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Protein

Death domain-containing protein CRADD

Gene

CRADD

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

Functioni

Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex.

GO - Molecular functioni

  • death domain binding Source: BHF-UCL
  • protease binding Source: BHF-UCL
  • protein binding, bridging Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-HSA-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.
SignaLinkiP78560.

Names & Taxonomyi

Protein namesi
Recommended name:
Death domain-containing protein CRADD
Alternative name(s):
Caspase and RIP adapter with death domain
RIP-associated protein with a death domain
Gene namesi
Name:CRADD
Synonyms:RAIDD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2340. CRADD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 34 (MRT34)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT34 is a non-syndromic form. Affected individuals have mildly delayed development and significantly impaired cognitive function, precluding independent living and self-care. Speech is rudimentary, but articulate; autism is not present.
See also OMIM:614499
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281G → R in MRT34. 1 Publication
VAR_067536

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiCRADD.
MIMi614499. phenotype.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA26860.

Polymorphism and mutation databases

BioMutaiCRADD.
DMDMi2498833.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Death domain-containing protein CRADDPRO_0000079326Add
BLAST

Proteomic databases

EPDiP78560.
PaxDbiP78560.
PRIDEiP78560.

PTM databases

iPTMnetiP78560.

Expressioni

Tissue specificityi

Constitutively expressed in most tissues, with particularly high expression in adult heart, testis, liver, skeletal muscle, fetal liver and kidney.

Gene expression databases

BgeeiP78560.
CleanExiHS_CRADD.
ExpressionAtlasiP78560. baseline and differential.
GenevisibleiP78560. HS.

Organism-specific databases

HPAiCAB005337.
HPA046546.

Interactioni

Subunit structurei

Interacts with PIDD.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL2Q8NEU83EBI-520375,EBI-741261
BBS5Q8N3I73EBI-520375,EBI-2892592
CASP2P4257512EBI-520375,EBI-520342
KCTD9Q7L2733EBI-520375,EBI-4397613
PIDD1Q9HB758EBI-520375,EBI-520427
taxP140793EBI-520375,EBI-9675698From a different organism.
TRIM54Q9BYV23EBI-520375,EBI-2130429

GO - Molecular functioni

  • death domain binding Source: BHF-UCL
  • protease binding Source: BHF-UCL
  • protein binding, bridging Source: BHF-UCL

Protein-protein interaction databases

BioGridi114275. 21 interactions.
IntActiP78560. 16 interactions.
MINTiMINT-1520976.
STRINGi9606.ENSP00000327647.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814Combined sources
Helixi27 – 337Combined sources
Helixi38 – 447Combined sources
Beta strandi48 – 503Combined sources
Helixi51 – 6010Combined sources
Turni61 – 633Combined sources
Helixi69 – 757Combined sources
Helixi79 – 9214Combined sources
Helixi110 – 1123Combined sources
Helixi117 – 12610Combined sources
Helixi131 – 1377Combined sources
Helixi142 – 15110Combined sources
Helixi156 – 17116Combined sources
Helixi172 – 1743Combined sources
Helixi177 – 18610Combined sources
Helixi192 – 1976Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O71X-ray2.00A94-199[»]
2OF5X-ray3.20A/B/C/D/E/F/G94-199[»]
3CRDNMR-A1-100[»]
ProteinModelPortaliP78560.
SMRiP78560. Positions 1-100, 109-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78560.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9191CARDPROSITE-ProRule annotationAdd
BLAST
Domaini116 – 18873DeathPROSITE-ProRule annotationAdd
BLAST

Domaini

Contains a death domain involved in the binding of RIP protein.
The CARD domain mediates the interaction with caspase-2.

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation
Contains 1 death domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IJAM. Eukaryota.
ENOG4111SYE. LUCA.
GeneTreeiENSGT00390000014448.
HOGENOMiHOG000111965.
HOVERGENiHBG051112.
InParanoidiP78560.
KOiK02832.
OMAiLGPEWEH.
PhylomeDBiP78560.
TreeFamiTF333055.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF00531. Death. 1 hit.
[Graphical view]
SMARTiSM00114. CARD. 1 hit.
SM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 2 hits.
PROSITEiPS50209. CARD. 1 hit.
PS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P78560-1) [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
MEARDKQVLR SLRLELGAEV LVEGLVLQYL YQEGILTENH IQEINAQTTG
60 70 80 90 100
LRKTMLLLDI LPSRGPKAFD TFLDSLQEFP WVREKLKKAR EEAMTDLPAG
110 120 130 140 150
DRLTGIPSHI LNSSPSDRQI NQLAQRLGPE WEPMVLSLGL SQTDIYRCKA
160 170 180 190
NHPHNVQSQV VEAFIRWRQR FGKQATFQSL HNGLRAVEVD PSLLLHMLE
Length:199
Mass (Da):22,745
Last modified:May 1, 1997 - v1
Checksum:i3437CC612C85E402
GO
Isoform 2 (identifier: P78560-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-199: DRLTGIPSHI...DPSLLLHMLE → CWP

Note: No experimental confirmation available.
Show »
Length:103
Mass (Da):11,826
Checksum:i04DFF4A1F09D0B56
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281G → R in MRT34. 1 Publication
VAR_067536

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 19999DRLTG…LHMLE → CWP in isoform 2. 1 PublicationVSP_056892Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84388 mRNA. Translation: AAC50952.1.
U79115 mRNA. Translation: AAB42217.1.
AK294986 mRNA. Translation: BAH11941.1.
AC012085 Genomic DNA. No translation available.
AC012464 Genomic DNA. No translation available.
AC025261 Genomic DNA. No translation available.
BC017042 mRNA. Translation: AAH17042.1.
CCDSiCCDS9048.1. [P78560-1]
RefSeqiNP_001307028.1. NM_001320099.1. [P78560-1]
NP_001307029.1. NM_001320100.1.
NP_001307030.1. NM_001320101.1.
NP_003796.1. NM_003805.4. [P78560-1]
UniGeneiHs.38533.
Hs.591016.
Hs.660031.
Hs.719191.

Genome annotation databases

EnsembliENST00000332896; ENSP00000327647; ENSG00000169372. [P78560-1]
ENST00000542893; ENSP00000439068; ENSG00000169372. [P78560-1]
ENST00000551065; ENSP00000448425; ENSG00000169372. [P78560-2]
GeneIDi8738.
KEGGihsa:8738.
UCSCiuc058rts.1. human. [P78560-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84388 mRNA. Translation: AAC50952.1.
U79115 mRNA. Translation: AAB42217.1.
AK294986 mRNA. Translation: BAH11941.1.
AC012085 Genomic DNA. No translation available.
AC012464 Genomic DNA. No translation available.
AC025261 Genomic DNA. No translation available.
BC017042 mRNA. Translation: AAH17042.1.
CCDSiCCDS9048.1. [P78560-1]
RefSeqiNP_001307028.1. NM_001320099.1. [P78560-1]
NP_001307029.1. NM_001320100.1.
NP_001307030.1. NM_001320101.1.
NP_003796.1. NM_003805.4. [P78560-1]
UniGeneiHs.38533.
Hs.591016.
Hs.660031.
Hs.719191.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O71X-ray2.00A94-199[»]
2OF5X-ray3.20A/B/C/D/E/F/G94-199[»]
3CRDNMR-A1-100[»]
ProteinModelPortaliP78560.
SMRiP78560. Positions 1-100, 109-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114275. 21 interactions.
IntActiP78560. 16 interactions.
MINTiMINT-1520976.
STRINGi9606.ENSP00000327647.

PTM databases

iPTMnetiP78560.

Polymorphism and mutation databases

BioMutaiCRADD.
DMDMi2498833.

Proteomic databases

EPDiP78560.
PaxDbiP78560.
PRIDEiP78560.

Protocols and materials databases

DNASUi8738.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332896; ENSP00000327647; ENSG00000169372. [P78560-1]
ENST00000542893; ENSP00000439068; ENSG00000169372. [P78560-1]
ENST00000551065; ENSP00000448425; ENSG00000169372. [P78560-2]
GeneIDi8738.
KEGGihsa:8738.
UCSCiuc058rts.1. human. [P78560-1]

Organism-specific databases

CTDi8738.
GeneCardsiCRADD.
HGNCiHGNC:2340. CRADD.
HPAiCAB005337.
HPA046546.
MalaCardsiCRADD.
MIMi603454. gene.
614499. phenotype.
neXtProtiNX_P78560.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA26860.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJAM. Eukaryota.
ENOG4111SYE. LUCA.
GeneTreeiENSGT00390000014448.
HOGENOMiHOG000111965.
HOVERGENiHBG051112.
InParanoidiP78560.
KOiK02832.
OMAiLGPEWEH.
PhylomeDBiP78560.
TreeFamiTF333055.

Enzyme and pathway databases

ReactomeiR-HSA-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.
SignaLinkiP78560.

Miscellaneous databases

ChiTaRSiCRADD. human.
EvolutionaryTraceiP78560.
GeneWikiiCRADD.
GenomeRNAii8738.
PROiP78560.
SOURCEiSearch...

Gene expression databases

BgeeiP78560.
CleanExiHS_CRADD.
ExpressionAtlasiP78560. baseline and differential.
GenevisibleiP78560. HS.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF00531. Death. 1 hit.
[Graphical view]
SMARTiSM00114. CARD. 1 hit.
SM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 2 hits.
PROSITEiPS50209. CARD. 1 hit.
PS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP."
    Ahmad M., Srinivasula S.M., Wang L., Talanian R.V., Litwack G., Fernandes-Alnemri T., Alnemri E.S.
    Cancer Res. 57:615-619(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "RAIDD is a new 'death' adaptor molecule."
    Duan H., Dixit V.M.
    Nature 385:86-89(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 2).
    Tissue: Brain.
  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. "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 1).
    Tissue: Colon.
  6. "The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress."
    Tinel A., Tschopp J.
    Science 304:843-846(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIDD.
  7. "Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage."
    Vakifahmetoglu H., Olsson M., Orrenius S., Zhivotovsky B.
    Oncogene 25:5683-5692(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIDD.
  8. "Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment."
    Chou J.J., Matsuo H., Duan H., Wagner G.
    Cell 94:171-180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-100.
  9. Cited for: VARIANT MRT34 ARG-128.

Entry informationi

Entry nameiCRADD_HUMAN
AccessioniPrimary (citable) accession number: P78560
Secondary accession number(s): B7Z2Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 149 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. 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.