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Protein

Poly [ADP-ribose] polymerase 11

Gene

PARP11

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

Functioni

Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (By similarity). In vitro, exhibits mono(ADP-ribosyl) transferase activity (PubMed:25673562).By similarity1 Publication

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation

GO - Molecular functioni

  • NAD+ ADP-ribosyltransferase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Differentiation, mRNA transport, Protein transport, Spermatogenesis, Translocation, Transport

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi2.4.2.30. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 11 (EC:2.4.2.30)
Short name:
PARP-11
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 11
Short name:
ARTD11
Gene namesi
Name:PARP11
Synonyms:C12orf6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1186. PARP11.

Subcellular locationi

GO - Cellular componenti

  • nuclear envelope Source: MGI
  • nuclear pore Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311Y → A: No effect on subcellular location at the nuclear envelope. 1 Publication
Mutagenesisi41 – 411F → A: No effect on subcellular location at the nuclear envelope. 1 Publication
Mutagenesisi77 – 771Y → A: Loss of subcellular location at the nuclear envelope. 1 Publication
Mutagenesisi86 – 861Q → A: Loss of subcellular location at the nuclear envelope. 1 Publication
Mutagenesisi95 – 951R → A: Loss of subcellular location at the nuclear envelope. 1 Publication
Mutagenesisi198 – 1981G → W: No effect on subcellular location at the nuclear envelope. 1 Publication

Organism-specific databases

PharmGKBiPA25507.

Chemistry

ChEMBLiCHEMBL2380189.

Polymorphism and mutation databases

DMDMi74734315.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Poly [ADP-ribose] polymerase 11PRO_0000273419Add
BLAST

Post-translational modificationi

In vitro, can undergo mono-ADP-ribosylation.1 Publication

Keywords - PTMi

ADP-ribosylation

Proteomic databases

PaxDbiQ9NR21.
PRIDEiQ9NR21.

PTM databases

iPTMnetiQ9NR21.
PhosphoSiteiQ9NR21.

Expressioni

Gene expression databases

BgeeiQ9NR21.
CleanExiHS_PARP11.
ExpressionAtlasiQ9NR21. baseline and differential.
GenevisibleiQ9NR21. HS.

Organism-specific databases

HPAiHPA026895.

Interactioni

Protein-protein interaction databases

BioGridi121365. 11 interactions.
IntActiQ9NR21. 5 interactions.
MINTiMINT-1446506.
STRINGi9606.ENSP00000228820.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315Combined sources
Beta strandi34 – 363Combined sources
Beta strandi44 – 463Combined sources
Helixi53 – 6210Combined sources
Beta strandi66 – 727Combined sources
Beta strandi75 – 806Combined sources
Turni81 – 844Combined sources
Beta strandi85 – 917Combined sources
Beta strandi94 – 1029Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK6NMR-A15-103[»]
ProteinModelPortaliQ9NR21.
SMRiQ9NR21. Positions 10-103, 131-330.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NR21.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 9985WWEPROSITE-ProRule annotationAdd
BLAST
Domaini116 – 331216PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 1 WWE domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IJ12. Eukaryota.
ENOG4110TY6. LUCA.
GeneTreeiENSGT00760000119084.
HOGENOMiHOG000237349.
HOVERGENiHBG056772.
InParanoidiQ9NR21.
KOiK15259.
OMAiDTNIQCS.
PhylomeDBiQ9NR21.
TreeFamiTF338389.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004170. WWE-dom.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NR21-1) [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
MFHKAEELFS KTTNNEVDDM DTSDTQWGWF YLAECGKWHM FQPDTNSQCS
60 70 80 90 100
VSSEDIEKSF KTNPCGSISF TTSKFSYKID FAEMKQMNLT TGKQRLIKRA
110 120 130 140 150
PFSISAFSYI CENEAIPMPP HWENVNTQVP YQLIPLHNQT HEYNEVANLF
160 170 180 190 200
GKTMDRNRIK RIQRIQNLDL WEFFCRKKAQ LKKKRGVPQI NEQMLFHGTS
210 220 230 240 250
SEFVEAICIH NFDWRINGIH GAVFGKGTYF ARDAAYSSRF CKDDIKHGNT
260 270 280 290 300
FQIHGVSLQQ RHLFRTYKSM FLARVLIGDY INGDSKYMRP PSKDGSYVNL
310 320 330
YDSCVDDTWN PKIFVVFDAN QIYPEYLIDF H
Length:331
Mass (Da):38,739
Last modified:October 1, 2000 - v1
Checksum:i732A46ABC0456E7E
GO
Isoform 2 (identifier: Q9NR21-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
     75-82: FSYKIDFA → MWEVAHVS

Show »
Length:257
Mass (Da):30,212
Checksum:iC31718D5A6CDD6D9
GO
Isoform 3 (identifier: Q9NR21-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MWEANPEM

Show »
Length:338
Mass (Da):39,597
Checksum:i2019EB49823BB08F
GO

Sequence cautioni

The sequence AAH17569.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH31073.1 differs from that shown.Probable cloning artifact.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7474Missing in isoform 2. 2 PublicationsVSP_022553Add
BLAST
Alternative sequencei1 – 11M → MWEANPEM in isoform 3. 1 PublicationVSP_040378
Alternative sequencei75 – 828FSYKIDFA → MWEVAHVS in isoform 2. 2 PublicationsVSP_022554

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263540 mRNA. Translation: AAF91391.1.
AK299372 mRNA. Translation: BAG61362.1.
CR749294 mRNA. Translation: CAH18149.1.
AC005842 Genomic DNA. No translation available.
AC006207 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88853.1.
BC017569 mRNA. Translation: AAH17569.1. Different initiation.
BC031073 mRNA. Translation: AAH31073.1. Sequence problems.
CCDSiCCDS66281.1. [Q9NR21-2]
CCDS8523.2. [Q9NR21-4]
RefSeqiNP_001273450.1. NM_001286521.1. [Q9NR21-2]
NP_001273451.1. NM_001286522.1. [Q9NR21-2]
NP_065100.2. NM_020367.5. [Q9NR21-4]
XP_005253768.1. XM_005253711.3. [Q9NR21-1]
XP_011519272.1. XM_011520970.1. [Q9NR21-1]
XP_011519273.1. XM_011520971.1. [Q9NR21-1]
XP_011519275.1. XM_011520973.1. [Q9NR21-1]
UniGeneiHs.657268.

Genome annotation databases

EnsembliENST00000228820; ENSP00000228820; ENSG00000111224. [Q9NR21-4]
ENST00000427057; ENSP00000397058; ENSG00000111224. [Q9NR21-2]
ENST00000447133; ENSP00000405385; ENSG00000111224. [Q9NR21-2]
GeneIDi57097.
KEGGihsa:57097.
UCSCiuc001qml.4. human. [Q9NR21-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263540 mRNA. Translation: AAF91391.1.
AK299372 mRNA. Translation: BAG61362.1.
CR749294 mRNA. Translation: CAH18149.1.
AC005842 Genomic DNA. No translation available.
AC006207 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88853.1.
BC017569 mRNA. Translation: AAH17569.1. Different initiation.
BC031073 mRNA. Translation: AAH31073.1. Sequence problems.
CCDSiCCDS66281.1. [Q9NR21-2]
CCDS8523.2. [Q9NR21-4]
RefSeqiNP_001273450.1. NM_001286521.1. [Q9NR21-2]
NP_001273451.1. NM_001286522.1. [Q9NR21-2]
NP_065100.2. NM_020367.5. [Q9NR21-4]
XP_005253768.1. XM_005253711.3. [Q9NR21-1]
XP_011519272.1. XM_011520970.1. [Q9NR21-1]
XP_011519273.1. XM_011520971.1. [Q9NR21-1]
XP_011519275.1. XM_011520973.1. [Q9NR21-1]
UniGeneiHs.657268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK6NMR-A15-103[»]
ProteinModelPortaliQ9NR21.
SMRiQ9NR21. Positions 10-103, 131-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121365. 11 interactions.
IntActiQ9NR21. 5 interactions.
MINTiMINT-1446506.
STRINGi9606.ENSP00000228820.

Chemistry

ChEMBLiCHEMBL2380189.

PTM databases

iPTMnetiQ9NR21.
PhosphoSiteiQ9NR21.

Polymorphism and mutation databases

DMDMi74734315.

Proteomic databases

PaxDbiQ9NR21.
PRIDEiQ9NR21.

Protocols and materials databases

DNASUi57097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228820; ENSP00000228820; ENSG00000111224. [Q9NR21-4]
ENST00000427057; ENSP00000397058; ENSG00000111224. [Q9NR21-2]
ENST00000447133; ENSP00000405385; ENSG00000111224. [Q9NR21-2]
GeneIDi57097.
KEGGihsa:57097.
UCSCiuc001qml.4. human. [Q9NR21-1]

Organism-specific databases

CTDi57097.
GeneCardsiPARP11.
HGNCiHGNC:1186. PARP11.
HPAiHPA026895.
MIMi616706. gene.
neXtProtiNX_Q9NR21.
PharmGKBiPA25507.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ12. Eukaryota.
ENOG4110TY6. LUCA.
GeneTreeiENSGT00760000119084.
HOGENOMiHOG000237349.
HOVERGENiHBG056772.
InParanoidiQ9NR21.
KOiK15259.
OMAiDTNIQCS.
PhylomeDBiQ9NR21.
TreeFamiTF338389.

Enzyme and pathway databases

BRENDAi2.4.2.30. 2681.

Miscellaneous databases

ChiTaRSiPARP11. human.
EvolutionaryTraceiQ9NR21.
GenomeRNAii57097.
PROiQ9NR21.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NR21.
CleanExiHS_PARP11.
ExpressionAtlasiQ9NR21. baseline and differential.
GenevisibleiQ9NR21. HS.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004170. WWE-dom.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transcripts in human map region 12p13.3."
    Lorenz B., Strom T.M.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  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] (ISOFORM 2).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] (ISOFORM 3).
    Tissue: Bone marrow and Brain.
  7. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
    Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
    Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  8. "Spermatid head elongation with normal nuclear shaping requires ADP-ribosyltransferase PARP11 (ARTD11) in mice."
    Meyer-Ficca M.L., Ihara M., Bader J.J., Leu N.A., Beneke S., Meyer R.G.
    Biol. Reprod. 92:80-80(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MONO-ADP-RIBOSYLATION, MUTAGENESIS OF TYR-31; PHE-41; TYR-77; GLN-86; ARG-95 AND GLY-198.
  9. "Solution structure of WWE domain in poly (ADP-ribose) polymerase family, member 11 (PARP11)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 15-103.

Entry informationi

Entry nameiPAR11_HUMAN
AccessioniPrimary (citable) accession number: Q9NR21
Secondary accession number(s): B4DRQ0, Q68DS1, Q8N5Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 110 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.