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

SPRY domain-containing SOCS box protein 2

Gene

SPSB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
SPRY domain-containing SOCS box protein 2
Short name:
SSB-2
Alternative name(s):
Gene-rich cluster protein C9
Gene namesi
Name:SPSB2
Synonyms:GRCC9, SSB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:29522. SPSB2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1194QTDH → HSVG: Enhances interaction with PAWR. 1 Publication

Organism-specific databases

PharmGKBiPA142670872.

Chemistry

ChEMBLiCHEMBL3325308.

Polymorphism and mutation databases

BioMutaiSPSB2.
DMDMi74732788.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263SPRY domain-containing SOCS box protein 2PRO_0000238474Add
BLAST

Proteomic databases

PaxDbiQ99619.
PRIDEiQ99619.

PTM databases

iPTMnetiQ99619.
PhosphoSiteiQ99619.

Expressioni

Gene expression databases

BgeeiQ99619.
CleanExiHS_SPSB2.
ExpressionAtlasiQ99619. baseline and differential.
GenevisibleiQ99619. HS.

Organism-specific databases

HPAiHPA055225.

Interactioni

Subunit structurei

Component of the probable ECS(SPSB2) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and SPSB2. Interacts with CUL5, RNF7, TCEB1 and TCEB2. Interacts with PAWR and MET.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIK3R3Q925693EBI-2323209,EBI-79893
PRMT1Q998732EBI-2323209,EBI-78738
TCEB1Q153693EBI-2323209,EBI-301231
vasP090522EBI-2323209,EBI-134067From a different organism.

Protein-protein interaction databases

BioGridi124227. 16 interactions.
IntActiQ99619. 9 interactions.
MINTiMINT-8417721.
STRINGi9606.ENSP00000428338.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 346Combined sources
Helixi40 – 456Combined sources
Beta strandi47 – 537Combined sources
Beta strandi57 – 604Combined sources
Helixi61 – 633Combined sources
Beta strandi65 – 684Combined sources
Beta strandi71 – 733Combined sources
Beta strandi75 – 817Combined sources
Beta strandi84 – 9411Combined sources
Helixi97 – 993Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi130 – 1345Combined sources
Turni135 – 1373Combined sources
Beta strandi139 – 1435Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi165 – 1728Combined sources
Turni173 – 1764Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi185 – 1917Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi211 – 2188Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EMWX-ray1.80A26-219[»]
ProteinModelPortaliQ99619.
SMRiQ99619. Positions 24-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99619.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 221196B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST
Domaini222 – 26342SOCS boxPROSITE-ProRule annotationAdd
BLAST

Domaini

The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes.By similarity

Sequence similaritiesi

Belongs to the SPSB family.Curated
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 SOCS box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3953. Eukaryota.
ENOG410XQC1. LUCA.
GeneTreeiENSGT00390000009402.
HOGENOMiHOG000230524.
HOVERGENiHBG055793.
InParanoidiQ99619.
KOiK10344.
OMAiWPREQRG.
OrthoDBiEOG72C513.
PhylomeDBiQ99619.
TreeFamiTF312822.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR001496. SOCS_box.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF07525. SOCS_box. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00253. SOCS. 1 hit.
SM00969. SOCS_box. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50225. SOCS. 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: Q99619-1) [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
MGQTALAGGS SSTPTPQALY PDLSCPEGLE ELLSAPPPDL GAQRRHGWNP
60 70 80 90 100
KDCSENIEVK EGGLYFERRP VAQSTDGARG KRGYSRGLHA WEISWPLEQR
110 120 130 140 150
GTHAVVGVAT ALAPLQTDHY AALLGSNSES WGWDIGRGKL YHQSKGPGAP
160 170 180 190 200
QYPAGTQGEQ LEVPERLLVV LDMEEGTLGY AIGGTYLGPA FRGLKGRTLY
210 220 230 240 250
PAVSAVWGQC QVRIRYLGER RAEPHSLLHL SRLCVRHNLG DTRLGQVSAL
260
PLPPAMKRYL LYQ
Length:263
Mass (Da):28,630
Last modified:May 1, 1997 - v1
Checksum:i0729EDDD0B598665
GO
Isoform 2 (identifier: Q99619-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     222-263: AEPHSLLHLS...PAMKRYLLYQ → GEAWGRRGEN...PQPLFSAGKG

Note: No experimental confirmation available.
Show »
Length:267
Mass (Da):28,642
Checksum:i741ACE1245483D0E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei222 – 26342AEPHS…YLLYQ → GEAWGRRGENFLSLVAVVWD GNSSDKSRGDGPSSSLPQPL FSAGKG in isoform 2. 1 PublicationVSP_057167Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF403027 mRNA. Translation: AAL57346.1.
AK297963 mRNA. Translation: BAH12697.1.
U47924 Genomic DNA. Translation: AAB51328.1.
CH471116 Genomic DNA. Translation: EAW88719.1.
CH471116 Genomic DNA. Translation: EAW88720.1.
BC002983 mRNA. Translation: AAH02983.1.
BC071933 mRNA. Translation: AAH71933.1.
CCDSiCCDS8567.1. [Q99619-1]
RefSeqiNP_001139788.1. NM_001146316.1. [Q99619-1]
NP_001306599.1. NM_001319670.1. [Q99619-1]
NP_116030.1. NM_032641.3. [Q99619-1]
XP_005253860.1. XM_005253803.3. [Q99619-2]
XP_011519334.1. XM_011521032.1. [Q99619-2]
UniGeneiHs.479856.

Genome annotation databases

EnsembliENST00000519357; ENSP00000431037; ENSG00000111671. [Q99619-2]
ENST00000523102; ENSP00000430872; ENSG00000111671. [Q99619-1]
ENST00000524270; ENSP00000428338; ENSG00000111671. [Q99619-1]
GeneIDi84727.
KEGGihsa:84727.
UCSCiuc001qrl.4. human. [Q99619-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF403027 mRNA. Translation: AAL57346.1.
AK297963 mRNA. Translation: BAH12697.1.
U47924 Genomic DNA. Translation: AAB51328.1.
CH471116 Genomic DNA. Translation: EAW88719.1.
CH471116 Genomic DNA. Translation: EAW88720.1.
BC002983 mRNA. Translation: AAH02983.1.
BC071933 mRNA. Translation: AAH71933.1.
CCDSiCCDS8567.1. [Q99619-1]
RefSeqiNP_001139788.1. NM_001146316.1. [Q99619-1]
NP_001306599.1. NM_001319670.1. [Q99619-1]
NP_116030.1. NM_032641.3. [Q99619-1]
XP_005253860.1. XM_005253803.3. [Q99619-2]
XP_011519334.1. XM_011521032.1. [Q99619-2]
UniGeneiHs.479856.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EMWX-ray1.80A26-219[»]
ProteinModelPortaliQ99619.
SMRiQ99619. Positions 24-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124227. 16 interactions.
IntActiQ99619. 9 interactions.
MINTiMINT-8417721.
STRINGi9606.ENSP00000428338.

Chemistry

ChEMBLiCHEMBL3325308.

PTM databases

iPTMnetiQ99619.
PhosphoSiteiQ99619.

Polymorphism and mutation databases

BioMutaiSPSB2.
DMDMi74732788.

Proteomic databases

PaxDbiQ99619.
PRIDEiQ99619.

Protocols and materials databases

DNASUi84727.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000519357; ENSP00000431037; ENSG00000111671. [Q99619-2]
ENST00000523102; ENSP00000430872; ENSG00000111671. [Q99619-1]
ENST00000524270; ENSP00000428338; ENSG00000111671. [Q99619-1]
GeneIDi84727.
KEGGihsa:84727.
UCSCiuc001qrl.4. human. [Q99619-1]

Organism-specific databases

CTDi84727.
GeneCardsiSPSB2.
HGNCiHGNC:29522. SPSB2.
HPAiHPA055225.
MIMi611658. gene.
neXtProtiNX_Q99619.
PharmGKBiPA142670872.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3953. Eukaryota.
ENOG410XQC1. LUCA.
GeneTreeiENSGT00390000009402.
HOGENOMiHOG000230524.
HOVERGENiHBG055793.
InParanoidiQ99619.
KOiK10344.
OMAiWPREQRG.
OrthoDBiEOG72C513.
PhylomeDBiQ99619.
TreeFamiTF312822.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ99619.
GenomeRNAii84727.
PROiQ99619.
SOURCEiSearch...

Gene expression databases

BgeeiQ99619.
CleanExiHS_SPSB2.
ExpressionAtlasiQ99619. baseline and differential.
GenevisibleiQ99619. HS.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR001496. SOCS_box.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF07525. SOCS_box. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00253. SOCS. 1 hit.
SM00969. SOCS_box. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SOCS box proteins."
    Friedel E.J., Nicholson S.E., Nicola N.A., Kile B.T., Hilton D.J.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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. "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
    Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
    Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 1).
    Tissue: Placenta and Spleen.
  7. "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases."
    Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., Nakayama K.I.
    Genes Dev. 18:3055-3065(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL5; RNF7; TCEB1 AND TCEB2.
  8. "The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response element pathway."
    Wang D., Li Z., Messing E.M., Wu G.
    J. Biol. Chem. 280:16393-16401(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MET.
  9. "Structural and functional insights into the B30.2/SPRY domain."
    Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.
    EMBO J. 25:1353-1363(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAWR, MUTAGENESIS OF 116-GLN--GLY-119.

Entry informationi

Entry nameiSPSB2_HUMAN
AccessioniPrimary (citable) accession number: Q99619
Secondary accession number(s): B7Z4W1, D3DUT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 133 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.