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Protein

Zinc finger protein 512

Gene

Znf512

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in transcriptional regulation.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri200 – 22324C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri290 – 31324C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri442 – 46524C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 512
Gene namesi
Name:Znf512
Synonyms:Kiaa1805, Zfp512
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1917345. Zfp512.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 562562Zinc finger protein 512PRO_0000333737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki335 – 335Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ69Z99.
MaxQBiQ69Z99.
PaxDbiQ69Z99.
PeptideAtlasiQ69Z99.
PRIDEiQ69Z99.

PTM databases

iPTMnetiQ69Z99.
PhosphoSiteiQ69Z99.

Expressioni

Gene expression databases

BgeeiQ69Z99.
ExpressionAtlasiQ69Z99. baseline and differential.
GenevisibleiQ69Z99. MM.

Interactioni

Protein-protein interaction databases

BioGridi234688. 2 interactions.
IntActiQ69Z99. 3 interactions.
MINTiMINT-4110900.
STRINGi10090.ENSMUSP00000075613.

Structurei

3D structure databases

ProteinModelPortaliQ69Z99.
SMRiQ69Z99. Positions 145-227, 251-276, 283-321, 408-434, 440-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri200 – 22324C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri290 – 31324C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri442 – 46524C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00490000043365.
HOGENOMiHOG000070082.
HOVERGENiHBG054123.
InParanoidiQ69Z99.
OMAiGPTSFKQ.
OrthoDBiEOG7T1R9K.
PhylomeDBiQ69Z99.
TreeFamiTF331185.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q69Z99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRLGAVTA TPGPTSLKQQ RSTRIVGAKN NRAQCSIKDN SFQYTIPHED
60 70 80 90 100
SLSGSSSASS CEPVSDFTAT LRKSTYWMKM RRIKPAATSQ VEGAGEKEKE
110 120 130 140 150
RAKGKRNVKQ EEDEDYRELP QKKHKLYGRK QRPKAQPHPK PQARRVRKEP
160 170 180 190 200
PVYAAGSMEE KWYLEIMDKG SVSCPTCQAV GRKTIEGLKK HMENCKQEMF
210 220 230 240 250
TCHHCGKQLH SLAGMKYHVM ANHNSLPILK AGDEVDEPSE RERLRTVLKR
260 270 280 290 300
MGKLRCMRES CSSTFTSIMG YLYHVRKCGK EASELEKLAL KCHHCGKPYR
310 320 330 340 350
SKAGLAYHMR SEHGPVFFPE SEQPDCLKEM SLEAKGGGRV QRRSAKIAVY
360 370 380 390 400
HLQELASAEL TKEWPKRKVL QDLVPDDRKL KYTRPGLPTF SQEVLHKWKT
410 420 430 440 450
DIKKYHRIQC PNQGCEAVYS SVSGLKAHLG SCTLGTFVAG KYKCLLCEKE
460 470 480 490 500
FVSESGVKYH INSVHAEDWF VVNPTTTKSF EKLMKIKQRQ QEEEKQRQQH
510 520 530 540 550
GRRRSLRRQQ QPCMEPPESQ LEPKAGKEQG GNEELVGPDP EPVPAQPQKA
560
EPAKTTHKRG RK
Length:562
Mass (Da):63,908
Last modified:May 20, 2008 - v2
Checksum:iDB522267A7113189
GO

Sequence cautioni

The sequence BAD32545.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811R → G in BAE32924 (PubMed:16141072).Curated
Sequence conflicti117 – 1171R → G in BAC39137 (PubMed:16141072).Curated
Sequence conflicti196 – 1961K → E in BAE29168 (PubMed:16141072).Curated
Sequence conflicti310 – 3101R → G in BAE32924 (PubMed:16141072).Curated
Sequence conflicti347 – 3471I → M in BAC39137 (PubMed:16141072).Curated
Sequence conflicti454 – 4541E → K in BAE27105 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173267 mRNA. Translation: BAD32545.1. Different initiation.
AK084205 mRNA. Translation: BAC39137.1.
AK146353 mRNA. Translation: BAE27105.1.
AK149921 mRNA. Translation: BAE29168.1.
AK154918 mRNA. Translation: BAE32924.1.
BC089160 mRNA. Translation: AAH89160.1.
CCDSiCCDS19183.1.
RefSeqiNP_766581.2. NM_172993.3.
UniGeneiMm.259127.

Genome annotation databases

EnsembliENSMUST00000076264; ENSMUSP00000075613; ENSMUSG00000062761.
GeneIDi269639.
KEGGimmu:269639.
UCSCiuc008wyg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173267 mRNA. Translation: BAD32545.1. Different initiation.
AK084205 mRNA. Translation: BAC39137.1.
AK146353 mRNA. Translation: BAE27105.1.
AK149921 mRNA. Translation: BAE29168.1.
AK154918 mRNA. Translation: BAE32924.1.
BC089160 mRNA. Translation: AAH89160.1.
CCDSiCCDS19183.1.
RefSeqiNP_766581.2. NM_172993.3.
UniGeneiMm.259127.

3D structure databases

ProteinModelPortaliQ69Z99.
SMRiQ69Z99. Positions 145-227, 251-276, 283-321, 408-434, 440-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234688. 2 interactions.
IntActiQ69Z99. 3 interactions.
MINTiMINT-4110900.
STRINGi10090.ENSMUSP00000075613.

PTM databases

iPTMnetiQ69Z99.
PhosphoSiteiQ69Z99.

Proteomic databases

EPDiQ69Z99.
MaxQBiQ69Z99.
PaxDbiQ69Z99.
PeptideAtlasiQ69Z99.
PRIDEiQ69Z99.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000076264; ENSMUSP00000075613; ENSMUSG00000062761.
GeneIDi269639.
KEGGimmu:269639.
UCSCiuc008wyg.2. mouse.

Organism-specific databases

CTDi269639.
MGIiMGI:1917345. Zfp512.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00490000043365.
HOGENOMiHOG000070082.
HOVERGENiHBG054123.
InParanoidiQ69Z99.
OMAiGPTSFKQ.
OrthoDBiEOG7T1R9K.
PhylomeDBiQ69Z99.
TreeFamiTF331185.

Miscellaneous databases

PROiQ69Z99.
SOURCEiSearch...

Gene expression databases

BgeeiQ69Z99.
ExpressionAtlasiQ69Z99. baseline and differential.
GenevisibleiQ69Z99. MM.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic intestine.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ, C57BL/6J and NOD.
    Tissue: Bone marrow and Eye.
  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].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiZN512_MOUSE
AccessioniPrimary (citable) accession number: Q69Z99
Secondary accession number(s): Q3U365
, Q3UDU3, Q3UJQ0, Q5FWY0, Q8BJF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: July 6, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.