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Protein

Inactive rhomboid protein 1

Gene

RHBDF1

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

Functioni

Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration.4 Publications

GO - Biological processi

  • cell migration Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • negative regulation of protein secretion Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • proteolysis Source: InterPro
  • regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  • regulation of proteasomal protein catabolic process Source: UniProtKB
  • regulation of protein secretion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Growth factor binding

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive rhomboid protein 1
Short name:
iRhom1
Alternative name(s):
Epidermal growth factor receptor-related protein
Rhomboid 5 homolog 1
Rhomboid family member 1
p100hRho
Gene namesi
Name:RHBDF1
Synonyms:C16orf8, DIST1, IRHOM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:20561. RHBDF1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 411411CytoplasmicSequence analysisAdd
BLAST
Transmembranei412 – 43221HelicalSequence analysisAdd
BLAST
Topological domaini433 – 655223LumenalSequence analysisAdd
BLAST
Transmembranei656 – 67621HelicalSequence analysisAdd
BLAST
Topological domaini677 – 69115CytoplasmicSequence analysisAdd
BLAST
Transmembranei692 – 71221HelicalSequence analysisAdd
BLAST
Topological domaini713 – 7142LumenalSequence analysis
Transmembranei715 – 73521HelicalSequence analysisAdd
BLAST
Topological domaini736 – 74611CytoplasmicSequence analysisAdd
BLAST
Transmembranei747 – 76721HelicalSequence analysisAdd
BLAST
Topological domaini768 – 7725LumenalSequence analysis
Transmembranei773 – 79321HelicalSequence analysisAdd
BLAST
Topological domaini794 – 80310CytoplasmicSequence analysis
Transmembranei804 – 82421HelicalSequence analysisAdd
BLAST
Topological domaini825 – 85531LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • Golgi membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311N → Q: No effect. 1 Publication
Mutagenesisi381 – 3811N → Q: No effect. 1 Publication
Mutagenesisi583 – 5831N → Q: Loss of N-glycosylation. 1 Publication

Organism-specific databases

PharmGKBiPA25563.

Polymorphism and mutation databases

BioMutaiRHBDF1.
DMDMi190360226.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 855855Inactive rhomboid protein 1PRO_0000340104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei180 – 1801PhosphothreonineBy similarity
Modified residuei183 – 1831PhosphothreonineBy similarity
Glycosylationi583 – 5831N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ96CC6.
PaxDbiQ96CC6.
PRIDEiQ96CC6.

PTM databases

iPTMnetiQ96CC6.
PhosphoSiteiQ96CC6.
SwissPalmiQ96CC6.

Expressioni

Tissue specificityi

Highly expressed in cerebellum, cerebrum, heart, skeletal muscle, placenta, pancreatic islet and testis. Detected at lower levels in colon, kidney, small intestine and lung.2 Publications

Gene expression databases

BgeeiQ96CC6.
CleanExiHS_RHBDF1.
ExpressionAtlasiQ96CC6. baseline and differential.
GenevisibleiQ96CC6. HS.

Interactioni

Subunit structurei

Homodimer, or homooligomer. Interacts with TGFA and HBEGF. Interacts with EGF; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD).2 Publications

Protein-protein interaction databases

BioGridi122129. 2 interactions.
IntActiQ96CC6. 1 interaction.
STRINGi9606.ENSP00000262316.

Structurei

3D structure databases

ProteinModelPortaliQ96CC6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S54 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2290. Eukaryota.
COG0705. LUCA.
GeneTreeiENSGT00390000012532.
HOGENOMiHOG000154118.
HOVERGENiHBG059673.
InParanoidiQ96CC6.
OMAiHMDCAIT.
OrthoDBiEOG7288QH.
PhylomeDBiQ96CC6.
TreeFamiTF312988.

Family and domain databases

Gene3Di1.20.1540.10. 2 hits.
InterProiIPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR022241. Rhomboid_SP.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 3 hits.
PfamiPF01694. Rhomboid. 1 hit.
PF12595. Rhomboid_SP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96CC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEARRDSTS SLQRKKPPWL KLDIPSAVPL TAEEPSFLQP LRRQAFLRSV
60 70 80 90 100
SMPAETAHIS SPHHELRRPV LQRQTSITQT IRRGTADWFG VSKDSDSTQK
110 120 130 140 150
WQRKSIRHCS QRYGKLKPQV LRELDLPSQD NVSLTSTETP PPLYVGPCQL
160 170 180 190 200
GMQKIIDPLA RGRAFRVADD TAEGLSAPHT PVTPGAASLC SFSSSRSGFH
210 220 230 240 250
RLPRRRKRES VAKMSFRAAA ALMKGRSVRD GTFRRAQRRS FTPASFLEED
260 270 280 290 300
TTDFPDELDT SFFAREGILH EELSTYPDEV FESPSEAALK DWEKAPEQAD
310 320 330 340 350
LTGGALDRSE LERSHLMLPL ERGWRKQKEG AAAPQPKVRL RQEVVSTAGP
360 370 380 390 400
RRGQRIAVPV RKLFAREKRP YGLGMVGRLT NRTYRKRIDS FVKRQIEDMD
410 420 430 440 450
DHRPFFTYWL TFVHSLVTIL AVCIYGIAPV GFSQHETVDS VLRNRGVYEN
460 470 480 490 500
VKYVQQENFW IGPSSEALIH LGAKFSPCMR QDPQVHSFIR SAREREKHSA
510 520 530 540 550
CCVRNDRSGC VQTSEEECSS TLAVWVKWPI HPSAPELAGH KRQFGSVCHQ
560 570 580 590 600
DPRVCDEPSS EDPHEWPEDI TKWPICTKNS AGNHTNHPHM DCVITGRPCC
610 620 630 640 650
IGTKGRCEIT SREYCDFMRG YFHEEATLCS QVHCMDDVCG LLPFLNPEVP
660 670 680 690 700
DQFYRLWLSL FLHAGILHCL VSICFQMTVL RDLEKLAGWH RIAIIYLLSG
710 720 730 740 750
VTGNLASAIF LPYRAEVGPA GSQFGILACL FVELFQSWQI LARPWRAFFK
760 770 780 790 800
LLAVVLFLFT FGLLPWIDNF AHISGFISGL FLSFAFLPYI SFGKFDLYRK
810 820 830 840 850
RCQIIIFQVV FLGLLAGLVV LFYVYPVRCE WCEFLTCIPF TDKFCEKYEL

DAQLH
Length:855
Mass (Da):97,401
Last modified:June 10, 2008 - v2
Checksum:iC39FCCE4CE89323B
GO

Sequence cautioni

The sequence AAA02490.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAK61212.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence ABD95905.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW85873.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51R → C in ABD95905 (PubMed:16728641).Curated
Sequence conflicti237 – 2371Q → R in AAH14425 (PubMed:15489334).Curated
Sequence conflicti418 – 4181T → A in BAB15318 (PubMed:14702039).Curated
Sequence conflicti551 – 5533DPR → GSQ in AAA02490 (PubMed:8318735).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti265 – 2651R → W.
Corresponds to variant rs3213511 [ dbSNP | Ensembl ].
VAR_044006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ431198 Genomic DNA. Translation: ABD95905.1. Sequence problems.
AK026010 mRNA. Translation: BAB15318.1.
AK291177 mRNA. Translation: BAF83866.1.
AE006462 Genomic DNA. Translation: AAK61212.1. Sequence problems.
Z69719 Genomic DNA. Translation: CAI95608.1.
CH471112 Genomic DNA. Translation: EAW85873.1. Sequence problems.
CH471112 Genomic DNA. Translation: EAW85876.1.
BC014425 mRNA. Translation: AAH14425.1.
M99624 mRNA. Translation: AAA02490.1. Different initiation.
CCDSiCCDS32344.1.
RefSeqiNP_071895.3. NM_022450.3.
XP_005255551.1. XM_005255494.1.
UniGeneiHs.744992.

Genome annotation databases

EnsembliENST00000262316; ENSP00000262316; ENSG00000007384.
GeneIDi64285.
KEGGihsa:64285.
UCSCiuc002cfl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ431198 Genomic DNA. Translation: ABD95905.1. Sequence problems.
AK026010 mRNA. Translation: BAB15318.1.
AK291177 mRNA. Translation: BAF83866.1.
AE006462 Genomic DNA. Translation: AAK61212.1. Sequence problems.
Z69719 Genomic DNA. Translation: CAI95608.1.
CH471112 Genomic DNA. Translation: EAW85873.1. Sequence problems.
CH471112 Genomic DNA. Translation: EAW85876.1.
BC014425 mRNA. Translation: AAH14425.1.
M99624 mRNA. Translation: AAA02490.1. Different initiation.
CCDSiCCDS32344.1.
RefSeqiNP_071895.3. NM_022450.3.
XP_005255551.1. XM_005255494.1.
UniGeneiHs.744992.

3D structure databases

ProteinModelPortaliQ96CC6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122129. 2 interactions.
IntActiQ96CC6. 1 interaction.
STRINGi9606.ENSP00000262316.

PTM databases

iPTMnetiQ96CC6.
PhosphoSiteiQ96CC6.
SwissPalmiQ96CC6.

Polymorphism and mutation databases

BioMutaiRHBDF1.
DMDMi190360226.

Proteomic databases

MaxQBiQ96CC6.
PaxDbiQ96CC6.
PRIDEiQ96CC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262316; ENSP00000262316; ENSG00000007384.
GeneIDi64285.
KEGGihsa:64285.
UCSCiuc002cfl.4. human.

Organism-specific databases

CTDi64285.
GeneCardsiRHBDF1.
H-InvDBHIX0012637.
HGNCiHGNC:20561. RHBDF1.
MIMi614403. gene.
neXtProtiNX_Q96CC6.
PharmGKBiPA25563.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2290. Eukaryota.
COG0705. LUCA.
GeneTreeiENSGT00390000012532.
HOGENOMiHOG000154118.
HOVERGENiHBG059673.
InParanoidiQ96CC6.
OMAiHMDCAIT.
OrthoDBiEOG7288QH.
PhylomeDBiQ96CC6.
TreeFamiTF312988.

Miscellaneous databases

ChiTaRSiRHBDF1. human.
GeneWikiiRHBDF1.
GenomeRNAii64285.
PROiQ96CC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ96CC6.
CleanExiHS_RHBDF1.
ExpressionAtlasiQ96CC6. baseline and differential.
GenevisibleiQ96CC6. HS.

Family and domain databases

Gene3Di1.20.1540.10. 2 hits.
InterProiIPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR022241. Rhomboid_SP.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 3 hits.
PfamiPF01694. Rhomboid. 1 hit.
PF12595. Rhomboid_SP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
  3. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [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].
    Tissue: Placenta.
  7. "Homology of a 130-kb region enclosing the alpha-globin gene cluster, the alpha-locus controlling region, and two non-globin genes in human and mouse."
    Kielman M.F., Smits R., Devi T.S., Fodde R., Bernini L.F.
    Mamm. Genome 4:314-323(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 510-669, TISSUE SPECIFICITY.
    Tissue: Brain.
  8. "Characterization of a human rhomboid homolog, p100hRho/RHBDF1, which interacts with TGF-alpha family ligands."
    Nakagawa T., Guichard A., Castro C.P., Xiao Y., Rizen M., Zhang H.-Z., Hu D., Bang A., Helms J., Bier E., Derynck R.
    Dev. Dyn. 233:1315-1331(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TGFA AND HBEGF, GLYCOSYLATION AT ASN-583, MUTAGENESIS OF ASN-131; ASN-381 AND ASN-583, TISSUE SPECIFICITY.
  9. "Human rhomboid family-1 gene silencing causes apoptosis or autophagy to epithelial cancer cells and inhibits xenograft tumor growth."
    Yan Z., Zou H., Tian F., Grandis J.R., Mixson A.J., Lu P.Y., Li L.Y.
    Mol. Cancer Ther. 7:1355-1364(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Human rhomboid family-1 gene RHBDF1 participates in GPCR-mediated transactivation of EGFR growth signals in head and neck squamous cancer cells."
    Zou H., Thomas S.M., Yan Z.W., Grandis J.R., Vogt A., Li L.Y.
    FASEB J. 23:425-432(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling."
    Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.
    Cell 145:79-91(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGF.

Entry informationi

Entry nameiRHDF1_HUMAN
AccessioniPrimary (citable) accession number: Q96CC6
Secondary accession number(s): Q04842
, Q1W6H2, Q4TT59, Q96S34, Q9H6E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 8, 2016
This is version 102 of the entry and version 2 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 16
    Human chromosome 16: 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. Peptidase families
    Classification of peptidase families and list of entries
  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.