Annotations: 2AFF

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2affa_	All beta proteins	SMAD/FHA domain	SMAD/FHA domain	FHA domain	Antigen ki-67	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	FHA domain	8024600	4002605	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	SMAD/FHA domain-like	8036979	3000137	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	FHA	e2affA1	A: beta sandwiches	X: SMAD/FHA domain (From Topology)	H: SMAD/FHA domain (From Topology)	T: SMAD/FHA domain	F: FHA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.200.20	Mainly Beta	Sandwich	Tumour Suppressor Smad4		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00498	FHA domain (FHA)	FHA domain	-	Family
B	PF12196	FHA Ki67 binding domain of hNIFK (hNIFK_binding)	FHA Ki67 binding domain of hNIFK	This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with Pfam:PF00076. There are two conserved sequence motifs: TPVCTP and LERRKS. This domain is found on the human nucleolar pr ...	This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with Pfam:PF00076. There are two conserved sequence motifs: TPVCTP and LERRKS. This domain is found on the human nucleolar protein hNIFK. It binds to the fork-head-associated domain of human Ki67. High-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. This interaction is involved in cell cycle regulation.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Antigen KI-67	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding DNA binding nucleic acid binding RNA binding	cellular process cell cycle regulation of chromosome segregation regulation of biological process regulation of cellular process regulation of cell cycle process biological regulation regulation of cell cycle chromosome segregation cell cycle process mitotic nuclear division regulation of cellular component organization organelle fission regulation of mitotic nuclear division cellular process cell cycle regulation of chromosome segregation regulation of biological process regulation of cellular process regulation of cell cycle process biological regulation regulation of cell cycle chromosome segregation cell cycle process mitotic nuclear division regulation of cellular component organization organelle fission regulation of mitotic nuclear division regulation of organelle organization mitotic cell cycle cellular component organization regulation of mitotic cell cycle organelle organization nuclear division mitotic cell cycle process regulation of nuclear division cellular component organization or biogenesis cell population proliferation regulation of chromatin organization protein-containing complex organization protein-DNA complex organization chromatin organization	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle membrane chromosome nuclear body nucleoplasm
B	MKI67 FHA domain interacting nucleolar phosphoprotein	RNA binding binding organic cyclic compound binding nucleic acid binding	cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis ribonucleoprotein complex biogenesis cellular biosynthetic process RNA metabolic process rRNA processing nucleobase-containing compound metabolic process ribosome biogenesis organic substance metabolic process cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis ribonucleoprotein complex biogenesis cellular biosynthetic process RNA metabolic process rRNA processing nucleobase-containing compound metabolic process ribosome biogenesis organic substance metabolic process organic substance biosynthetic process RNA processing rRNA metabolic process cellular metabolic process primary metabolic process gene expression ribosomal large subunit biogenesis macromolecule biosynthetic process nucleic acid metabolic process maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) organic cyclic compound metabolic process biosynthetic process ncRNA metabolic process nucleic acid catabolic process metabolic process macromolecule metabolic process maturation of LSU-rRNA RNA biosynthetic process DNA-templated transcription nucleic acid biosynthetic process rRNA transcription nucleobase-containing compound biosynthetic process organic cyclic compound biosynthetic process	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle chromosome condensed nuclear chromosome nuclear chromosome condensed chromosome cytoplasm nucleoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR008984	SMAD/FHA domain superfamily	Homologous Superfamily
A	IPR000253	Forkhead-associated (FHA) domain	Domain
A	IPR012568	KI67R	Repeat
A	IPR029334	Protein phosphatase 1 binding domain	Domain
B	IPR021043	MKI67 FHA domain-interacting nucleolar phosphoprotein, FHA Ki67 binding	Domain
B	IPR000504	RNA recognition motif domain	Domain
B	IPR012677	Nucleotide-binding alpha-beta plait domain superfamily	Homologous Superfamily
B	IPR035979	RNA-binding domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P46013	psoriasis mesenchymal chondrosarcoma malignant colon neoplasm granular cell carcinoma adenocarcinoma lung adenocarcinoma breast carcinoma ovarian cancer peripheral nervous system disease colorectal cancer Copper-Overload Cirrhosis peripheral neuropathy tubular adenocarcinoma breast cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia psoriasis mesenchymal chondrosarcoma malignant colon neoplasm granular cell carcinoma adenocarcinoma lung adenocarcinoma breast carcinoma ovarian cancer peripheral nervous system disease colorectal cancer Copper-Overload Cirrhosis peripheral neuropathy tubular adenocarcinoma breast cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia ductal breast carcinoma in situ primitive neuroectodermal tumor pustulosis palmaris et plantaris hepatocellular carcinoma ulcerative colitis invasive ductal breast carcinoma malignant ependymoma atypical teratoid rhabdoid tumor colonic neoplasm pancreatic intraductal papillary-mucinous carcinoma cribriform carcinoma of breast endometriosis hepatitis spina bifida IgA glomerulonephritis large cell medulloblastoma lung cancer adrenal cortex carcinoma malignant glioma benign colon neoplasm non-small cell lung carcinoma ovarian neoplasm pancreatic intraductal papillary-mucinous neoplasm glioblastoma interstitial cystitis atopic eczema malignant mesothelioma malignant pancreatic neoplasm medulloblastoma osteosarcoma colorectal carcinoma pancreatic ductal adenocarcinoma cribriform carcinoma
B	Pharos: Q9BYG3	diabetes mellitus large cell medulloblastoma myopathy glioblastoma malignant glioma ovarian cancer juvenile dermatomyositis medulloblastoma primitive neuroectodermal tumor

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B	SEP	Parent Component: SER RESID: AA0037 PSI-MOD : O-phospho-L-serine MOD:00046
B	TPO	Parent Component: THR RESID: AA0037 , AA0038 PSI-MOD : O-phospho-L-serine MOD:00046 , O-phospho-L-threonine MOD:00047

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.