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Protein

Zinc finger CCCH domain-containing protein 14

Gene

ZC3H14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in poly(A) tail length control in neuronal cells. Binds the polyadenosine RNA oligonucleotides.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri595 – 62026C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri621 – 64020C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri641 – 65616C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri682 – 69918C3H1-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri701 – 71919C3H1-type 5PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • poly(A) binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger CCCH domain-containing protein 14
Alternative name(s):
Mammalian suppressor of tau pathology-2
Short name:
MSUT-2
Renal carcinoma antigen NY-REN-37
Gene namesi
Name:ZC3H14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20509. ZC3H14.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

MalaCardsiZC3H14.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA145007270.

Polymorphism and mutation databases

BioMutaiZC3H14.
DMDMi74737935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Zinc finger CCCH domain-containing protein 14PRO_0000331311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei85 – 851PhosphoserineBy similarity
Cross-linki175 – 175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei343 – 3431PhosphoserineCombined sources
Modified residuei357 – 3571N6-acetyllysineCombined sources
Cross-linki413 – 413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei515 – 5151PhosphoserineCombined sources
Modified residuei527 – 5271PhosphoserineBy similarity
Modified residuei620 – 6201PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6PJT7.
MaxQBiQ6PJT7.
PaxDbiQ6PJT7.
PRIDEiQ6PJT7.

PTM databases

iPTMnetiQ6PJT7.
PhosphoSiteiQ6PJT7.

Expressioni

Gene expression databases

BgeeiQ6PJT7.
CleanExiHS_ZC3H14.
ExpressionAtlasiQ6PJT7. baseline and differential.
GenevisibleiQ6PJT7. HS.

Organism-specific databases

HPAiHPA049798.
HPA053510.

Interactioni

Subunit structurei

Interacts with HOOK2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DDIT3P35638-23EBI-740660,EBI-10173632

Protein-protein interaction databases

BioGridi122967. 50 interactions.
IntActiQ6PJT7. 23 interactions.
MINTiMINT-1455250.
STRINGi9606.ENSP00000251038.

Structurei

3D structure databases

ProteinModelPortaliQ6PJT7.
SMRiQ6PJT7. Positions 598-656, 680-718.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ZC3H14 family.Curated
Contains 5 C3H1-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri595 – 62026C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri621 – 64020C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri641 – 65616C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri682 – 69918C3H1-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri701 – 71919C3H1-type 5PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG3702. Eukaryota.
ENOG410YE77. LUCA.
GeneTreeiENSGT00440000038430.
HOGENOMiHOG000074062.
HOVERGENiHBG108760.
InParanoidiQ6PJT7.
OMAiFNHDGEE.
OrthoDBiEOG7JT6VG.
PhylomeDBiQ6PJT7.
TreeFamiTF329509.

Family and domain databases

InterProiIPR000571. Znf_CCCH.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 3 hits.
[Graphical view]
PROSITEiPS50103. ZF_C3H1. 3 hits.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PJT7-1) [UniParc]FASTAAdd to basket

Also known as: Isoform 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.

« Hide

        10         20         30         40         50
MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED
60 70 80 90 100
LSLFLGNNTI RFTVWLHGVL DKLRSVTTEP SSLKSSDTNI FDSNVPSNKS
110 120 130 140 150
NFSRGDERRH EAAVPPLAIP SARPEKRDSR VSTSSQESKT TNVRQTYDDG
160 170 180 190 200
AATRLMSTVK PLREPAPSED VIDIKPEPDD LIDEDLNFVQ ENPLSQKKPT
210 220 230 240 250
VTLTYGSSRP SIEIYRPPAS RNADSGVHLN RLQFQQQQNS IHAAKQLDMQ
260 270 280 290 300
SSWVYETGRL CEPEVLNSLE ETYSPFFRNN SEKMSMEDEN FRKRKLPVVS
310 320 330 340 350
SVVKVKKFNH DGEEEEEDDD YGSRTGSISS SVSVPAKPER RPSLPPSKQA
360 370 380 390 400
NKNLILKAIS EAQESVTKTT NYSTVPQKQT LPVAPRTRTS QEELLAEVVQ
410 420 430 440 450
GQSRTPRISP PIKEEETKGD SVEKNQGTQQ RQLLSRLQID PVMAETLQMS
460 470 480 490 500
QDYYDMESMV HADTRSFILK KPKLSEEVVV APNQESGMKT ADSLRVLSGH
510 520 530 540 550
LMQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEDMC FEGMKPVNQT
560 570 580 590 600
AASNKGLRGL LHPQQLHLLS RQLEDPNGSF SNAEMSELSV AQKPEKLLER
610 620 630 640 650
CKYWPACKNG DECAYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDAKCTKP
660 670 680 690 700
DCPFTHVSRR IPVLSPKPAV APPAPPSSSQ LCRYFPACKK MECPFYHPKH
710 720 730
CRFNTQCTRP DCTFYHPTIN VPPRHALKWI RPQTSE
Length:736
Mass (Da):82,876
Last modified:July 5, 2004 - v1
Checksum:iBCF3E36CBA66170A
GO
Isoform 2 (identifier: Q6PJT7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     669-669: Missing.

Show »
Length:735
Mass (Da):82,805
Checksum:i23DE4F1ECFAB49DE
GO
Isoform 3 (identifier: Q6PJT7-3) [UniParc]FASTAAdd to basket

Also known as: Isoform 2

The sequence of this isoform differs from the canonical sequence as follows:
     427-582: Missing.
     669-669: Missing.

Show »
Length:579
Mass (Da):65,425
Checksum:i9F97392E74A1F612
GO
Isoform 4 (identifier: Q6PJT7-4) [UniParc]FASTAAdd to basket

Also known as: Isoform 3 short

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.
     452-582: Missing.

Show »
Length:571
Mass (Da):64,502
Checksum:i95D7DEA373BCA94B
GO
Isoform 5 (identifier: Q6PJT7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     427-451: Missing.

Show »
Length:711
Mass (Da):80,021
Checksum:i9D8B3AF17DC0FB13
GO
Isoform 6 (identifier: Q6PJT7-6) [UniParc]FASTAAdd to basket

Also known as: Isoform 4

The sequence of this isoform differs from the canonical sequence as follows:
     1-298: Missing.
     299-426: VSSVVKVKKF...TKGDSVEKNQ → MRMSSKFPSP...IIGFLRNVEK
     452-582: Missing.
     669-669: Missing.

Show »
Length:306
Mass (Da):34,867
Checksum:i6122BC10CFCE1D25
GO
Isoform 8 (identifier: Q6PJT7-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-454: Missing.
     455-582: DMESMVHADT...LEDPNGSFSN → MRMSSKFPSP...IIGFLRNVEK

Show »
Length:282
Mass (Da):32,084
Checksum:iD32BB78C85628238
GO
Isoform 9 (identifier: Q6PJT7-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     577-581: Missing.
     669-669: Missing.

Note: No experimental confirmation available.
Show »
Length:730
Mass (Da):82,312
Checksum:i667DAF346CBEB6A4
GO
Isoform 10 (identifier: Q6PJT7-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-159: Missing.
     427-582: Missing.

Note: No experimental confirmation available.
Show »
Length:543
Mass (Da):61,354
Checksum:i1FC746F7E0BB614C
GO
Isoform 11 (identifier: Q6PJT7-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-113: Missing.
     452-582: Missing.
     669-669: Missing.

Note: No experimental confirmation available.
Show »
Length:585
Mass (Da):66,140
Checksum:iE62A6DB4F267FEEE
GO

Sequence cautioni

The sequence AAL83289.1 differs from that shown.Several sequencing errors.Curated
The sequence AAS90302.1 differs from that shown.Aberrant splicing.Curated
The sequence AAS90302.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AK021868 differs from that shown. Reason: Frameshift at position 199. Curated
The sequence CAE45933.1 differs from that shown.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131A → V in BAG63510 (PubMed:14702039).Curated
Sequence conflicti323 – 3231S → P in BAG64229 (PubMed:14702039).Curated
Sequence conflicti532 – 5321M → V in BAG65136 (PubMed:14702039).Curated
Sequence conflicti674 – 6741A → V in AAH23641 (PubMed:15489334).Curated
Sequence conflicti712 – 7121C → F in AAS90302 (Ref. 2) Curated
Sequence conflicti712 – 7121C → F in CAE45933 (PubMed:17974005).Curated
Sequence conflicti718 – 7181T → P in BAG65136 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 454454Missing in isoform 8. 1 PublicationVSP_033162Add
BLAST
Alternative sequencei1 – 298298Missing in isoform 6. 1 PublicationVSP_033163Add
BLAST
Alternative sequencei1 – 3434Missing in isoform 4. 2 PublicationsVSP_033164Add
BLAST
Alternative sequencei95 – 11319Missing in isoform 11. 1 PublicationVSP_055096Add
BLAST
Alternative sequencei123 – 15937Missing in isoform 10. 1 PublicationVSP_055097Add
BLAST
Alternative sequencei299 – 426128VSSVV…VEKNQ → MRMSSKFPSPPLPIFLPPEP VDLGSITSSSCSLNELDNIS HLLRKISADINEIKGMKAAI LTVEANLFDLNVRVSKNEAK ISSLEVKMNEYSTTYECNRQ FEDQEEDTESQSRTTDVKII GFLRNVEK in isoform 6. 1 PublicationVSP_033165Add
BLAST
Alternative sequencei427 – 582156Missing in isoform 3 and isoform 10. 2 PublicationsVSP_033166Add
BLAST
Alternative sequencei427 – 45125Missing in isoform 5. 1 PublicationVSP_033167Add
BLAST
Alternative sequencei452 – 582131Missing in isoform 4, isoform 6 and isoform 11. 4 PublicationsVSP_033168Add
BLAST
Alternative sequencei455 – 582128DMESM…GSFSN → MRMSSKFPSPPLPIFLPPEP VDLGSITSSSCSLNELDNIS HLLRKISADINEIKGMKAAI LTVEANLFDLNVRVSKNEAK ISSLEVKMNEYSTTYECNRQ FEDQEEDTESQSRTTDVKII GFLRNVEK in isoform 8. 1 PublicationVSP_033169Add
BLAST
Alternative sequencei577 – 5815Missing in isoform 9. 1 PublicationVSP_044645
Alternative sequencei669 – 6691Missing in isoform 2, isoform 3, isoform 6, isoform 9 and isoform 11. 5 PublicationsVSP_033171

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF474376 mRNA. Translation: AAL83289.1. Sequence problems.
AY578060 mRNA. Translation: AAS90299.1.
AY578061 mRNA. Translation: AAS90300.1.
AY578062 mRNA. Translation: AAS90301.1.
AY578063 mRNA. Translation: AAS90302.1. Sequence problems.
AK021868 mRNA. No translation available.
AK302136 mRNA. Translation: BAG63510.1.
AK303123 mRNA. Translation: BAG64229.1.
AK304275 mRNA. Translation: BAG65136.1.
AL834215 mRNA. Translation: CAD38897.1.
BX640716 mRNA. Translation: CAE45835.1.
BX640876 mRNA. Translation: CAE45933.1. Sequence problems.
AL162171 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81385.1.
CH471061 Genomic DNA. Translation: EAW81388.1.
CH471061 Genomic DNA. Translation: EAW81389.1.
CH471061 Genomic DNA. Translation: EAW81390.1.
BC011793 mRNA. Translation: AAH11793.1.
BC023641 mRNA. Translation: AAH23641.1.
BC027607 mRNA. Translation: AAH27607.1.
BX248265 mRNA. Translation: CAD62593.1.
BX248281 mRNA. Translation: CAD62609.1.
BX248769 mRNA. Translation: CAD66576.1.
AF155107 mRNA. Translation: AAD42873.1.
CCDSiCCDS32133.1. [Q6PJT7-1]
CCDS32134.1. [Q6PJT7-3]
CCDS32135.1. [Q6PJT7-4]
CCDS32136.1. [Q6PJT7-6]
CCDS55938.1. [Q6PJT7-9]
RefSeqiNP_001153575.1. NM_001160103.1. [Q6PJT7-2]
NP_001153576.1. NM_001160104.1. [Q6PJT7-9]
NP_079100.2. NM_024824.4. [Q6PJT7-1]
NP_997543.1. NM_207660.3. [Q6PJT7-3]
NP_997544.1. NM_207661.2. [Q6PJT7-4]
NP_997545.2. NM_207662.3. [Q6PJT7-6]
XP_005268125.1. XM_005268068.3. [Q6PJT7-5]
UniGeneiHs.686171.

Genome annotation databases

EnsembliENST00000251038; ENSP00000251038; ENSG00000100722. [Q6PJT7-1]
ENST00000302216; ENSP00000307025; ENSG00000100722. [Q6PJT7-3]
ENST00000318308; ENSP00000327176; ENSG00000100722. [Q6PJT7-6]
ENST00000336693; ENSP00000338002; ENSG00000100722. [Q6PJT7-4]
ENST00000393514; ENSP00000377150; ENSG00000100722. [Q6PJT7-5]
ENST00000406216; ENSP00000384682; ENSG00000100722. [Q6PJT7-8]
ENST00000555755; ENSP00000452475; ENSG00000100722. [Q6PJT7-9]
GeneIDi79882.
KEGGihsa:79882.
UCSCiuc001xww.4. human. [Q6PJT7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF474376 mRNA. Translation: AAL83289.1. Sequence problems.
AY578060 mRNA. Translation: AAS90299.1.
AY578061 mRNA. Translation: AAS90300.1.
AY578062 mRNA. Translation: AAS90301.1.
AY578063 mRNA. Translation: AAS90302.1. Sequence problems.
AK021868 mRNA. No translation available.
AK302136 mRNA. Translation: BAG63510.1.
AK303123 mRNA. Translation: BAG64229.1.
AK304275 mRNA. Translation: BAG65136.1.
AL834215 mRNA. Translation: CAD38897.1.
BX640716 mRNA. Translation: CAE45835.1.
BX640876 mRNA. Translation: CAE45933.1. Sequence problems.
AL162171 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81385.1.
CH471061 Genomic DNA. Translation: EAW81388.1.
CH471061 Genomic DNA. Translation: EAW81389.1.
CH471061 Genomic DNA. Translation: EAW81390.1.
BC011793 mRNA. Translation: AAH11793.1.
BC023641 mRNA. Translation: AAH23641.1.
BC027607 mRNA. Translation: AAH27607.1.
BX248265 mRNA. Translation: CAD62593.1.
BX248281 mRNA. Translation: CAD62609.1.
BX248769 mRNA. Translation: CAD66576.1.
AF155107 mRNA. Translation: AAD42873.1.
CCDSiCCDS32133.1. [Q6PJT7-1]
CCDS32134.1. [Q6PJT7-3]
CCDS32135.1. [Q6PJT7-4]
CCDS32136.1. [Q6PJT7-6]
CCDS55938.1. [Q6PJT7-9]
RefSeqiNP_001153575.1. NM_001160103.1. [Q6PJT7-2]
NP_001153576.1. NM_001160104.1. [Q6PJT7-9]
NP_079100.2. NM_024824.4. [Q6PJT7-1]
NP_997543.1. NM_207660.3. [Q6PJT7-3]
NP_997544.1. NM_207661.2. [Q6PJT7-4]
NP_997545.2. NM_207662.3. [Q6PJT7-6]
XP_005268125.1. XM_005268068.3. [Q6PJT7-5]
UniGeneiHs.686171.

3D structure databases

ProteinModelPortaliQ6PJT7.
SMRiQ6PJT7. Positions 598-656, 680-718.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122967. 50 interactions.
IntActiQ6PJT7. 23 interactions.
MINTiMINT-1455250.
STRINGi9606.ENSP00000251038.

PTM databases

iPTMnetiQ6PJT7.
PhosphoSiteiQ6PJT7.

Polymorphism and mutation databases

BioMutaiZC3H14.
DMDMi74737935.

Proteomic databases

EPDiQ6PJT7.
MaxQBiQ6PJT7.
PaxDbiQ6PJT7.
PRIDEiQ6PJT7.

Protocols and materials databases

DNASUi79882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251038; ENSP00000251038; ENSG00000100722. [Q6PJT7-1]
ENST00000302216; ENSP00000307025; ENSG00000100722. [Q6PJT7-3]
ENST00000318308; ENSP00000327176; ENSG00000100722. [Q6PJT7-6]
ENST00000336693; ENSP00000338002; ENSG00000100722. [Q6PJT7-4]
ENST00000393514; ENSP00000377150; ENSG00000100722. [Q6PJT7-5]
ENST00000406216; ENSP00000384682; ENSG00000100722. [Q6PJT7-8]
ENST00000555755; ENSP00000452475; ENSG00000100722. [Q6PJT7-9]
GeneIDi79882.
KEGGihsa:79882.
UCSCiuc001xww.4. human. [Q6PJT7-1]

Organism-specific databases

CTDi79882.
GeneCardsiZC3H14.
HGNCiHGNC:20509. ZC3H14.
HPAiHPA049798.
HPA053510.
MalaCardsiZC3H14.
MIMi613279. gene.
neXtProtiNX_Q6PJT7.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA145007270.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3702. Eukaryota.
ENOG410YE77. LUCA.
GeneTreeiENSGT00440000038430.
HOGENOMiHOG000074062.
HOVERGENiHBG108760.
InParanoidiQ6PJT7.
OMAiFNHDGEE.
OrthoDBiEOG7JT6VG.
PhylomeDBiQ6PJT7.
TreeFamiTF329509.

Miscellaneous databases

ChiTaRSiZC3H14. human.
GenomeRNAii79882.
PROiQ6PJT7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PJT7.
CleanExiHS_ZC3H14.
ExpressionAtlasiQ6PJT7. baseline and differential.
GenevisibleiQ6PJT7. HS.

Family and domain databases

InterProiIPR000571. Znf_CCCH.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 3 hits.
[Graphical view]
PROSITEiPS50103. ZF_C3H1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Guo J.H.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
  2. "Homo sapiens putative NY-REN-37 antigen alternatively spliced isoforms."
    Zhou G., Wang X., Yu L.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9; 10 AND 11).
    Tissue: Embryo, Testis, Thymus and Trachea.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Esophageal carcinoma and Testis.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-736 (ISOFORM 2).
    Tissue: Muscle, Skin and Testis.
  8. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-736 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-736 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 630-736 (ISOFORM 1).
    Tissue: Neuroblastoma and Placenta.
  9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 563-736 (ISOFORM 2), IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  10. "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-515 AND SER-620, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Splice variants of the human ZC3H14 gene generate multiple isoforms of a zinc finger polyadenosine RNA binding protein."
    Leung S.W., Apponi L.H., Cornejo O.E., Kitchen C.M., Valentini S.R., Pavlath G.K., Dunham C.M., Corbett A.H.
    Gene 439:71-78(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
  16. "SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans."
    Guthrie C.R., Schellenberg G.D., Kraemer B.C.
    Hum. Mol. Genet. 18:1825-1838(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOOK2.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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 SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "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-175 AND LYS-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "A conserved role for the zinc finger polyadenosine RNA binding protein, ZC3H14, in control of poly(A) tail length."
    Kelly S.M., Leung S.W., Pak C., Banerjee A., Moberg K.H., Corbett A.H.
    RNA 20:681-688(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MISCELLANEOUS, SUBCELLULAR LOCATION.
  26. "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-175 AND LYS-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZC3HE_HUMAN
AccessioniPrimary (citable) accession number: Q6PJT7
Secondary accession number(s): A8MY46
, B4DXU8, B4DZW7, B4E2H4, G3V5R4, Q6MZU4, Q6PJ32, Q6PUI6, Q6PUI8, Q86TQ5, Q86TW0, Q86TW1, Q8NCT6, Q8NCZ3, Q8TDE2, Q9HAC9, Q9Y5A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 124 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

ZC3H14 can functionally substitute for Nab2 in fly neurons and can rescue defects in development and locomotion that are present in dNab2 null flies.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

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.