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Q14966 (ZN638_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein 638
Alternative name(s):
Cutaneous T-cell lymphoma-associated antigen se33-1
Short name=CTCL-associated antigen se33-1
Nuclear protein 220
Zinc finger matrin-like protein
Gene names
Name:ZNF638
Synonyms:NP220, ZFML
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1978 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Early regulator of adipogenesis that works as a transcription cofactor of CEBPs, controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 By similarity. Binds to cytidine clusters in double-stranded DNA. Ref.1

Subunit structure

Interacts with FHL2. Interacts with CEBPA, CEBPD and CEBPG By similarity. Ref.7

Subcellular location

Nucleus speckle Ref.1 Ref.7.

Miscellaneous

Isoform 5 is a tumor-associated antigen found in several cutaneous T-cell lymphoma (CTCL), and in particular in mycosis fungoides patients and in Sezary syndrome patients.

Sequence similarities

Contains 1 matrin-type zinc finger.

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAH64530.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q14966-1)

Also known as: Alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14966-2)

The sequence of this isoform differs from the canonical sequence as follows:
     793-814: AKTGQAKASVAKVNKSTGKSAS → GLLPTGGGNNYPQIVLAPGLCH
     815-1978: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q14966-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1918-1938: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q14966-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1139: SPGLKNSPID...ESTPSIQTET → RLWLSKTLRI...WMNLLLWMRL
     1140-1978: Missing.
Isoform 5 (identifier: Q14966-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-903: Missing.
Note: Broadly expressed.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19781978Zinc finger protein 638
PRO_0000082011

Regions

Domain676 – 75176RRM 1
Domain905 – 97975RRM 2
DNA binding1353 – 1477125 Ref.1
Zinc finger1928 – 195831Matrin-type
Compositional bias472 – 574103Arg-rich
Compositional bias1087 – 1355269Glu-rich
Compositional bias1580 – 15856Poly-Lys

Amino acid modifications

Modified residue1281Phosphoserine Ref.9 Ref.12 Ref.13 Ref.15 Ref.16
Modified residue3831Phosphoserine Ref.13 Ref.16
Modified residue4201Phosphoserine Ref.13
Modified residue5521Phosphoserine Ref.8 Ref.16
Modified residue6051Phosphoserine Ref.10
Modified residue6141Phosphoserine Ref.13
Modified residue11001Phosphoserine Ref.15
Modified residue14011Phosphoserine Ref.13 Ref.18
Modified residue16671Phosphoserine Ref.16
Modified residue18821Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 903903Missing in isoform 5.
VSP_014801
Alternative sequence793 – 81422AKTGQ…GKSAS → GLLPTGGGNNYPQIVLAPGL CH in isoform 2.
VSP_014802
Alternative sequence815 – 19781164Missing in isoform 2.
VSP_014803
Alternative sequence1100 – 113940SPGLK…IQTET → RLWLSKTLRILKALLVEVPN LKRSHYFHLIWMNLLLWMRL in isoform 4.
VSP_014804
Alternative sequence1140 – 1978839Missing in isoform 4.
VSP_014805
Alternative sequence1918 – 193821Missing in isoform 3.
VSP_014806
Natural variant1101I → V. Ref.4
Corresponds to variant rs12612365 [ dbSNP | Ensembl ].
VAR_023069
Natural variant9801N → S. Ref.2
Corresponds to variant rs3732235 [ dbSNP | Ensembl ].
VAR_023070
Natural variant14621S → N.
Corresponds to variant rs10427371 [ dbSNP | Ensembl ].
VAR_052238
Natural variant17261V → M. Ref.4
Corresponds to variant rs1804020 [ dbSNP | Ensembl ].
VAR_023071
Natural variant19121A → V. Ref.2
Corresponds to variant rs11542286 [ dbSNP | Ensembl ].
VAR_023072

Experimental info

Sequence conflict581H → L in BAA11748. Ref.1
Sequence conflict2091I → V in AAM97681. Ref.3
Sequence conflict2621M → I in CAD97667. Ref.4
Sequence conflict5991A → V in CAH18177. Ref.4
Sequence conflict8011S → C in BAA11748. Ref.1
Sequence conflict9771A → D in CAD97667. Ref.4
Sequence conflict12051F → L in CAD97667. Ref.4
Sequence conflict12431S → P in CAD97667. Ref.4
Sequence conflict13361G → S in CAH18177. Ref.4
Sequence conflict14041A → T in CAD97667. Ref.4
Sequence conflict17141T → I Ref.1
Sequence conflict17141T → I Ref.2

Sequences

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

Last modified July 19, 2005. Version 2.
Checksum: FC006A4BA4885455

FASTA1,978220,625
        10         20         30         40         50         60 
MSRPRFNPRG DFPLQRPRAP NPSGMRPPGP FMRPGSMGLP RFYPAGRARG IPHRFAGHES 

        70         80         90        100        110        120 
YQNMGPQRMN VQVTQHRTDP RLTKEKLDFH EAQQKKGKPH GSRWDDEPHI SASVAVKQSS 

       130        140        150        160        170        180 
VTQVTEQSPK VQSRYTKESA SSILASFGLS NEDLEELSRY PDEQLTPENM PLILRDIRMR 

       190        200        210        220        230        240 
KMGRRLPNLP SQSRNKETLG SEAVSSNVID YGHASKYGYT EDPLEVRIYD PEIPTDEVEN 

       250        260        270        280        290        300 
EFQSQQNISA SVPNPNVICN SMFPVEDVFR QMDFPGESSN NRSFFSVESG TKMSGLHISG 

       310        320        330        340        350        360 
GQSVLEPIKS VNQSINQTVS QTMSQSLIPP SMNQQPFSSE LISSVSQQER IPHEPVINSS 

       370        380        390        400        410        420 
NVHVGSRGSK KNYQSQADIP IRSPFGIVKA SWLPKFSHAD AQKMKRLPTP SMMNDYYAAS 

       430        440        450        460        470        480 
PRIFPHLCSL CNVECSHLKD WIQHQNTSTH IESCRQLRQQ YPDWNPEILP SRRNEGNRKE 

       490        500        510        520        530        540 
NETPRRRSHS PSPRRSRRSS SSHRFRRSRS PMHYMYRPRS RSPRICHRFI SRYRSRSRSR 

       550        560        570        580        590        600 
SPYRIRNPFR GSPKCFRSVS PERMSRRSVR SSDRKKALED VVQRSGHGTE FNKQKHLEAA 

       610        620        630        640        650        660 
DKGHSPAQKP KTSSGTKPSV KPTSATKSDS NLGGHSIRCK SKNLEDDTLS ECKQVSDKAV 

       670        680        690        700        710        720 
SLQRKLRKEQ SLHYGSVLLI TELPEDGCTE EDVRKLFQPF GKVNDVLIVP YRKEAYLEME 

       730        740        750        760        770        780 
FKEAITAIMK YIETTPLTIK GKSVKICVPG KKKAQNKEVK KKTLESKKVS ASTLKRDADA 

       790        800        810        820        830        840 
SKAVEIVTST SAAKTGQAKA SVAKVNKSTG KSASSVKSVV TVAVKGNKAS IKTAKSGGKK 

       850        860        870        880        890        900 
SLEAKKTGNV KNKDSNKPVT IPENSEIKTS IEVKATENCA KEAISDAALE ATENEPLNKE 

       910        920        930        940        950        960 
TEEMCVMLVS NLPNKGYSVE EVYDLAKPFG GLKDILILSS HKKAYIEINR KAAESMVKFY 

       970        980        990       1000       1010       1020 
TCFPVLMDGN QLSISMAPEN MNIKDEEAIF ITLVKENDPE ANIDTIYDRF VHLDNLPEDG 

      1030       1040       1050       1060       1070       1080 
LQCVLCVGLQ FGKVDHHVFI SNRNKAILQL DSPESAQSMY SFLKQNPQNI GDHMLTCSLS 

      1090       1100       1110       1120       1130       1140 
PKIDLPEVQI EHDPELEKES PGLKNSPIDE SEVQTATDSP SVKPNELEEE STPSIQTETL 

      1150       1160       1170       1180       1190       1200 
VQQEEPCEEE AEKATCDSDF AVETLELETQ GEEVKEEIPL VASASVSIEQ FTENAEECAL 

      1210       1220       1230       1240       1250       1260 
NQQMFNSDLE KKGAEIINPK TALLPSDSVF AEERNLKGIL EESPSEAEDF ISGITQTMVE 

      1270       1280       1290       1300       1310       1320 
AVAEVEKNET VSEILPSTCI VTLVPGIPTG DEKTVDKKNI SEKKGNMDEK EEKEFNTKET 

      1330       1340       1350       1360       1370       1380 
RMDLQIGTEK AEKNEGRMDA EKVEKMAAMK EKPAENTLFK AYPNKGVGQA NKPDETSKTS 

      1390       1400       1410       1420       1430       1440 
ILAVSDVSSS KPSIKAVIVS SPKAKATVSK TENQKSFPKS VPRDQINAEK KLSAKEFGLL 

      1450       1460       1470       1480       1490       1500 
KPTSARSGLA ESSSKFKPTQ SSLTRGGSGR ISALQGKLSK LDYRDITKQS QETEARPSIM 

      1510       1520       1530       1540       1550       1560 
KRDDSNNKTL AEQNTKNPKS TTGRSSKSKE EPLFPFNLDE FVTVDEVIEE VNPSQAKQNP 

      1570       1580       1590       1600       1610       1620 
LKGKRKETLK NVPFSELNLK KKKGKTSTPR GVEGELSFVT LDEIGEEEDA AAHLAQALVT 

      1630       1640       1650       1660       1670       1680 
VDEVIDEEEL NMEEMVKNSN SLFTLDELID QDDCISHSEP KDVTVLSVAE EQDLLKQERL 

      1690       1700       1710       1720       1730       1740 
VTVDEIGEVE ELPLNESADI TFATLNTKGN EGDTVRDSIG FISSQVPEDP STLVTVDEIQ 

      1750       1760       1770       1780       1790       1800 
DDSSDLHLVT LDEVTEEDED SLADFNNLKE ELNFVTVDEV GEEEDGDNDL KVELAQSKND 

      1810       1820       1830       1840       1850       1860 
HPTDKKGNRK KRAVDTKKTK LESLSQVGPV NENVMEEDLK TMIERHLTAK TPTKRVRIGK 

      1870       1880       1890       1900       1910       1920 
TLPSEKAVVT EPAKGEEAFQ MSEVDEESGL KDSEPERKRK KTEDSSSGKS VASDVPEELD 

      1930       1940       1950       1960       1970 
FLVPKAGFFC PICSLFYSGE KAMTNHCKST RHKQNTEKFM AKQRKEKEQN EAEERSSR 

« Hide

Isoform 2 [UniParc].

Checksum: D3DEC862617E65FF
Show »

FASTA81492,052
Isoform 3 [UniParc].

Checksum: 7BFD62828B7911B8
Show »

FASTA1,957218,246
Isoform 4 [UniParc].

Checksum: BD7EAA34D634A34D
Show »

FASTA1,139128,489
Isoform 5 [UniParc].

Checksum: 8927B07C562F396B
Show »

FASTA1,075119,295

References

« Hide 'large scale' references
[1]"A large DNA-binding nuclear protein with RNA recognition motif and serine/arginine-rich domain."
Inagaki H., Matsushima Y., Nakamura K., Ohshima M., Kadowaki T., Kitagawa Y.
J. Biol. Chem. 271:12525-12531(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, SUBCELLULAR LOCATION, FUNCTION.
Tissue: Epithelium.
[2]"Serological detection of cutaneous T-cell lymphoma-associated antigens."
Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.
Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN, VARIANTS SER-980 AND VAL-1912.
Tissue: Testis.
[3]"Identification of a variant splice form of human nuclear protein NP220 mRNA encoding an isoform with truncated carboxyl-terminal."
Chan C.W., Tsui S.K.W., Fung K.P., Lee C.Y., Waye M.M.Y.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Testis.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-110 AND MET-1726.
Tissue: Cervix and Testis.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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; 2 AND 3).
Tissue: Cerebellum, Skin and Testis.
[7]"Interaction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220."
Ng E.K.O., Chan K.K., Wong C.H., Tsui S.K.W., Ngai S.M., Lee S.M.Y., Kotaka M., Lee C.Y., Waye M.M.Y., Fung K.P.
J. Cell. Biochem. 84:556-566(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FHL2.
[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-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"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-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-383; SER-420; SER-614; SER-1401 AND SER-1882, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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-128 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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-128; SER-383; SER-552 AND SER-1667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-1401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D83032 mRNA. Translation: BAA11748.1.
AF273049 mRNA. Translation: AAG34909.1.
AF534078 mRNA. Translation: AAM97681.1.
BX537425 mRNA. Translation: CAD97667.1.
CR749322 mRNA. Translation: CAH18177.1.
AC007878 Genomic DNA. Translation: AAF66079.1.
AC096569 Genomic DNA. Translation: AAY14979.1.
AC104084 Genomic DNA. No translation available.
AC109343 Genomic DNA. No translation available.
BC024000 mRNA. Translation: AAH24000.1.
BC064530 mRNA. Translation: AAH64530.1. Sequence problems.
BC083513 mRNA. Translation: AAH83513.1.
BC143728 mRNA. Translation: AAI43729.1.
PIRJU0239.
JU0240.
RefSeqNP_001014972.1. NM_001014972.2.
NP_001239541.1. NM_001252612.1.
NP_001239542.1. NM_001252613.1.
NP_055312.2. NM_014497.4.
UniGeneHs.434401.
Hs.732823.

3D structure databases

ProteinModelPortalQ14966.
SMRQ14966. Positions 674-749.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118145. 26 interactions.
DIPDIP-42386N.
IntActQ14966. 20 interactions.
MINTMINT-1439144.

PTM databases

PhosphoSiteQ14966.

Polymorphism databases

DMDM71153483.

Proteomic databases

PaxDbQ14966.
PRIDEQ14966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264447; ENSP00000264447; ENSG00000075292. [Q14966-1]
ENST00000355812; ENSP00000348066; ENSG00000075292. [Q14966-4]
ENST00000377802; ENSP00000367033; ENSG00000075292. [Q14966-2]
ENST00000409544; ENSP00000386433; ENSG00000075292. [Q14966-1]
GeneID27332.
KEGGhsa:27332.
UCSCuc002shw.3. human. [Q14966-2]
uc002shx.3. human. [Q14966-1]
uc002shz.3. human. [Q14966-3]
uc002sib.1. human. [Q14966-4]

Organism-specific databases

CTD27332.
GeneCardsGC02P071412.
HGNCHGNC:17894. ZNF638.
HPAHPA036784.
MIM614349. gene.
neXtProtNX_Q14966.
PharmGKBPA134983478.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45231.
HOVERGENHBG094186.
InParanoidQ14966.
OMAVDKHETV.
PhylomeDBQ14966.
TreeFamTF333921.

Gene expression databases

ArrayExpressQ14966.
BgeeQ14966.
CleanExHS_ZNF638.
GenevestigatorQ14966.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 2 hits.
SM00451. ZnF_U1. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZNF638. human.
GeneWikiZNF638.
GenomeRNAi27332.
NextBio50376.
PROQ14966.
SOURCESearch...

Entry information

Entry nameZN638_HUMAN
AccessionPrimary (citable) accession number: Q14966
Secondary accession number(s): B5MDV1 expand/collapse secondary AC list , B7ZLD1, Q53R34, Q5XJ05, Q68DP3, Q6P2H2, Q7Z3T7, Q8NF92, Q8TCA1, Q9H2G1, Q9NP37
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM