHC NRLFATKPEL
710 720 730 740 750
LDYKGKMFQF CGKNCSDEYK KINNVMAMCE YCKIEKIVKE TVRFSGADKS
760 770 780 790 800
FCSEGCKLLY KHDLAKRWGN HCKMCSYCLQ TSPKLVQNNL GGKVEEFCCE
810 820 830 840 850
ECMSKYTVLF YQMAKCDACK RQGKLSESLK WRGEMKHFCN LLCILMFCNQ
860 870 880 890 900
QSVCDPPSQN NAANISMVQA ASAGPPSLRK DSTPVIANVV SLASAPAAQP
910 920 930 940 950
TVNSNSVLQG AVPTVTAKII GDASTQTDAL KLPPSQPPRL LKNKALLCKP
960 970 980 990 1000
ITQTKATSCK PHTQNKECQT EDTPSQPQII VVPVPVPVFV PIPLHLYTQY
1010 1020 1030 1040 1050
APVPFGIPVP MPVPMLIPSS MDSEDKVTES IEDIKEKLPT HPFEADLLEM
1060 1070 1080 1090 1100
AEMIAEDEEK KTLSQGESQT SEHELFLDTK IFEKDQGSTY SGDLESEAVS
1110 1120 1130 1140 1150
TPHSWEEELN HYALKSNAVQ EADSELKQFS KGETEQDLEA DFPSDSFDPL
1160 1170 1180 1190 1200
NKGQGIQARS RTRRRHRDGF PQPRRRGRKK SIVAVEPRSL IQGAFQGCSV
1210 1220 1230 1240 1250
SGMTLKYMYG VNAWKNWVQW KNAKEEQGDL KCGGVEQASS SPRSDPLGST
1260 1270 1280 1290 1300
QDHALSQESS EPGCRVRSIK LKEDILSCTF AELSLGLCQF IQEVRRPNGE
1310 1320 1330 1340 1350
KYDPDSILYL CLGIQQYLFE NGRIDNIFTE PYSRFMIELT KLLKIWEPTI
1360 1370 1380 1390 1400
LPNGYMFSRI EEEHLWECKQ LGAYSPIVLL NTLLFFNTKY FQLKNVTEHL
1410 1420 1430 1440 1450
KLSFAHVMRR TRTLKYSTKM TYLRFFPPLQ KQESEPDKLT VGKRKRNEDD
1460 1470 1480 1490 1500
EVPVGVEMAE NTDNPLRCPV RLYEFYLSKC SESVKQRNDV FYLQPERSCV
1510 1520 1530 1540
PNSPMWYSTF PIDPGTLDTM LTRILMVREV HEELAKAKSE DSDVELSD
Length:1,548
Mass (Da):172,788
Last modified:December 7, 2004 - v1
Checksum:i3B5B730EA9B9882B
GO
Isoform 2 (identifier: Q5VZL5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     524-612: Missing.

Note: Gene prediction based on EST data.
Show »
Length:1,459
Mass (Da):163,194
Checksum:iC03E97C233E69C62
GO
Isoform 3 (identifier: Q5VZL5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-324: Missing.

Note: No experimental confirmation available.
Show »
Length:1,224
Mass (Da):136,330
Checksum:i98D348234B1300DE
GO
Isoform 4 (identifier: Q5VZL5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.

Note: No experimental confirmation available.
Show »
Length:1,516
Mass (Da):169,237
Checksum:i707C9F213EEEEE91
GO

Sequence cautioni

The sequence CAI22686.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI22687.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2802AQ → RT in BAA24855 (PubMed:9455477).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti452 – 4521V → I.1 Publication
Corresponds to variant rs34924462 [ dbSNP | Ensembl ].
VAR_034764
Natural varianti1410 – 14101R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035672

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 324324Missing in isoform 3. 1 PublicationVSP_027512Add
BLAST
Alternative sequencei1 – 3232Missing in isoform 4. 1 PublicationVSP_027513Add
BLAST
Alternative sequencei524 – 61289Missing in isoform 2. CuratedVSP_027514Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL160000, AL356362, AL590434 Genomic DNA. Translation: CAH71313.1.
AL590434, AL160000, AL356362 Genomic DNA. Translation: CAI12468.1.
AL356362 Genomic DNA. Translation: CAI22686.1. Sequence problems.
AL356362 Genomic DNA. Translation: CAI22687.1. Sequence problems.
AL356362, AL160000, AL590434 Genomic DNA. Translation: CAI22691.1.
CH471059 Genomic DNA. Translation: EAX07417.1.
BC012093 mRNA. Translation: AAH12093.2.
BC127113 mRNA. Translation: AAI27114.1.
BC127114 mRNA. Translation: AAI27115.1.
AB007885 mRNA. Translation: BAA24855.2.
CCDSiCCDS389.1. [Q5VZL5-1]
PIRiT00059.
RefSeqiNP_005086.2. NM_005095.2. [Q5VZL5-1]
XP_005271388.1. XM_005271331.1. [Q5VZL5-3]
XP_011540725.1. XM_011542423.1. [Q5VZL5-4]
XP_011540726.1. XM_011542424.1. [Q5VZL5-4]
XP_011540727.1. XM_011542425.1. [Q5VZL5-3]
UniGeneiHs.269211.

Genome annotation databases

EnsembliENST00000314607; ENSP00000322915; ENSG00000146463. [Q5VZL5-1]
GeneIDi9202.
KEGGihsa:9202.
UCSCiuc001byt.3. human. [Q5VZL5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL160000, AL356362, AL590434 Genomic DNA. Translation: CAH71313.1.
AL590434, AL160000, AL356362 Genomic DNA. Translation: CAI12468.1.
AL356362 Genomic DNA. Translation: CAI22686.1. Sequence problems.
AL356362 Genomic DNA. Translation: CAI22687.1. Sequence problems.
AL356362, AL160000, AL590434 Genomic DNA. Translation: CAI22691.1.
CH471059 Genomic DNA. Translation: EAX07417.1.
BC012093 mRNA. Translation: AAH12093.2.
BC127113 mRNA. Translation: AAI27114.1.
BC127114 mRNA. Translation: AAI27115.1.
AB007885 mRNA. Translation: BAA24855.2.
CCDSiCCDS389.1. [Q5VZL5-1]
PIRiT00059.
RefSeqiNP_005086.2. NM_005095.2. [Q5VZL5-1]
XP_005271388.1. XM_005271331.1. [Q5VZL5-3]
XP_011540725.1. XM_011542423.1. [Q5VZL5-4]
XP_011540726.1. XM_011542424.1. [Q5VZL5-4]
XP_011540727.1. XM_011542425.1. [Q5VZL5-3]
UniGeneiHs.269211.

3D structure databases

ProteinModelPortaliQ5VZL5.
SMRiQ5VZL5. Positions 338-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114636. 34 interactions.
IntActiQ5VZL5. 20 interactions.
STRINGi9606.ENSP00000322915.

PTM databases

iPTMnetiQ5VZL5.
PhosphoSiteiQ5VZL5.

Polymorphism and mutation databases

BioMutaiZMYM4.
DMDMi74762280.

Proteomic databases

EPDiQ5VZL5.
MaxQBiQ5VZL5.
PaxDbiQ5VZL5.
PRIDEiQ5VZL5.

Protocols and materials databases

DNASUi9202.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314607; ENSP00000322915; ENSG00000146463. [Q5VZL5-1]
GeneIDi9202.
KEGGihsa:9202.
UCSCiuc001byt.3. human. [Q5VZL5-1]

Organism-specific databases

CTDi9202.
GeneCardsiZMYM4.
HGNCiHGNC:13055. ZMYM4.
HPAiHPA051301.
HPA054802.
MIMi613568. gene.
neXtProtiNX_Q5VZL5.
PharmGKBiPA37633.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE8I. Eukaryota.
ENOG410XQR6. LUCA.
GeneTreeiENSGT00550000074408.
HOVERGENiHBG106731.
InParanoidiQ5VZL5.
OMAiDNIFTEP.
OrthoDBiEOG75J0M6.
PhylomeDBiQ5VZL5.
TreeFamiTF336988.

Miscellaneous databases

ChiTaRSiZMYM4. human.
GenomeRNAii9202.
PMAP-CutDBQ5VZL5.
PROiQ5VZL5.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VZL5.
CleanExiHS_ZMYM4.
ExpressionAtlasiQ5VZL5. baseline and differential.
GenevisibleiQ5VZL5. HS.

Family and domain databases

InterProiIPR021893. DUF3504.
IPR011017. TRASH_dom.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF12012. DUF3504. 1 hit.
PF06467. zf-FCS. 5 hits.
[Graphical view]
SMARTiSM00746. TRASH. 10 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 3 AND 4).
    Tissue: Placenta.
  4. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
    Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-1548, VARIANT ILE-452.
    Tissue: Brain.
  5. "Assignment of ZNF262 to human chromosome band 1p34-->p32 by in situ hybridization."
    Sohal J., Chase A., Goldman J.M., Cross N.C.P.
    Cytogenet. Cell Genet. 85:306-307(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "Cloning and mapping of members of the MYM family."
    Smedley D., Hamoudi R., Lu Y.-J., Cooper C., Shipley J.
    Genomics 60:244-247(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27."
    Shchors K., Yehiely F., Kular R.K., Kotlo K.U., Brewer G., Deiss L.P.
    J. Biol. Chem. 277:47061-47072(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF UTR.
  8. "Cell death inhibiting RNA (CDIR) modulates IFN-gamma-stimulated sensitization to Fas/CD95/Apo-1 and TRAIL/Apo-2L-induced apoptosis."
    Shchors K., Yehiely F., Deiss L.P.
    Cell Cycle 3:1606-1611(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF UTR.
  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-122 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 THR-107; SER-110; SER-122 AND SER-1030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-122; SER-1181; SER-1539; SER-1542 AND SER-1547, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250; LYS-273 AND LYS-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149; LYS-250; LYS-273 AND LYS-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250 AND LYS-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-1410.

Entry informationi

Entry nameiZMYM4_HUMAN
AccessioniPrimary (citable) accession number: Q5VZL5
Secondary accession number(s): A0JP19
, A0JP20, O43308, Q5T5E1, Q5T5E2, Q7L3Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 7, 2004
Last modified: June 8, 2016
This is version 112 of the entry and version 1 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

Miscellaneous

The 3'-UTR region of the mRNA encoding this protein contains a motif called CDIR (for cell death inhibiting RNA) that binds HNRPD/AUF1 and HSPB1/HSP27. It is able to inhibit interferon-gamma induced apoptosis.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.