Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc finger protein 510

Gene

ZNF510

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri254 – 27623C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri404 – 42623C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri432 – 45423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri460 – 48223C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri488 – 51023C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri516 – 53823C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri544 – 56623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri572 – 59423C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri600 – 62223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri628 – 65023C2H2-type 10PROSITE-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

Enzyme and pathway databases

ReactomeiR-HSA-212436. Generic Transcription Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 510
Gene namesi
Name:ZNF510
Synonyms:KIAA0972
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:29161. ZNF510.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134944603.

Polymorphism and mutation databases

BioMutaiZNF510.
DMDMi20178235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683Zinc finger protein 510PRO_0000047628Add
BLAST

Proteomic databases

PaxDbiQ9Y2H8.
PRIDEiQ9Y2H8.

PTM databases

iPTMnetiQ9Y2H8.
PhosphoSiteiQ9Y2H8.

Expressioni

Gene expression databases

BgeeiQ9Y2H8.
CleanExiHS_ZNF510.
ExpressionAtlasiQ9Y2H8. baseline and differential.
GenevisibleiQ9Y2H8. HS.

Organism-specific databases

HPAiHPA049139.
HPA053427.

Interactioni

Protein-protein interaction databases

BioGridi116536. 2 interactions.
IntActiQ9Y2H8. 23 interactions.
MINTiMINT-1187569.
STRINGi9606.ENSP00000223428.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2H8.
SMRiQ9Y2H8. Positions 44-87, 203-663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 11772KRABPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 10 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 KRAB domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri254 – 27623C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri404 – 42623C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri432 – 45423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri460 – 48223C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri488 – 51023C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri516 – 53823C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri544 – 56623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri572 – 59423C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri600 – 62223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri628 – 65023C2H2-type 10PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129694.
HOGENOMiHOG000234617.
HOVERGENiHBG018163.
InParanoidiQ9Y2H8.
KOiK09228.
OMAiSTKMSCK.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ9Y2H8.
TreeFamiTF337898.

Family and domain databases

Gene3Di3.30.160.60. 11 hits.
InterProiIPR001909. KRAB.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 6 hits.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 10 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 10 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y2H8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPHPEAITD CVTLNTVGQL AEGGYPLRFS TLFQEQQKMN ISQASVSFKD
60 70 80 90 100
VTIEFTQEEW QQMAPVQKNL YRDVMLENYS NLVSVGYCCF KPEVIFKLEQ
110 120 130 140 150
GEEPWFSEEE FSNQSHPKDY RGDDLIKQNK KIKDKHLEQA ICINNKTLTT
160 170 180 190 200
EEEKVLGKPF TLHVAAVAST KMSCKCNSWE VNLQSISEFI INNRNYSTKK
210 220 230 240 250
IGCGNVCENS PFKINFEKTQ TGEKFYEHNK NMKALNYNEN LPKHPKFQTL
260 270 280 290 300
EQAFECNKIG KAFNDKANCV KHNSSHTGET SSKDDEFRKN CDKKTLFDHR
310 320 330 340 350
RTGTGKKHLH LNQCGKSFEK STVEEYNKLN MGIKHYELNP SGNNFNRKAH
360 370 380 390 400
LTDPQTAVIE ENPLVSNDRT QTWVKSSEYH ENKKSYQTSV HRVRRRSHSM
410 420 430 440 450
MKPYKCNECG KSFCQKGHLI QHQRTHTGEK PFECSECGKT FSQKSHLSTH
460 470 480 490 500
QRIHTAEKPY KCNECGKTFV QKSTLRGHQR IHTGEKPYEC SECGKTFVQK
510 520 530 540 550
STLRDHHRIH TGEKSFQCNQ CGKTFGQKSN LRIHQRTHTG EKTYQCNECE
560 570 580 590 600
KSFWRKDHLI QHQKTHTGEK PFKCNECGKT FARTSTLRVH QRIHTGEKPF
610 620 630 640 650
KCNECGKKFV RKAILSDHQR IHTGEKPFQC NKCGKTFGQK SNLRIHQRTH
660 670 680
SGEKSYECNE YGKLCKKSTL SLYQKIQGEG NPY
Length:683
Mass (Da):79,142
Last modified:November 1, 1999 - v1
Checksum:iA87DB365993EE3F3
GO

Sequence cautioni

The sequence BAA76816.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431Q → R.
Corresponds to variant rs2289651 [ dbSNP | Ensembl ].
VAR_019982
Natural varianti89 – 891C → R.
Corresponds to variant rs3780548 [ dbSNP | Ensembl ].
VAR_021893
Natural varianti273 – 2731N → K.
Corresponds to variant rs10217154 [ dbSNP | Ensembl ].
VAR_052848
Natural varianti398 – 3981H → D.
Corresponds to variant rs11999094 [ dbSNP | Ensembl ].
VAR_052849
Natural varianti401 – 4011M → I.
Corresponds to variant rs10217494 [ dbSNP | Ensembl ].
VAR_052850
Natural varianti634 – 6341G → E.
Corresponds to variant rs10119874 [ dbSNP | Ensembl ].
VAR_052851

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023189 mRNA. Translation: BAA76816.2. Different initiation.
AK292600 mRNA. Translation: BAF85289.1.
AL589843 Genomic DNA. Translation: CAI15266.1.
CH471174 Genomic DNA. Translation: EAW92666.1.
BC058022 mRNA. Translation: AAH58022.1. Different termination.
CCDSiCCDS35074.1.
RefSeqiNP_001300988.1. NM_001314059.1.
NP_055745.1. NM_014930.2.
XP_005251864.1. XM_005251807.2.
UniGeneiHs.633105.
Hs.75264.

Genome annotation databases

EnsembliENST00000223428; ENSP00000223428; ENSG00000081386.
ENST00000375231; ENSP00000364379; ENSG00000081386.
GeneIDi22869.
KEGGihsa:22869.
UCSCiuc004awn.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023189 mRNA. Translation: BAA76816.2. Different initiation.
AK292600 mRNA. Translation: BAF85289.1.
AL589843 Genomic DNA. Translation: CAI15266.1.
CH471174 Genomic DNA. Translation: EAW92666.1.
BC058022 mRNA. Translation: AAH58022.1. Different termination.
CCDSiCCDS35074.1.
RefSeqiNP_001300988.1. NM_001314059.1.
NP_055745.1. NM_014930.2.
XP_005251864.1. XM_005251807.2.
UniGeneiHs.633105.
Hs.75264.

3D structure databases

ProteinModelPortaliQ9Y2H8.
SMRiQ9Y2H8. Positions 44-87, 203-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116536. 2 interactions.
IntActiQ9Y2H8. 23 interactions.
MINTiMINT-1187569.
STRINGi9606.ENSP00000223428.

PTM databases

iPTMnetiQ9Y2H8.
PhosphoSiteiQ9Y2H8.

Polymorphism and mutation databases

BioMutaiZNF510.
DMDMi20178235.

Proteomic databases

PaxDbiQ9Y2H8.
PRIDEiQ9Y2H8.

Protocols and materials databases

DNASUi22869.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223428; ENSP00000223428; ENSG00000081386.
ENST00000375231; ENSP00000364379; ENSG00000081386.
GeneIDi22869.
KEGGihsa:22869.
UCSCiuc004awn.1. human.

Organism-specific databases

CTDi22869.
GeneCardsiZNF510.
HGNCiHGNC:29161. ZNF510.
HPAiHPA049139.
HPA053427.
neXtProtiNX_Q9Y2H8.
PharmGKBiPA134944603.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129694.
HOGENOMiHOG000234617.
HOVERGENiHBG018163.
InParanoidiQ9Y2H8.
KOiK09228.
OMAiSTKMSCK.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ9Y2H8.
TreeFamiTF337898.

Enzyme and pathway databases

ReactomeiR-HSA-212436. Generic Transcription Pathway.

Miscellaneous databases

ChiTaRSiZNF510. human.
GenomeRNAii22869.
NextBioi43395.
PROiQ9Y2H8.

Gene expression databases

BgeeiQ9Y2H8.
CleanExiHS_ZNF510.
ExpressionAtlasiQ9Y2H8. baseline and differential.
GenevisibleiQ9Y2H8. HS.

Family and domain databases

Gene3Di3.30.160.60. 11 hits.
InterProiIPR001909. KRAB.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 6 hits.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 10 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 10 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "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].
    Tissue: Testis.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] OF 1-467.
    Tissue: Prostate.

Entry informationi

Entry nameiZN510_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2H8
Secondary accession number(s): Q5SZP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 140 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. 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.